Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC...

73
PEPTIDES INTERNATIONAL Order Hotline 1-800-777-4779 502-266-8787 141 ENZYME INHIBITORS AND SUBSTRATES Peptidyl-NH O CH 3 O + H 2 O Peptide + N 2 H O O CH 3 Enzyme Reagents 1) Substrate stock solution: Vial, in DMSO at 10 mM 2) AMC stock solution: Content of vial (Code MCA-3099-v AMC), in DMSO at 1 mM 3) Buffer 4) Enzyme solution Procedure Choose the proper conditions for the measurement, such as substrate concentration and sensitivity setting, depending on the purpose of the experiment and the instrument available. Described here is one of the recommended procedures for the fluorometric method (initial-rate method). 1) Set a fluorescence spectrophotometer at λex = 380 nm and λem = 460 nm at 25 °C (1.0 Relative fluorescence unit at 10 -6 M of AMC) 2) Pipette 2940 µL of buffer and 30 µL of substrate stock solution into the cuvette 3) Incubate in the fluorescence spectrophotometer for 3-4 min (for temperature equilibration) 4) Add 30 µL of enzyme solution 5) Record the increase of the fluorescence intensity for 3-4 min 6) Calculate the amount of AMC released using the following equation The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig. 1a) or 2) photometrically at 370 nm (Fig. 1b). Assay Methods Using Peptidyl-MCA Substrates (1) Principle * Photometric measurement can be carried out by the same procedure as that of the fluorometric method using a UV spectrophotometer. Set the wavelength at 370 nm (ε 7700). Peptidyl-MCA AMC

Transcript of Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC...

Page 1: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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ENZYME INHIBITO

RS AND SuBSTRATES

Peptidyl-NH O

CH3

O + H2O Peptide + N2H OO

CH3

Enzyme

Reagents 1) Substrate stock solution: Vial, in DMSO at 10 mM 2) AMC stock solution: Content of vial (Code MCA-3099-v AMC), in DMSO at 1 mM 3) Buffer 4) Enzyme solution

Procedure Choose the proper conditions for the measurement, such as substrate concentration and sensitivity setting, depending on the purpose of the experiment and the instrument available. Described here is one of the recommended procedures for the fluorometric method (initial-rate method).

1) Set a fluorescence spectrophotometer at λex = 380 nm and λem = 460 nm at 25 °C (1.0 Relative fluorescence unit at 10-6 M of AMC)

2) Pipette 2940 µL of buffer and 30 µL of substrate stock solution into the cuvette 3) Incubate in the fluorescence spectrophotometer for 3-4 min (for temperature equilibration) 4) Add 30 µL of enzyme solution 5) Record the increase of the fluorescence intensity for 3-4 min 6) Calculate the amount of AMC released using the following equation

The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig. 1a) or 2) photometrically at 370 nm (Fig. 1b).

Assay Methods Using Peptidyl-MCA Substrates (1)Principle

* Photometric measurement can be carried out by the same procedure as that of the fluorometric method using a UV spectrophotometer. Set the wavelength at 370 nm (ε 7700).

Peptidyl-MCA AMC

Page 2: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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Wavelength (nm)

400 450 500 550

Ex = 350 nmEx = 380 nm

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Fig. 2 b Fluorescence Spectra of AMC (Product)

Wavelength (nm)

350 400 450 500 550

Ex = 330 nmEx = 340 nmEx= 350 nmEx = 360 nmEx= 370 nmEx = 380 nm

F ig. 2 a F luorescence Spectra of Peptidyl-MC A (Substrate)

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Assay Methods Using Peptidyl-MCA Substrates (2) (Measurement on an Auto-Fluorescence Spectrophotometer for Multiplate) Reagents 1) Substrate stock solution: Content of vial, in DMSO at 10 mM 2) AMC standard solution: Content of vial (Code MCA-3099-v AMC), in DMSO at 1 mM 3) Buffer 4) Enzyme solution

Instrument: Auto-fluorescence spectrophotometer Selection of filter: 380 nm, 390 nm or 355 nm filter will be recommended for measurement. In using 355 nm filter, observe caution for overlapping of fluorescence of the substrate itself.

Procedure

Choose the proper conditions for the measurement, such as substrate, enzyme concentration and other reaction conditions, depending on the purpose of the experiment.

1) Set the auto-fluorescence spectrophotometer at λex = 380 nm, λem = 460 nm at 25 °C (1.0 Relative fluorescence unit at 10-6 M of AMC)

2) Pipette 160 µL of buffer and 20 µL of substrate solution in well for final concentration of 100 µM 3) Incubate the plate in the fluorescence spectrophotometer for 3-4 min (for temperature equilibration) 4) Take the multiplate out and add 20 µL of enzyme solution in each well5) Mount the plate in the fluorescence spectrophotometer6) Record the increase in fluorescence intensity for 30 min with a premixing time of 3 sec7) Calculate the amount of released AMC

Page 3: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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RS AND SuBSTRATESAssay Methods Using Peptidyl-MCA Substrates (3)(Example for Caspase-7 using an Auto-fluorescence Spectrophotometer for Multiplate) Reagents 1) Substrate stock solution: Content of vial (Code SAP-3171-v Ac-DEVD-MCA), in DMSO at

10 mM 2) AMC standard solution: Content of vial (Code MCA-3099-v AMC), in DMSO at 1 mM 3) Buffer: ICE standard buffer (100 mM HEPES-KOH, pH 7.5, 10% sucrose (w/v), 0.1%

CHAPS (w/v) ,10 mM DTT, 0.1 mg/ml ovalbumin) 4) Enzyme solution: reconstitute Caspase-7 in buffer

Instrument: Fluoroskan Ascent (Labsystems) This instrument can be used for both initial rate assay and end point assay

Procedure a) Initial rate assay for 30 min at lex = 390 nm, lem = 460 nm b) End-point (30 min) assay at 5 different substrate

concentrations at lex = 355 nm or 380 nm, lem = 460 nm 1) Set a fluorescence spectrophotometer at lex =

390 nm ( or 380 nm, 355 nm), lem = 460 nm. Relative fluorescence is determined with 10-6 M of AMC at each condition

2) Substrate: Dilute the stock solution with the buffer (×10, ×20, ×40, ×80, ×160)

3) Caspase-7: Dissolve in buffer 4) Pipette 160 μl of buffer and 20 μl of substrate

solutions (1, 1/2, 1/4, 1/8, 1/16 mM) in each well 5) Incubate in the fluorescence spectrophotometer

for 3-4 min for temperature equilibration 6) Take the multiplate out and add 20 μl of enzyme

solution to each well 7) Mount the plate in the fluorescence spectrophotometer 8) Calculate the amount of released AMC

Results

Reaction Time

Substrate conc. (µM)

0 min

30 min

50

0

250

0 20 40 60 80 100 120

Fluo

resc

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(Em

460

nm

)

0

1000

1500

2000

0

3000

4000

3500

b2) End-point assay(Ex 355 nm)

XXX XX

Reaction Time (min)

Substrate conc. ( M)

X100

50

25

12.5

6.25

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50

0

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200

300

250

0 5 10 15 20 25 30 35

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60 n

m)

µ

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Reaction Time

Substrate conc. (µM)

0 min

30 min

100

50

0

150

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200

0 20 40 60 80 100 120

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Page 4: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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Wavelength (nm)

Fig. Fluorescence Spectra of MOCAc-Pro-Leu-Gly-OH

300 350 400 450

Ex SpectrumEm=393 nm

Em SpectrumEx=328 nm

Enzyme

100

50

0

60 sec

dF

Amount (pmol) of the reference compound released/min

=

= 3 X dF pmol/min

100 pmol X dF % X 3 ml1 ml X 100 % X 1 min

Time

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Reagents 1) Substrate stock solution: Code MOC-3163-v in DMSO at 2 • 10-4 M 2) MOCAc-Pro-Leu-Gly (reference compound) stock solution: Code MOC-3164-s in 10 ml of DMSO (2 • 10-5 M) 3) Buffer: 0.1 M-Tris • HCl, pH 7.5 containing 0.1 M NaCl, 10 mM CaCl2 and 0.05% Brij-35 4) Enzyme solution

Procedure Choose the proper conditions for the measurement, such as substrate concentration and sensitivity setting, depending on the purpose of the experiment and the instrument available. Described here is one of the recommended procedures for the fluorometric method (initial-rate method).

1) Set a fluorescence spectrophotometer at λex = 328 nm and λem = 393 nm at 25 °C (1.0 Relative fluorescence unit at 10-7 M of the reference compound) 2) Pipette 2900 µl of buffer and 50 µl of substrate stock solution into the cuvette 3) Incubate in the fluorescence spectrophotometer for 3-4 min (for temperature equilibration) 4) Add 50 µl of enzyme solution 5) Record the increase of the fluorescence intensity for 3-4 min 6) Calculate the amount of reference compound released using the following equation

Assay Method Using MOCAc/Dnp type Fluorescence-Quenching Substrates(Example using MOC-3163-v MOCAc-Pro-Leu-Gly-Leu-A2pr(Dnp)-Ala-Arg-NH2)

Principle The highly fluorescent (7-methoxycoumarin-4-yl)acetyl (MOCAc) group in the substrate such as Code MOC-3163-v is efficiently quenched by the 2,4-dinitrophenyl (Dnp) group. When metalloenzyme cleaves to the Gly-Leu bond, the fluorescence at λex = 328 nm and λem = 393 nm increases 190-fold.1

1) C.G. Knight, F. Willenbrock, and G. Murphy, FEBS Lett., 296, 263 (1992).

Page 5: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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Enzyme

100

50

0

60 sec

dF

Amount (pmol) of the cleaved substrate/min

=

= 2 X dF pmol/min

1000 pmol X dF % X 0.2 ml1 ml X 100 % X 1 min

Time

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= 1

nm

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(%)

1) D.M. Bickett, M.D. Green, J. Berman, M. Dezube, A.S. Howe, P.J. Brown, J.T. Roth, and G.M. McGeehan, Anal. Biochem., 212, 58 (1993). 2) S. Tanskul, K. Oda, H. Oyama, N. Noparatnaraporn, M. Tsunemi, and K. Takada, Biochem. Biophys. Res. Commun., 309, 547 (2003).

Reagents1) Substrate stock solution: 100 μM-10 μM in an appropriate solvent2) Reference compounds stock solution: a 1:1 mixture of two solutions of Code STD-3720-v and

STD-3721-v, each of which is reconstituted by dissolving peptides in 0.5 ml of DMSO at the concentration of 2 mM (1 mM, each reference compound)

3) Enzyme solution: an enzyme of interest in an appropriate buffer4) BufferProcedure Choose the proper conditions for the measurement, such as substrate concentration and sensitivity setting, depending on the purpose of the experiment and the instrument available. Described here is one of the recommended procedures for the fluorometric method (initial-rate method).

1) Set a fluorescence spectrometer at λex = 340 nm and λem = 440 nm (1.0 Relative fluorescence unit at 1 µM of the reference compound) 2) Pipette 160 µl of buffer and 2-20 µl of substrate solution in well for final concentration of 1 µM. 3) Incubate in the fluorescence spectrophotometer for 3-4 min for temperature equilibration 4) Add 20 µl of enzyme solution prepared at an appropriate concentration 5) Record the increase of the fluorescence intensity 6) Calculate the amount of the cleaved substrate using the following equation

Assay Method Using Nma/Dnp type Fluorescence-Quenching SubstratesPrincipleThe highly fluorescent 2-(N-methylamino)benzoyl (Nma) group in the substrates such as Code SFQ-3217-v and SFR-3224-v is efficiently quenched by the 2,4-dinitrophenyl (Dnp) group. When an enzyme of interest cleaves any peptide bond between Nma- and Dnp-containing amino acid residues in the substrate, the fluorescence at λex = 340 nm and λem = 440 nm increases in proportion to the release of the Nma fluorophore from the internal Dnp quencher.1,2

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Fig. Fluorescence Spectra of a 1:1 mixture of D-A2pr(Nma)-Gly and Ala-Phe-Pro-Lys(Dnp)-D-Arg-D-Arg

300 350 400 450 500

Ex SpectrumEm=440 nm

Em SpectrumEx=340 nm

Page 6: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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Amount (mmol) of pNA released/min = 1 mmol X dA X 3 ml 1 ml X 9.992 x 1 min

= 0.32 X dA mmol/minEnzyme dA

60 secpNA

1/992

0 M=0

.101 m

mol/m

l

Time0

0.5

1.0OD 405 nm

Assay Method Using Peptidyl-pNA SubstratesPrinciple A protease with limited specificity hydrolyzes a peptidyl-pNA substrate, releasing p-nitroaniline (pNA) as follows:

Peptidyl-pNA pNA

Fig. UV-Aborption Spectra

5

10

15

300 400 500Wavelength (nm)

405 nm

e X 103

Peptidyl-N- -NO2 Peptide + H2N - - NO2

Peptidyl-pNA pNA

H

The initial rate of increase in the pNA concentration can be monitored photometrically at 405 nm.

Reagents 1) Substrate stock solution: 10 mM (DMSO or distilled water) 2) Buffer 3) Enzyme solution

Procedure Choose the proper conditions for the measurement, such as substrate concentration and sensitivity setting, depending on the purpose of the experiment and the instrument available. Described here is one of the recommended procedures for the photometric method (initial-rate method).

1) Set a spectrophotometer at λ= 405 nm at 25˚ C (ε405 nm=9920)* 2) Pipette 2940 µl of buffer and 30 µl of substrate stock solution into the cuvette 3) Incubate in the spectrophotometer for 3-4 min (for temperature equilibration) 4) Add 30 µl of enzyme solution 5) Record the increase of the absorption intensity for 3-4 min 6) Calculate the amount of pNA released using the following equation

*R. Lottenberg, U. Christensen, C.M. Jackson, and P.L. Coleman, In, Proteolytic Enzymes Part C, Methods in Enzymolology, Vol. 80, (L. Lorand, ed.) Academic Press, New York, 1981, pp. 341-361.

Page 7: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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Enzyme Inhibitors

AminopeptidaseActinonin

3-[[1-[[2-(hydroxymethyl)-1-pyrrolidinyl]-carbonyl]-2-methylpropyl]-carbamoyl]-octanohydroxamic acid (M.W. 385.51) C19H35N3O5 [13434-13-4] Synthetic Product Inhibitor for Aminopeptidase M and Leucyl Aminopeptidase

IAC-4157-PI-20 °C

25 mg100 mg

CH3

O NHCH3

CH3 O

N

OH

O

NH

OH

IAC-4157-PI

3421140

Amastatin[(2S,3R)-3-Amino-2-hydroxy-5-methylhexanoyl]-l-valyl-l-valyl-l-aspartic acid(M.W. 474.55) C21H38N4O8 [67655-94-1] Synthetic Product

IAM-4095-v-20 °C

0.5 mgvial

O

NH

NH

NH

O

OH O

NH2

O

OH

O

OH

4095-v

80

Amastatin (Bulk)[(2S,3R)-3-Amino-2-hydroxy-5-methylhexanoyl]-l-valyl-l-valyl-l-aspartic acid(M.W. 474.55) C21H38N4O8 Synthetic Product

IAM-4095-20 °C

25 mg 1150

Inhibitor for Aminopeptidase A/PS and Leucyl Aminopeptidase

Arphamenine A(Sulfate Form)

IAR-4148-v-20 °C

0.5 mg vial

4148

NH

NH2NH

NH2

O

O

OH

40

(2R,5S)-5-Amino-8-guanidino-4-oxo-2-phenylmethyloctanoic acid (M.W. 320.39) C16H24N4O3 [96551-81-4] Microbial ProductH. Umezawa, T. Aoyagi, S. Ohuchi, A. Okuyama, H. Suda, T. Takita, M. Hamada, and T. Takeuchi, J. Antibiotics, 36, 1572 (1983). (Original with IC50) S. Ohuchi, H. Suda, H. Naganawa, T. Takita, T. Aoyagi, H. Umezawa, H. Nakamura, and Y. Iitaka, J. Antibiotics, 36, 1576 (1983). (Original; Chem. Structure) • This compound is distributed through Peptide Institute, Inc. under the technical and scientific advices of the Microbial Chemistry Research Foundation.

Arphamenine B(Sulfate Form)(2R, 5S)-5-Amino-8-Guanidino-4-Oxo-2-p-hydroxyphenylmethyloctanoic Acid (M.W. 336.39) C16H24N4O4 [103900-19-2] Microbial Product

IAR-4149-v-20 °C

0.5 mg vial

4149-v

NH

NH2NH

NH2

O

O

OH

OH

45

Page 8: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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148 Order Hotline 1-800-777-4779 502-266-8787

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PTID

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ATIO

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ENZY

ME

INHI

BITO

RS A

ND S

uBST

RATE

S

148 Order Hotline 1-800-777-4779 502-266-8787

Arphamenine B (Bulk)(2R, 5S)-5-Amino-8-Guanidino-4-Oxo-2-p-

IAR-4149-20 °C

25 mg100 mg

275

995hydroxyphenylmethyloctanoic Acid • hemisulfate monohydrate(M.W. 336.39 • 49.04 • 18.02) C16H24N4O4 • ½H2SO4 • H2O [144110-38-3] Microbial Product Inhibitor for Aminopeptidase B H. Umezawa, T. Aoyagi, S. Ohuchi, A. Okuyama, H. Suda, T. Takita, M. Hamada, and T. Takeuchi, J. Antibiotics, 36, 1572, (1983). (Original with IC50) S. Ohuchi, H. Suda, H. Naganawa, T. Takita, T. Aoyagi, H. Umezawa, H. Nakamura, and Y. Iitaka, J. Antibiotics, 36, 1576 (1983). (Original; Chem. Structure) • This compound is distributed through Peptide Institute, Inc. under the technical and scientific advices of the Microbial Chemistry Research Foundation.

Ebelactone A (Bulk)3,11-Dihydroxy-2,4,6,8,10,12-hexamethyl- 9-oxo-(E)-6-tetra-decen-3-olide (M.W. 338.48) C20H34O4 [76808-16-7] Microbial Product Inhibitor for Esterase, Lipase, and N-Formylmethionine Aminopeptidase

IEB-4155-20 °C

25 mg

4155

OO O OH

1150

H. Umezawa, T. Aoyagi, K. Uotani, M. Hamada, T. Takeuchi, and S. Takahashi, J. Antibiotics, 33, 1594 (1980). K. Uotani, H. Naganawa, S. Kondo, T. Aoyagi, and H. Umezawa, J. Antibiotics, 35, 1495 (1982). K. Uotani, H. Naganawa, T. Aoyagi, and H. Umezawa, J. Antibiotics., 35, 1670 (1982). • This compound is distributed exclusively through Peptide Institute, Inc. under the license of the Microbial Chemistry Research Foundation.

Leuhistin(2R,3S)-3-Amino-2-hydroxy-2-(1H-imidazol-4-ylmethyl)-5-methylhexanoic acid(M.W. 241.29) C11H19N3O3 [129085-76-3] Microbial Product Inhibitor for Aminopeptidase M

ILH-4249-v-20 °C

0.5 mg vial

4249-v

NH

N

NH2OH OH

O

45

T. Aoyagi, S. Yoshida, N. Matsuda, T. Ikeda, N. Hamada, and T. Takeuchi, J. Antibiotics, 44, 573 (1991). (Original; IC50) S. Yoshida, H. Nagasawa, T. Aoyagi, T. Takeuchi, Y. Takeuchi, Y. Kodama, J. Antibiotics, 44, 579 (1991). (Original; Chem. Structure) S. Yoshida, T. Aoyagi, and T. Takeuchi, J. Antibiotics, 44, 683 (1991). (Original; Biosynthesis) • This compound is distributed exclusively through Peptide Institute, Inc. under the license of the Microbial Chemistry Research Foundation.

Phebestin (2S,3R)-3-Amino-2-hydroxy-4-phenylbutanoyl-l-valyl-l-phenylalanine (M.W. 441.53) C24H31N3O5 Synthetic Product Inhibitor for Aminopeptidase N

IPH-4342-v-20 °C

5 mg vial

4342-v

NH2

OHNH

O

O

NH

O

OH

115

M. Nagai, F. Kojima, H. Naganawa, M. Hamada, T. Aoyagi, and T. Takeuchi, J. Antibiotics, 50, 82 (1997). (Original) • This compound is distributed exclusively through Peptide Institute, Inc. under the license of the Microbial Chemistry Research Foundation.

Ubenimex (Bestatin) (Bulk)[(2S,3R)-3-Amino-2-hydroxy-4-Phenyl-Butanoyl]-l-Leu (M.W. 308.38) C16H24N2O4 [58970-76-6]H. Umezawa, T. Aoyagi, H. Suda, M. Hamada, and T. Takeuchi, J. Antibiotics, 29, 97 (1976).

IBS-4093-PI-20 °C

25 mg100 mg

O

NH

CH3

CH3

COOHNH

OH

IBS-4093-PI

120360

Page 9: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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Angiotensin I Converting Enzyme InhibitorsBradykinin-Potentiator B

Pyr-Gly-Leu-Pro-Pro-Arg-Pro-Lys-lle-Pro-Pro (M.W. 1182.4) C56H91N15O13 [30892-86-5] Synthetic Product

IAB-4009-v-20 °C

0.5 mgvial

35

Bradykinin-Potentiator B (Bulk)Pyr-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-Pro-Pro • AcOH • 4H2O (M.W. 1182.4 • 60.05 • 72.06) C56H91N15O13 • CH3COOH • 4H2O Synthetic Product

IAB-4009-20 °C

25 mg 539

Inhibitor for Peptidyl-Dipeptidase A, Kininase II, and ACE (Angiotensin I Converting Enzyme)H. Kato and T. Sazuki, Biochemistry, 10, 972 (1971). (Original)

Bradykinin-Potentiator C Pyr-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-Pro-Pro (M.W. 1052.2) C51H77N11O13 [30953-20-9] Synthetic Product

IAC-4010-v-20 °C

0.5 mg vial

30

Cpp-AAF-pAbN-[(RS)-1-Carboxy-3-phenyl-propyl]-Ala-Ala-Phe-4-Abz-OH (M.W. 89.67) C32H37N4O7 Inhibitor of ACEM.Orlowski, et al., Biochemistry, 27, 597 (1988)D.T.O.Martins, et al., Br. J. Pharmacol., 103, 1851 (1991)C.H.Williams, et al.., Biochem. J., 294, 681 (1993)R.Yamin, et al., J. Biol. Chem., 274, 18777 (1999)

IAP-3754-PI-20 °C

1 mg5 mg

105420

Des-Pro2-BradykininArg-Pro-Gly-Phe-Ser-Pro-Phe-Arg (M.W. 963.09) C45H66N14O10 [80943-05-1] Synthetic Product

IBK-4097-v-20 °C

0.5 mg vial

35

Des-Pro2-Bradykinin (Bulk)Arg-Pro-Gly-Phe-Ser-Pro-Phe-Arg • 2AcOH • 3H2O(M.W. 963.09 • 120.10 • 54.05) C45H66N14O10 • 2CH3COOH • 3H2O Synthetic Product

IBK-4097-20 °C

25 mg

520

Inhibitor for Peptidyl-Dipeptidase A, Kininase II, and ACE (Angiotensin I Converting Enzyme)M. Naruse, S. Tamanami, K. Shuto, S. Sakakibara, and T. Kimura, Chem. Pharm. Bull., 29, 3369 (1981). (Original)

Foroxymithine(3S,6S)-3-(3-{N-[N-(Na-Acetyl-Nd-Formyl-Nd-hydroxy-l-Ornithyl)-l-Seryl]-N-(Hydroxy)Amino}Propyl)-6-[3-(N-Formyl-N-Hydroxyamino)Propyl]-2,5-Piperazinedione (M.W. 575.57) C22H37N7O11 [100157-28-6] Microbial Product

IFR-4190-v-20 °C

0.5 mg vial

75

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PEPT

IDES

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150 Order Hotline 1-800-777-4779 502-266-8787

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ES IN

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ATIO

NAL

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ME

INHI

BITO

RS A

ND S

uBST

RATE

S

150 Order Hotline 1-800-777-4779 502-266-8787

Foroxymithine (Bulk)(3S,6S)-3-(3-{N-[N-(N a-Acetyl-N d-Formyl-N d-hydroxy-l-Ornithyl)-l-Seryl]-N-(Hydroxy)Amino}Propyl)-6-[3-(N-Formyl-N-Hydroxyamino)Propyl]-2,5-Piperazinedione (M.W. 575.57) C22H37N7O11 [100157-28-6] Microbial ProductInhibitor for ACE (Angiotensin I Converting Enzyme)H. Umezawa, T. Aoyagi, K. Ogawa, T. Obata, H. Iinuma, H. Naganawa, M. Hamada, and T. Takeuchi, J. Antibiotics, 38, 1813 (1985). (Original; Chem. Structure with IC50)

IFR-4190-20 °C

4190-v

OH

O

NH

O

NH

O

N

N

H O

OH

OH

NH

O

O

NH

N

O H

OH

25 mg 1050

d-Aspartyl Endopeptidase InhibitorBz-Arg-His-d-Asp-CH2Cl

(Trifluoroacetate Form)[Bz-RHd-CMK](Benzoyl-l-arginyl-l-histidyl-d-aspart-1-yl) chloromethane (M.W. 563.01) C24H31N8O6Cl Synthetic Product Selective Inhibitor for D-Aspartyl EndopeptidaseT. Kinouchi, S. Ishiura, Y. Mabuchi, Y. Urakami-Manaka, H. Nishio, Y. Nishiuchi, M. Tsunemi, K. Takada, M. Watanabe, M. Ikeda, H. Matsui, S. Tomioka, H. Kawahara, T. Hamamoto, K. Suzuki, and Y. Kagawa, Biochem. Biophys. Res. Commun., 314, 730 (2004). • This compound is produced by Peptide Institute, Inc. under the license of Japan Science and Technology Agency.

ICL-3223-v-20 °C

5 mgvial

NHN

NH

O

NH

NH NH2

NH

ONH

O

OH

O

OCI

3223-v

240

Bestatin See Code IBS-4093-PI Ubenimex on page 152.BQ-123, BQ-610, and BQ-788 See pages 166.CA-074 See Code IEC-4322-v on page 159.CA-074 Me See Code IEC-4323-v on page 159.

Calpain InhibitorsAc-Leu-Leu-Nle-H (aldehyde)

ALLN, MG 101Acetyl-l-leucyl-l-leucyl-l-norleucinal (M.W. 383.54) C20H37N3O4 Inhibitor for Calpain I and Proteasome

IAL-3671-PI-20 °C

5 mg

O

NH

O

NH

O

NH

O

H

3671-PI

46

T. Sasaki, M. Kishi, M. Saito, T. Tanaka, N. Higuchi, E. Kominami, N. Katunuma, and T. Murachi, J. Enzyme Inhib., 3, 195 (1990).

Ac-Leu-Leu-Met-H (aldehyde)ALLMAcetyl-l-leucyl-l-leucyl-l-methioninal (M.W. 401.57) C19H35N3O4S Inhibitor for Calpain II and Proteasome

T. Sasaki, M. Kishi, M. Saito, T. Tanaka, N. Higuchi, E. Kominami, N. Katunuma, and T. Murachi, J. Enzyme Inhib., 3, 195 (1990).

IAL-3678-PI-20 °C

5 mg

O

NH

O

NH

O

NH

S

H

O

3678-PI

46

E-64-c and E-64-d See page 160.

Page 11: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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Order Hotline 1-800-777-4779 502-266-8787 151

ENZYME INHIBITO

RS AND SuBSTRATES

Z-Leu-Leu-H (aldehyde)Benzyloxycarbonyl-l-leucyl-l-leucinal(M.W. 362.46) C20H30N2O4 Synthetic Product Inhibitor for Calpain*

IZL-3178-v-20 °C

5 mgvial

3178-v

O

O

NH

O

NH

O

H

50

Y. Saito, S. Tsubuki, H. Ito, and S. Kawashima, Neurosci. Lett., 120, 1 (1990). S. Tsubuki, Y. Saito, M. Tomioka, H. Ito, and S. Kawashima, J. Biochem., 119, 572 (1996). *This compound does not inhibit Proteasome at the level of 10-6 M concentration.

Caspase InhibitorsAc-Asp-Asn-Leu-Asp-H (aldehyde)

Acetyl-l-aspartyl-l-asparaginyl-l-leucyl-l-aspart-1-al (M.W. 501.49) C20H31N5O10 Synthetic Product Selective Inhibitor for Caspase-3 Designed by in silico Screening System

ICA-3221-v-20 °C

5 mgvial

O

NH

O

OH

O

NH

O

NH

O

O

NH

O

OHH

O

NH2

3221-v

240

A. Yoshimori, R. Takasawa, and S. Tanuma, BMC Pharmacol., 4, 7 (2004). A. Yoshimori, R. Takasawa, and S. Tanuma, Bio. Pharm. Bull., 27, 968 (2004). • This compound is produced by Peptide Institute, Inc. under the license of the Institute for Theoretical Medicine, Inc.

Ac-Asp-Gln-Thr-Asp-H (aldehyde)Acetyl-l-aspartyl-l-glutaminyl-l-threonyl-l-aspart-1-al (M.W. 503.46) C19H29N5O11 Synthetic Product Inhibitor for Caspase-7/3 (Deduced from the Cleavage Site of Focal Adhesion Kinase and Gelsolin)

ICA-3194-v-20 °C

5 mgvial

NH

OH

O

O

HO

O

NH

O

O

NHOH O

NH

NH2O

OH

3194-v

290

L.-P. Wen, J.A. Fahrni, S. Troie, J.-L. Guan, K. Orth, and G.D. Rosen, J. Biol. Chem., 272, 26056 (1997). S. Kothakota, T. Azuma, C. Reinhard, A. Klippel, J. Tang, K. Chu, T.J. McGarry, M.W. Kirschner, K. Koths, D.J. Kwiatkowski, and L.T. Williams, Science, 278, 294 (1997).

Ac-Asp-Glu-Val-Asp-H (aldehyde)Acetyl-l-aspartyl-l-glutamyl-l-valyl-l-aspart-1-al (M.W. 502.47) C20H30N4O11 [184179-08-6] Synthetic Product Inhibitor for Caspase-3/7/8D.W. Nicholson, A. Ali, N.A. Thornberry, J.P. Vaillancourt, C.K. Ding, M. Gallant, Y. Gareau, P.R. Griffin, M. Labelle, Y.A. Lazebnik, N.A. Munday, S.M. Raju, M.E. Smulson, T.-T. Yamin, V.L. Yu, and D.K. Miller, Nature, 376, 37 (1995).

IAP-3172-v-20 °C

5 mgvial

NH

OH

O

O

HO

NH

O

NH

O

OH

O

NH

O

OHO

3172-v

225

M. Enari, R.V. Talanian, W.W. Wong, and S. Nagata, Nature, 380, 723 (1996). N.A. Thornberry, T.A. Rano, E.P. Peterson, D.M. Rasper, T. Timkey, M. Garcia-Calvo, V.M. Houtzager, P.A. Nordstrom, S. Roy, J.P. Vaillancourt, K.T. Chapman, and D.W. Nicholson, J. Biol. Chem., 272, 17907 (1997).

Ac-Asp-Met-Gln-Asp-H (aldehyde)Acetyl-l-aspartyl-l-methionyl-l-glutaminyl-l-aspart-1-al (M.W. 533.55) C20H31N5O10S [259199-63-8] Synthetic Product Inhibitor for Caspase-3

ICA-3192-v-20 °C

5 mg vial

3192-v

NH

OH

O

O

HO

NH

O

NH

O

OH

O

NH

O

S

O NH2

350

A. Takahashi, H. Hirata, S. Yonehara, Y. Imai, K.-K. Lee, R.W. Moyer, P.C. Turner, P.W. Mesner, T. Okazaki, H. Sawai, S. Kishi, K. Yamamoto, M. Okuma, and M. Sasada, Oncogene, 14, 2741 (1997).H. Hirata, A. Takahashi, S. Kobayashi, S. Yonehara, H. Sawai, T. Okazaki, K. Yamamoto, and M. Sasada, J. Exp. Med., 187, 587 (1998).

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152 Order Hotline 1-800-777-4779 502-266-8787

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S

152 Order Hotline 1-800-777-4779 502-266-8787

Ac-Ile-Glu-Thr-Asp-H (aldehyde)Acetyl-l-isoleucyl-l-glutamyl-l-threonyl-l-aspart-1-al (M.W. 502.52) C21H34N4O10 [191338-86-0] Synthetic Product Inhibitor for Caspase-8/6 and Granzyme B (Deduced from the Cleavage Site of Procaspase-3)Z. Han, E.A. Hendrickson, T. A. Bremner, and J.H. Wyche, J. Biol. Chem., 272, 13432 (1997). M. Garcia-Calvo, E.P. Peterson, B. Leiting, R. Ruel, D.W. Nicholson, and N.A. Thornberry, J. Biol. Chem., 273, 32608 (1998).

ICA-3196-v-20 °C

3196-v

NH

OH

O

O

HO

NH

O

NH

O

NH

O

OH

OH

O

5 mg vial

230

Ac-Leu-Glu-His-Asp-H (aldehyde)(Trifluoroacetate Form) Acetyl-l-leucyl-l-glutamyl-l-histidyl-l-aspart-1-al (M.W. 538.55) C23H34N6O9 Synthetic Product Inhibitor for Caspase-9N.A. Thornberry, T.A. Rano, E.P. Peterson, D.M. Rasper, T. Timkey, M. Garcia-Calvo, V.M. Houtzager, P.A. Nordstrom, S. Roy, J.P. Vaillancourt, K.T. Chapman, and D.W. Nicholson, J. Biol. Chem., 272, 17907 (1997).

ICA-3199-v -20 °C

5 mg vial

NH

OH

O

O

HO

NH

O

NH

O

NH

O

OHO

NHN

3199-v

290

Ac-Trp-Glu-His-Asp-H (aldehyde)Acetyl-l-tryptophyl-l-glutamyl-l-histidyl-l-aspart-1-al (M.W. 611.60) C28H33N7O9 [189275-71-6] Synthetic Product Inhibitor for Caspase-1T.A. Rano, T. Timkey, E.P. Peterson, J. Rotonda, D.W. Nicholson, J.W. Becker, K.T. Chapman, and N.A. Thornberry, Chem. Biol., 4, 149 (1997). M. Garcia-Calvo, E.P. Peterson, B. Leiting, R. Ruel, D.W. Nicholson, and N.A. Thornberry, J. Biol. Chem., 273, 32608 (1998).

ICA-3187-v-20 °C

5 mg vial

NH

NH

OH

O

O

HO

NH

O

NH

O

NH

O

OHO

NHN

3187-v

230

Ac-Tyr-Val-Ala-Asp-CH2Cl(Acetyl-l-tyrosyl-l-valyl-l-alanyl-l-aspart-1-yl)chloromethane (M.W. 540.99) C24H33N4O8Cl [178603-78-6] Synthetic Product Inhibitor for CaspasesY.A. Lazebnik, S.H. Kaufmann, S. Desnoyers, G.G. Poirier, and W.C. Earnshaw, Nature, 371, 346 (1994). M. Enari, H. Hug, and S. Nagata, Nature, 375, 78 (1995).

ICL-3180-v -20 °C

5 mg vial

3180-v

O

NH

NH

ONH

O

OH

NH

O

O

OH

CI

O

230

C.E. Milligan, D. Prevette, H. Yaginuma, S. Homma, C. Cardwell, L.C. Fritz, K.J. Tomaselli, R.W. Oppenheim, and L.M. Schwartz, Neuron, 15, 385 (1995). E. Fujita, T. Mukasa, T. Tsukahara, K. Arahata, S. Omura, and T. Momoi, Biochem. Biophys. Res. Commun., 224, 74 (1996).

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PRODUCT CODE QTy PRICE PEPTIDES INTERNATIO

NAL

Order Hotline 1-800-777-4779 502-266-8787 153

ENZYME INHIBITO

RS AND SuBSTRATES

Ac-Tyr-Val-Ala-Asp-H (aldehyde)Acetyl-l-tyrosyl-l-valyl-l-alanyl-l-aspart-1-al (M.W. 492.52) C23H32N4O8 [143313-51-3] Synthetic Product Inhibitor for Caspase-1N.A. Thornberry, H.G. Bull, J.R. Calaycay, K.T. Chapman, A.D. Howard, M.J. Kostura, D.K. Miller, S.M. Molineaux, J.R. Weidner, J. Aunins, K.O. Elliston, J.M. Ayala, F.J. Casano, J. Chin, G.J.-F. Ding, L.A. Egger, E.P. Gaffney, G. Limjuco, O.C. Palyha, S.M. Raju, A.M. Rolando, J.P. Salley,

IAT-3165-v-20 °C

3165-vO

NH

NH

ONH

O

OH

NH

O

O

OH

H

O

5 mg vial

225

T.-T. Yamin, T.D. Lee, J.E. Shively, M. MacCross, R.A. Mumford, J.A. Schmidt, and M.J. Tocci, Nature, 356, 768 (1992). S.M. Molineaux, F.J. Casano, A.M. Rolando, E.P. Peterson, G. Limjuco, J. Chin, P.R. Griffin, J.R. Calaycay, G.J.-F. Ding, T.-T. Yamin, O.C. Palyha, S. Luell, D. Fletcher, D.K. Miller, A.D. Howard, N.A. Thornberry, and M.J. Kostura, Proc. Natl. Acad. Sci. USA, 90, 1809 (1993). M. Enari, R.V. Talanian, W.W. Wong, and S. Nagata, Nature, 380, 723 (1996). M. Garcia-Calvo, E.P. Peterson, B. Leiting, R. Ruel, D.W. Nicholson, and N.A. Thornberry, J. Biol. Chem., 273, 32608 (1998).

Ac-Tyr-Val-Lys-Asp-H (aldehyde)Acetyl-l-tyrosyl-l-valyl-l-lysyl-l-aspart-1-al (M.W. 549.62) C26H39N5O8 Synthetic Product Inhibitor for Caspase-1, Affinity Ligand for Caspase-1N.A. Thornberry, H.G. Bull, J.R. Calaycay, K.T. Chapman, A.D. Howard, M.J. Kostura, D.K. Miller, S.M. Molineaux, J.R. Weidner, J. Aunins, K.O. Elliston, J.M. Ayala, F.J. Casano, J. Chin, G.J.-F. Ding, L.A. Egger, E.P. Gaffney, G. Limjuco, O.C. Palyha, S.M. Raju, A.M. Rolando, J.P. Salley, T.-T. Yamin,

IAT-3166-v-20 °C

3166-v O

NH

NH

ONH

O

OH

NH

O

O

OH

H

NH2

O

5 mgvial

225

T.D. Lee, J.E. Shively, M. MacCross, R.A. Mumford, J.A. Schmidt, and M.J. Tocci, Nature, 356, 768 (1992).T.L. Graybill, R.E. Dolle, C.T. Helaszek, R.E. Miller, and M.A. Ator, Int. J. Pept. Protein Res., 44, 173 (1994).

Ac-Val-Asp-Val-Ala-Asp-H (aldehyde)Acetyl-l-valyl-l-aspartyl-l-valyl-l-alanyl-l-aspart-1-al (M.W. 543.57) C23H37N5O10 [194022-51-0] Synthetic Product Inhibitor for Caspase-2R.V. Talanian, C. Quinlan, S. Trautz, M.C. Hackett, J.A. Mankovich, D. Banach, T. Ghayur, K.D. Brady, and W.W. Wong, J. Biol. Chem., 272, 9677 (1997).

IVD-3204-v-20 °C

5 mgvial

3204-v

O

NH

NH

O

NH

NH

NH

O

O

H

O

O

OH

OH

O

O

350

Ac-Val-Glu-Ile-Asp-H (aldehyde)Acetyl-l-valyl-l-glutamyl-l-isoleucyl-l-aspart-1-al (M.W. 500.54) C22H36N4O9 Synthetic Product Inhibitor for Caspase-6 H. Hirata, A. Takahashi, S. Kobayashi, S. Yonehara, H. Sawai, T. Okazaki, K. Yamamoto, and M. Sasada, J. Exp. Med., 187, 587 (1998).

IVA-3182-v -20 °C

5 mg vial

3182-v

O

NH

NH

O

O

O OH

NH

OH

HO

NH

O

O

250

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154 Order Hotline 1-800-777-4779 502-266-8787

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154 Order Hotline 1-800-777-4779 502-266-8787

Biotinyl-Asp-Glu-Val-Asp-H (aldehyde)Biotinyl-l-aspartyl-l-glutamyl-l-valyl-l-aspart-1-al (M.W. 686.73) C28H42N6O12S [178603-73-1] Synthetic Product Inhibitor for Caspase-3/7/8D.W. Nicholson, A. Ali, N.A. Thornberry, J.P. Vaillancort, C.K. Ding, M. Gallant, Y. Gareau, P.R. Griffin, M. Labelle, Y.A. Lazebnik, N.A. Munday, S.M. Raju, M.E. Smulson,T.-T. Yamin, V.L. Yu, and D.K. Miller, Nature, 376, 37 (1995).

IBA-3173-v -20 °C

1 mg vial

O

NH

NH

S

O

NH

O

OH

O

NH

O OH

O

NH

O

NH

O

OHH

O

3173-v

115

Z-Asp-CH2-DCB(Benzyloxycarbonyl-l-aspart-1-yl)[(2,6-dichlorobenzoyl)oxy]methane(M.W. 454.26) C20H17NO7Cl2 [153088-73-4] Synthetic Product Inhibitor for Caspases

ICE-3174-v-20 °C

5 mg vial

O NH

O

O

O

O

O

OH

CI

CI

3174-v

225

R.E. Dolle, D. Hoyer, C.V.C. Prasad, S.J. Schmidt, C.T. Helaszek, R.E. Miller, and M.A. Ator, J. Med. Chem., 37, 563 (1994). T. Mashima, M. Naito, S. Kataoka, H. Kawai, and T. Tsuruo, Biochem. Biophys. Res. Commun., 209, 907 (1995).

Z-Glu-Lys(Biotinyl)-Asp-CH2-DMB[Benzyloxycarbonyl-l-glutamyl-(Ne-biotinyl-l-lysyl)-l-aspart-1-yl]-[(2,6-dimethylbenzoyl)oxy]methane (M.W. 897.00) C43H56N6O13S Synthetic Product Affinity Ligand for Caspases

L.M. Martins, T. Kottke, P.W. Mesner, G.S. Basi, S. Shinha, N. Frigon, Jr., E. Tatar, J.S. Tung, K. Bryant, A. Takahashi, P.A. Svingen, B.J. Madden, D.J. McCormick, W.C. Earnshaw, and S.H. Kaufmann, J. Biol. Chem., 272, 7421 (1997). L.M. Martins, P.W. Mesner, T.J. Kottke, G.S. Basi, S. Sinha, J.S. Tung, P.A. Svingen, B.J. Madden, A. Takahashi, D.J. McCormick, W.C. Earnshaw, and S. H. Kaufmann, Blood, 90, 4283 (1997).

ICA-3189-v -20 °C

1 mg vial

3189-v

O NH

NH

O

O

O OH

NH

O

O

O

OH

O

O

NH

O

S

N

NH

OH

115

Z-Val-Ala-Asp(OMe)-CH2F[Z-VAD-FMK]{Benzyloxycarbonyl-l-valyl-l-alanyl-[(2S)-2-amino-3-(methoxycarbonyl)propionyl]} fluoromethane (M.W. 467.49) C22H30N3O7F Synthetic Product Inhibitor for Caspases

ICA-3188-v-20 °C

1 mg vial

O NH

O

O

NH

NH

O

O

OF

OCH3

3188-v

130

E.A. Slee, H. Zhu, S.C. Chow, M. MacFarlane, D.W. Nicholson, and G.M. Cohen, Biochem. J., 315, 21 (1996). H. Zhu, H.O. Fearnhead, and G.M. Cohen, FEBS Lett., 374, 303 (1995).

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Order Hotline 1-800-777-4779 502-266-8787 155

ENZYME INHIBITO

RS AND SuBSTRATES

Cathepsin and Thiol Protease InhibitorsAntipain

(Hydrochloride Form)[(S)-1-Carboxy-2-Phenylethyl]- Carbamoyl-l-arginyl-l-valylargininal (M.W. 604.70) C27H44N10O6 [37691-11-5] Microbial Product

IAP-4062-v-20 °C

0.5 mg vial

NH

NH NH2

OH O

NH

O

NH

NH

NH NH2

O

NH

O

NH

O

H

4062-v

45

Antipain (Bulk)[(S)-1-Carboxy-2-phenylethyl]-carbamoyl-l-arginyl-l-valylargininal • monohydrochloride dihydrate (M.W. 604.70 • 36.46 • 36.03) C27H44N10O6 • HCI • 2H2O Microbial Product Inhibitor for Trypsin, u-PA, Papain, and Cathepsin A/B

IAP-4062-20 °C

25 mg100 mg

120

315

H. Suda, T. Aoyagi, M. Hamada, T. Takeuchi, and H. Umezawa, J. Antibiotics, 25, 263 (1972). (Original) S. Umezawa, K. Tatsuta, K. Fujimoto, T. Tsuchiya, H. Umezawa, and H. Naganawa, J. Antibiotics, 25, 267 (1972). (Original; Chem. Structure) J. Chau, J. Biol. Chem., 258, 4434 (1983). (Inhibitory Activity) • This compound is distributed through Peptide Institute, Inc. under the technical and scientific advices of the Microbial

Chemistry Research Foundation.

CA-074[(2 S, 3S)-3-Propylcarbamoyloxirane-2-carbonyl]-l-isoleucyl-l-proline methyl ester(M.W. 383.44) C18H29N3O6 [134448-10-5] Synthetic Product Inhibitor for Cathepsin BM. Murata, S. Miyashita, C. Yokoo, M. Tamai, K. Hanada, K. Hatayama, T. Towatari, T. Nikawa, and N. Katunuma, FEBS Lett., 280, 307 (1991).

IEC-4322-v -20 °C

5 mg vial

ONH

O

O

NH

O

N

OOH

4322-v

170

(Original; IC50) T. Towatari, T. Nikawa, M. Murata, C. Yokoo, M. Tamai, K. Hanada, and N. Katunuma, FEBS Lett., 280, 311 (1991). (Original; Pharmacol.) T. Inubushi, H. Kakegawa, Y. Kishino, and N. Katunuma, J. Biochem., 116, 282 (1994). (Biochem.)

CA-074 Me[(2 S, 3S)-3-Propylcarbamoyloxirane-2-carbonyl]-l-isoleucyl-l-proline methyl ester (M.W. 397.47) C19H31N3O6 [147859-80-1] Synthetic Product Proinhibitor for Intracellular Cathepsin B Membrane Permeable Analog of CA-074

IEC-4323-v-20 °C

5 mg vial

4323-v

ONH

O

O

NH

O

N

OO

170

D.J. Buttle, M. Murata, C.G. Knight, and A.J. Barrett, Arch. Biochem. Biophys., 299, 377 (1992). (Original) • This compound is distributed through Peptide Institute, Inc. under the license of Taisho Pharmaceutical Co., Ltd.

Page 16: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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156 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT CODE QTy PRICE PE

PTID

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ATIO

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ENZY

ME

INHI

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RS A

ND S

uBST

RATE

S

156 Order Hotline 1-800-777-4779 502-266-8787

E-64[(2 S, 3S)-3-Carboxyoxiran-2-carbonyl]-l-leucine (4-guanidi-nobutyl)amide (M.W. 357.41) C15H27N5O5 • ½H2O [66701-25-5] Synthetic Product

IES-4096-v-20 °C

0.5 mg vial

45

E-64 (Bulk)[(2 S, 3S)-3-Carboxyoxiran-2-carbonyl]-l-leucine (4-guanidi-nobutyl)amide hemihydrate (M.W. 357.41 • 9.01) C15H27N5O5 • ½H2O [66701-25-5] Synthetic Product Inhibitor fof Thiol ProteasesK. Hanada, M. Tamai, M. Yamagishi, S. Ohmura, J. Sawada, and I. Tanaka, Agric. Biol. Chem., 42, 523 (1978). (Original) K. Hanada, M. Tamai, S. Ohmura, J. Sawada, T. Seki, and I. Tanaka, Agric. Biol. Chem., 42, 529 (1978). (Structure & Chem. Synthesis) Y. Shoji-Kasai, M. Senshu, S. Iwashita, and K. Imahori, Proc. Natl. Acad. Sci. USA, 85, 146 (1988). (Pharmacol.)

IES-4096-20 °C

25 mg100 mg

4096-v

OOH

O

O

NH

O

NH

NH

NH

NH2

150350

E-64-c[(2 S, 3S)-3-Carboxyoxirane-2-carbonyl]-l-leucine (3-meth-ylbutyl)amide (M.W. 314.38) C15H26N2O5 [76684-89-4] Synthetic Product Inhibitor for Thiol Protease (Cathepsin B/H/L and Calpain)

IEC-4320-v-20 °C

5 mg vial

4320-v

OOH

O

O

NH

O

NH

115

S. Hashida, T. Towatari, E. Kominami, and N. Katunuma, J. Biochem, 88, 1805 (1980). M. Tamai, K. Hanada, T. Adachi, K. Oguma, K. Kashiwagi, S. Omura, and M. Ohzeki, J. Biochem, 90, 255 (1981). A.J. Barrett, A.A. Kembhavi, M.A. Brown, H. Kirschke, C.G. Knight, M. Tamai, and K. Hanada, Biochem. J., 201, 189 (1982). K. Suzuki, J. Biochem., 93, 1305 (1983).

E-64-d[(2 S, 3S)-3-Ethoxycarbonyloxirane-2-carbonyl]-l-leucine (3-methylbutyl)amide (M.W. 342.43) C17H30N2O5 [88321-09-9] Synthetic Product Inhibitor for Thiol Protease (Cathepsin B/H/L and Calpain) Membrane Permeable Analog of E-64-c

IED-4321-v-20 °C

5 mg vial

4321-v

O

O

O

NH

O

NH

O

115

M. Tamai, K. Matsumoto, S. Omura, I. Koyama, Y. Ozawa, and K. Hanada, J. Pharmacobio-Dyn., 9, 672 (1986). (Original) M. Tamai, C. Yokoo, M. Murata, K. Oguma, K. Sota, E. Sato, and Y. Kanaoka, Chem. Pharm. Bull., 35, 1098 (1987). (Chem. Synthesis & Biochem.)

Leupeptin(Sulfate Form)Acetyl-l-leucyl-l-leucyl-l-argininal (M.W. 426.55) C20H38N6O4 [55123-66-5] Microbial Product

ILP-4041-v-20 °C

0.5 mg vial

4041-v

O

NH

O

NH

NH

O

NH

NH HN2

O

H

40

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Order Hotline 1-800-777-4779 502-266-8787 157

ENZYME INHIBITO

RS AND SuBSTRATES

Leupeptin (Bulk)Acetyl-l-leucyl-l-leucyl-l-argininal hemisulfate monohydrate (M.W. 426.55 • 49.04 • 18.02) C20H38N6O4 • ½H2O [103476-89-7] Microbial Product Inhibitor for Trypsin, Plasmin, Papain, and Cathepsin B

ILP-4041-20 °C

25 mg100 mg

1 g

70

170

1247

S. Kondo, K. Kawamura, J. Iwanaga, M. Hamada, T. Aoyagi, K. Maeda, T. Takeuchi, and H. Umezawa, Chem. Pharm. Bull., 17, 1896 (1969). (Biological Activity) T. Aoyagi, T. Takeuchi, A. Matsuzaki, K. Kawamura, S. Kondo, M. Hamada, K. Maeda, and H. Umezawa, J. Antibiotics, 22, 283 (1969). (Original) T. Aoyagi, S. Miyata, M. Nanbo, F. Kojima, M. Matsuzaki, M. Ishizuka, T. Takeuchi, and H. Umezawa, J. Antibiotics, 22, 558 (1969). (Biological Activity) R.M. McConnell, J.L. York, D. Frizzell, and C. Ezell, J. Med. Chem., 36, 1084 (1993). (Inhibitory Activity) • This compound is distributed through Peptide Institute, Inc.under the technical and scientific advice of the Microbial Chemistry Research Foundation.

N-(4-Biphenylacetyl)-Cys(Me)-d-Arg-Phe-N-Phenylethylamide

(M.W. 735.96) C41H49N7O4SInhibitor for Cathepsin

IEC-3644-PI-20 °C

5 mg 65

S.F. Chowdhury, J. Sivaraman, J. Wang, G. Devanathan, P. Lachance, H. Qi, R. Ménard, J. Lefebvre, Y. Konishi, M. Cygler, T. Sulea, and E.O. Purisima, J. Med. Chem., 45, (2002).

Pepstatin A Purity: higher than 90% (HPLC)

Isovaleryl-l-valyl-l-valyl[(3S,4S)-4-amino-3-hydroxy-6-methylheptanoyl]-l-alanyl[(3S,4S)-4-Amino-3-hydroxy-6- methylheptanoic acid]

IPA-4397-v-20 °C

0.5 mg vial

4397-v

NH

NH

NH

NH

NH

OHO

O

O

OH O

O

OH O

50

• This compound is distributed through Peptide Institute, Inc. under the technical and scientific advice of the Institute of Microbial Chemistry Research Foundation.

Pepstatin A Purity: higher than 90% (HPLC)

IPA-4397-20 °C

25 mg100 mg

85200

Isovaleryl-l-valyl-l-valyl[(3S,4S)-4-amino-3-hydroxy-6- methylheptanoyl]-l-alanyl [(3S,4S)-4-Amino-3-hydroxy-6-methylheptanoic acid](M.W. 685.89) C34H63N5O9 [26305-03-3] Microbial Product Inhibitor for Pepsin, Cathepsin D/E and Renin H. Umezawa, T. Aoyagi, H. Morishima, M. Matsuzaki, M. Hamada, and T. Takeuchi, J. Antibiotics, 23, 259 (1970). (Original) T. Aoyagi, H. Morishima, R. Nishizawa, S. Kunimoto, T. Takeuchi, H. Umezawa, and H. Ikezawa, J. Antibiotics, 25, 689 (1972). (Biological Activity) • This compound is distributed through Peptide Institute, Inc. under the technical and scientific advice of the Institute of Microbial Chemistry Research Foundation.

Page 18: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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158 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT CODE QTy PRICE Z-Leu-Leu-Leu-H (aldehyde) [MG-132]

Benzyloxycarbonyl-l-leucyl-l-leucyl-l-leucinal (M.W. 475.62) C26H41N3O5 [133407-82-6] Synthetic Product Inhibitor for Proteasome and Cathepsin K

IZL-3175-v-20 °C

5 mgvial

O

O

NH

O

NH

O

NHO

H

3175-v

50

Y. Saito, S. Tsubuki, H. Ito, and S. Kawashima, Neurosci. Lett., 120, 1 (1990). T.J. Jensen, M.A. Loo, S. Pind, D.B. Williams, A.L. Goldberg, and J.R. Riordan, Cell, 83, 129 (1995). B.J. Votta, M.A. Levy, A. Badger, J. Bradbeer, R.A. Dodds, I.E. James, S. Thompson, M.J.Bossard, T. Carr, J.R. Conner, T.A. Tomaszek, L. Szewczuk, F.H. Drake, D.F. Veber, and M. Gowen, J. Bone Miner. Res., 12, 1396 (1997) • This compound is distributed through Peptide Institute, Inc. under the license of Dr. H. Ito.

Chymotrypsin and Chymotrypsin-like InhibitorsAla-Ala-Phe-CH2Cl See Code IAA-3202-v on page 169.

Aprotinin (Bulk)Arg-Pro-Asp-Phe-Cys-Leu-Glu-Pro-Pro-Tyr-Thr-Gly-Pro- Cys-Lys-Ala-Arg-Ile-Ile-Arg-Tyr-Phe-Tyr-Asn-Ala-Lys- Ala-Gly-Leu-Cys-Gln-Thr-Phe-Val-Tyr-Gly-Gly-Cys- Arg-Ala-Lys-Arg-Asn-Asn-Phe-Lys-Ser-Ala-Glu- Asp-Cys-Met-Arg-Thr-Cys-Gly-Gly-Ala

IAT-3830-PI-20 °C

25 mg100 mg

195575

(Disulfide bonds between Cys5-Cys55, Cys14-Cys38, and Cys30-Cys51) (M.W. 6511.57) C284H432N84O79S7

I. Trautschold, E. Werle and G. Zickgraf-Rudel, Biochem. Pharm., 16, 59 (1967).

Chymostatin*A Mixture of Type A, B, and C

ICy-4063-v-20 °C

0.5 mg vial

40

[(S)-1-Carboxy-2-phenylethyl]carbamoyl-a-[2-iminohexahydro-4(S)- pyrimidyl]-(S)-glycyl-X-phenylalaninal X: l-leucyl (Type A), l-valyl (Type B), l-isoleucyl (Type C) [9076-44-2] Microbial Product

Chymostatin* (Bulk)A Mixture of Type A, B, and C[(S)-1-Carboxy-2-phenylethyl]carbamoyl-a-[2-iminohexa-hydro-4(S)-pyrimidyl]-(S)-glycyl-X-phenylalaninal

ICy-4063-20 °C

25 mg100 mg

200

595

X: l-leucyl (Type A), l-valyl (Type B), l-isoleucyl (Type C) [9076-44-2] Microbial Product Inhibitor for Chymotrypsin, Chymase, Papain, and Cathepsin B/G

H. Umezawa, et al., J. Antibiotics, 23, 425 (1970). (Original) K. Tatsuta, et al.,, J. Antibiotics, 26, 625 (1973). (Chem. Structure) R.L. Stein and A.M. Strimpler, Biochemistry, 26, 2611 (1987). (Inhibitory Activity) L.A. Johnson, K.E. Moon, and M. Eisenberg, Biochim. Biophys. Acta, 953, 269 (1988). (Inhibitory Activity) • This compound is distributed through Peptide Institute, Inc. under the technical and scientific advice of the Microbial Chemistry Research Foundation.

Coagulation Factors Inhibitors Also see IAP-4062-v and IAP-4062 Antipain on page 159; ILP-4041-v and ILP-4041 Leupeptin on pages 160-161.

H-Gly-Pro-Arg-Pro-OH(Trifluoroacetate Form)

INH-3797-PI-20 °C

5 mg25 mg

35130

GPRP (M.W. 425.49) C18H31N7O5 [67869-62-9] Fibrinolysis Inhibiting Factor

Page 19: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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Order Hotline 1-800-777-4779 502-266-8787 159

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RS AND SuBSTRATES

Examples of Proteolytic Enzymes and Their Inhibitors

Collagenase / MMP / Stromelysin Inhibitors .GalardinTM

Peptides International is now offering GalardinTM, an addition to other widely used enzyme inhibitors.1 Galardin or GM6001 is a potent, broad-spectrum matrix metal-loproteinase (MMP) inhibitor and is a member of the hydroxamate class of inhibitors. We are pleased to add galardin to complement our popular line of TAPI MMP inhibi-tors.21. J. Gordon, B.K. Kelly, and G.A. Miller, Nature. 195, 701 (1962).2. K. Darlak, R.B. Miller, M.S. Stack, A.F. Spatola, and R.D. Grey, J. Biol. Chem., 265, 5199 (1990).

GalardinTM GM6001, Ilomastat

N-[(2R)-2-(Hydroxamidocarbonylmethyl)-4-methylpentanoyl]-l-tryptophan methylamide(M.W. 388.47) C20H28N4O4Inhibitor for Collagenases and MMPsD. Grobelny, I. Poncz, and R.E. Galardy, Biochemistry, 31, 7152 (1992).

INH-3927-PI-20 °C

5 mg 175

Ac-SIMP-1Ac-S-CH2-(R)-CH(CH2CH(CH3)2)-CO-Phe-Ala-NH2(2R)-S-Acetyl-2-mercaptomethyl-4-methylpentanoyl-l-phenylalanyl-l-alanine amide (M.W. 421.56) C21H31N3O4S (Protected precursor) Collagenase Inhibitor

ISN-3821-PI-20 °C

5 mg

S NH

NH

NH2

O O

O

O

ISN-3821-PI Ac-SIMP-1

75

• Product produced under license from Research Corporation Technologies

Ac-SIMP-2(Protected Precursor) Ac-S-CH2-(R)-CH(CH2CH(CH3)2)-CO-Nal-Ala-NH2(2R)-S-Acetyl-2-mercaptomethyl-4-methylpentanoyl-l-b-(2-naphthyl)alanyl-l-alanine amide (M.W. 471.62) C25H33N3O4S Collagenase Inhibitor

ISN-3831-PI-20 °C

5 mg

S NH

NH

NH2

O O

O

O

ISN-3831-PI

95

• Product produced under license from Research Corporation Technologies.

SIMP-2(Free thiol form) HS-CH2-(R)-CH(CH2CH(CH3)2)-CO-Nal-Ala-NH2(2R)-2-mercaptomethyl-4-methylpentanoyl-l-b-(2-naphthyl)alanyl-l-alanine amide (M.W. 429.59) C23H31N3O3S Collagenase Inhibitor

ISN-3835-PI-20 °C

5 mg

SH NH

NH

NH2

O

O

O

ISN-3835-PI SIMP-2

110

• Product produced under license from Research Corporation Technologies.

TAPI-OHONHCOCH2CH(CH2CH(CH3)2)CO-Nal-Ala-NH2 N-(R)-(2-(Hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-l-3-(2'-naphthyl)alanyl-l-alanine amide (M.W. 456.53) C24H32N4O5 Inhibitor for Matrix Metalloproteases (MMP)

INH-3850-PI-20 °C

1 mg5 mg

OHNH

O

O

NH

NH

O

O

NH2

3850

125495

NEW!

Page 20: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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160 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT CODE QTy PRICE K. Darlak, R.B. Miller, M.S. Stack, A.F. Spatola, and R.D. Grey, J. Biol. Chem., 265, 5199 (1990). A.F. Spatola, K. Darlak, S. Pegoraro, K. Nijhawan, M. Anzolin, L. Lankiewicz, and R.D. Gray, Peptides: Chemistry & Biology, J.A. Smith & J.E. Rivier (Eds.), ESCOM, Leiden, 1992, p. 820. K.M. Mohler, P.R. Sleath, J.N. Fitzner, D.P. Cerretti, M.Alderson, S.S Kerwar, D.S. Torrance, C. Otten-Evans, T. Greenstreet, K. Weerawarna, S.R. Kronheim, M. Petersen, M. Gerhart, C.J. Kozlosky, C.J. March, and R.A. Black, Nature, 370, 218 (1984).

TAPI-1HONHCOCH2CH(CH2CH(CH3)2)CO-Nal-Ala-NHCH2CH2NH2 N-(R)-(2-(Hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-l-3-(2'-naphthyl)alanyl-l-alanine 2-aminoethyl amide (M.W. 499.60) C26H37N5O5 Inhibitor for Matrix Metalloproteases (MMP)

INH-3855-PI-20 °C

1 mg5 mg

OHNH

O

O

NH

NH

O

O

NH

NH2

3855

125495

K. Darlak, R.B. Miller, M.S. Stack, A.F. Spatola, and R.D. Grey, J. Biol. Chem., 265, 5199 (1990). A.F. Spatola, K. Darlak, S. Pegoraro, K. Nijhawan, M. Anzolin, L. Lankiewicz, and R.D. Gray, Peptides: Chemistry & Biology, J.A. Smith & J.E. Rivier (Eds.), ESCOM, Leiden, 1992, p. 820. K.M. Mohler, et al., Nature, 370, 218 (1984).

TAPI-2HONHCOCH2CH(CH2CH(CH3)2)CO-t-butyl-Gly-Ala-NHCH2CH2NH2 N-(R)-(2-(Hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-l-t-butyl-glycyl-l-alanine 2-aminoethyl amide (M.W. 415.53) C19H37N5O5 Inhibitor for Metalloproteases (MMP)

INH-3852-PI-20 °C

1 mg5 mg

OHNH

O

O

NH

NH

O

O

NH

NH2

3852-v

125495

J. Arribas, L. Coodly, P. Vollmer, T.K. Kishimoto, S. Rose-John, and J. Massagué, J. Biol. Chem., 271, 11376 (1996). N.M. Hooper, E.H. Karran, and A.J. Turner, Biochem. J., 321, 265 (1997).

Dipeptidyl Peptidase II (DPP II) InhibitorsH-Dab-Pip

(Trifluoroacetate Form) L-2,4-Diaminobutyrylpiperidinamide(M.W. 185.27) C9H19N3O Inhibitor for Dipeptidyl Peptidase II (DPP II)

IDP-3655-PI-20 °C

5 mg

N

ONH2

NH2

H-Dab-PipIDP-3655-PIDipeptidyl Peptidase II (DPP II) Inhibitor

K. Senten, P. Van der Veken, G. Bal, I. De Meester, A.-M. Lambier, S. Sharpé, B. Bauvois, A. Haemers, and K. Augustyns, Bioorg. Med. Chem. Lett. 12, 2825 (2002).

Diprotin AIle-Pro-Ile (M.W. 341.45) C17H31N3O4 [90614-48-5]

IDP-4132-v-20 °C

0.5 mg vial

22

Diprotin A (Bulk)Ile-Pro-Ile • H2O Synthetic Product Inhibitor for Dipeptidyl-Aminopeptidase IV

IDP-4132-20 °C

25 mg100 mg

75

170

H. Umezawa, T. Aoyagi, K. Ogawa, H. Naganawa, M. Hamada, and T. Takeuchi, J. Antibiotics, 37, 422 (1984). (Original; IC50 & Chem. Structure) • This compound is distributed exclusively through Peptide Institute, Inc. under the license of the Microbial Chemistry Research Foundation.

E-64 See page 160.

Elastase Inhibitors

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PRODUCT CODE QTy PRICE PEPTIDES INTERNATIO

NAL

Order Hotline 1-800-777-4779 502-266-8787 161

ENZYME INHIBITO

RS AND SuBSTRATES

Cl-Ac-(OH)Leu-Ala-Gly-NH2 N-Chloroacetyl-N-hydroxy-l-leucyl-l-alanylglycine amide (M.W. 350.80) C13H23N4O5Cl Synthetic Product

ICL-4146-v-20 °C

0.5 mg vial

35

Cl-Ac-(OH)Leu-Ala-Gly-NH2 (Bulk)N-Chloroacetyl-N-hydroxy-l-leucyl-l-alanylglycine amideN. Nishino and J.C. Powers, J. Biol. Chem., 255, 3482 (1980). (Original)

ICL-4146-20 °C

25 mg100 mg

4146-v

CIO

NOH O

NH

O

NH

O

NH2

230595

Elafin (Human) Ala-Gln-Glu-Pro-Val-Lys-Gly-Pro-Val-Ser-Thr-Lys-Pro-Gly-Ser-Cys-Pro-Ile-Ile-Leu-Ile-Arg-Cys-Ala-Met-Leu-Asn-Pro-Pro-Asn-Arg-Cys-Leu-Lys-Asp-Thr-Asp-Cys-Pro-Gly-Ile-Lys-Lys-Cys-Cys-Glu-Gly-Ser-Cys-Gly-Met-Ala-Cys-Phe-Val-Pro-Gln

PEL-4243-v-20 °C

20 mg vial

375

(Disulfide bonds between Cys16-Cys45, Cys23-Cys49, Cys32-Cys44 and Cys38-Cys53) (M.W. 5999.1) C254H416N72O75S10 Synthetic Product Elastase-Specific Inhibitor from Human Skin

O. Wiedow, J.-M. Schröder, H. Gregory, J.A. Young, and E. Christophers, J. Biol. Chem., 265, 14791 (1990). (Original) O. Wiedow, J.-M. Schröder, H. Gregory, J.A. Young, and E. Christophers, J. Biol. Chem., 266, 3356 (1991). (Correction of Sequence) M. Tsunemi, H. Kato, Y. Nishiuchi, S. Kumagaye, and S. Sakakibara, Biochem. Biophys. Res. Commun., 185, 967 (1992). (Chem. Synthesis & Biochem.) M. Tsunemi, Y. Matsuura, S. Sakakibara, and Y. Katsube, Biochemistry, 35, 11570 (1996). (Biochem; Crystal Structure of Elafin-Pancreatic Elastase)

ElastatinalMicrobial Product

IEL-4064-v-20 °C

0.5 mg vial

45

Elastatinal (Bulk)Microbial ProductInhibitor for Elastase

IEL-4064-20 °C

25 mg100 mg

190

660

H. Umezawa, T. Aoyagi, A. Okura, H. Morishima, T. Takeuchi, and Y. Okami, J. Antibiotics, 26, 787 (1973). (Original) • This compound is distributed exclusively through Peptide Institute, Inc. under the license of the Microbial Chemistry Research Foundation.

Endothelin A & B Receptors (Antagonists) BQ-123 Sodium Salt

cyclo (d-Trp-d-Asp-Pro-d-Val-Leu) (M.W. 610.72) C31H42N6O7

PED-3512-PI-20 °C

1 mg5 mg

65

195

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162 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT CODE QTy PRICE BQ-610 Sodium Salt

Homopiperidinyl-CO-Leu-d-Trp(CHO)-d-Trp-OH (M.W. 656.79) C36H44N6O6

K. Ishikawa, T. Fukami, T. Nagase, T. Mase, T. Hayama, K. Niiyama, K. Fujita, Y. Urakawa, U. Kumagai, T. Fukuroda, M. Ihara, and M. Yano. in C.H. Schneider, and A.N. Eberle (Eds.), Peptides, 1992, ESCOM, Leiden, 1993, p. 685.

PED-3610-PI-20 °C

1 mg 5 mg

N-CO-Leu-D-Trp(CHO)-D-Trp-OH

75275

BQ-788 Sodium SaltN-cis-2,6-Dimethylpiperidinocarbonyl-l-g-Me-Leu-d-Trp(COOMe)-d-Nle (Sodium Salt)(M.W. 663.80) C34H50N5O7NaSoluble: 2 mg in 1 mL H2OT. Fukuroda, T. Fujikawa, S. Ozaki, K. Ishikawa, M. Yano, and M. Nishikibe, Biochem. Biophys Res. Commun., 199, 1461 (1994).

PED-3788-PI-20 °C

1 mg5 mg

N

N

NH

O

O

NH

NH

OONa

OO

O

3788

140495

d-Glucaro-δ-Lactam See Code CAR-24004-v on page 224.

Gingipain InhibitorsKyT-1

(Hydrochloride Form)(3S)-N-[(1S)-5-Amino-1-(N,N-dimethylcarbamoyl)pentyl]-3-[(2S)-6-amino-2-[(benzyloxycarbonyl)amino]hexanoylamino]-6-guanidino-2-oxohexanamide (M.W. 619.76) C29H49N9O6 Synthetic Product Inhibitor for Arg-Gingipain

IRG-4395-v-20 °C

1 mg vial

O NH

ONH

O

ONH

O

NH

NH2 NH

NH2

NH2

N

O

4395-v

300

T. Kadowaki, A. Baba, N. Abe, R. Takii, M. Hashimoto, T. Tsukuba, S. Okazaki, Y. Suda, T. Asao, and K.Yamamoto,Mol. Pharmacol., 66, 1599 (2004). (Original)

KyT-36(Hydrochloride Form)(2S)-N-[(1S)-1-(4-Aminobutyl)-2-oxo-2-(N-benzylcarbamoyl)ethyl]-N'-(N-methylphenylamino)-2-[(benzyloxycarbonyl)amino]pentane-1,5-diamide (M.W. 630.73) C34H42N6O6 Synthetic Product Inhibitor for Lys-GingipainT. Kadowaki, A. Baba, N. Abe, R. Takii, M. Hashimoto, T. Tsukuba, S. Okazaki, Y. Suda, T. Asao, and K.Yamamoto, Mol. Pharmacol., 66, 1599 (2004). (Original)

IKG-4396-v-20 °C

1 mgvial

O NH

O

O NHN

NH

O

ONH

O

NH2

4396-v

300

IDE Inhibitor 6bK(Fumaryl-Lys-Cha-d-Bpa)-Lys-NH2

J.P. Maianti, et al., Nature, doi: 10.1038/nature13297. [Epub ahead of print] (2014).

IDE-3798-PI-20 °C

1 mg5 mg

4001600

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RS AND SuBSTRATES

Myr-Ser-Ile-Tyr-Arg-Arg-Gly-Ala-Arg-Arg-Trp-Arg-Lys-Leu See Code PKC-3403-v on page 221.MG-101 See Code IAL-3671-PI Ac-Leu-Leu-Nle-H on page 154.MG-115 See Code IAT-3170-v Z-Leu-Leu-Nva-H (aldehyde) on page 171.MG-132 See Code IZL-3175-v Z-Leu-Leu-Leu-H (aldehyde) on page 162.MMP Inhibitors See Collagenase Inhibitors on page 163-164 and TAPI-O, TAPI-1 and TAPI-2 on page 164.

Neutral Endopeptidase InhibitorsPhosphoramidon (Sodium Salt)

N-(a-Rhamnopyranosyloxyhydroxyphosphinyl)-l-leucyl-l-tryptophan (M.W. 543.50) C23H34N3O10P [36357-77-4] Microbial Product

IPO-4082-v-20 °C

0.5 mgvial

4082-v

NH

OH

ONH

ONH

POH

OO

O

OH OH

OH

CH3

45

Phosphoramidon (Bulk)N-(a-Rhamnopyranosyloxyhydroxyphosphinyl)--l-leucyl-l-tryptophan disodium salt dihydrate (M.W. 541.49 • 45.98 • 36.03) C23H32N3O10P [119942-99-3] Microbial Product

IPO-4082-20 °C

25 mg100 mg

180

570

Inhibitor for Thermolysin, Neutral Endopeptidase-24.11 (ANP Degradation Enzyme), and Endothelin converting Enzyme

H. Suda, T. Aoyagi, T. Takeuchi, and H. Umezawa, J. Antibiotics, 26, 621 (1973). (Original) S.L. Stephenson and A.J. Kenny, Biochem. J., 243, 183 (1987). (Pharmacol.) B.P. Roques and A. Beaumont, Trends Pharmacol. Sci., 11, 245 (1990). (Review) Y. Matsumura, K. Hisaki, M. Takaoka, and S. Morimoto, Eur. J. Pharmacol., 185, 103 (1990). (Pharmacol.) • This compound is distributed exclusively through Peptide Institute, Inc. under the license of the Microbial Chemistry Research Foundation.

Nojirimycin Bisulfite See Code CAR-24003-v on page 224.Pepsin See Code IPA-4397-v and IPA-4397 on page 161. Pepstatin A See Code IPA-4397-v and IPA-4397 on page 161. PSI See Code IAT-3169-v Z-Ile-Glu(OtBu)-Ala-Leu-H (aldehyde) on page 171.Plasmin See ILP-4041-v and ILP-4041 Leupeptin on pages 160-161.

Propyl Endopeptidase InhibitorSUAM-14746

3-({4-[2-(E)-Styrylphenoxy]butanoyl}-L-4-hydroxyprolyl)-thiazolidine(M.W. 466.59) C26H30N2O4S Synthetic Product Inhibitor for Prolyl Endopeptidase

ISU-3214-v -20 °C

5 mgvial

O

N

O

OH

O

N S

3214-v

180

M.Saito, M. Hashimoto, N. Kawaguchi, H. Shibata, H. Fukami, T. Tanaka, and N. Higuchi, J. Enzyme Inhib., 5, 51 (1991) (Assay Method) • This compound is distributed under license of Suntory Ltd.

Protein Kinase Inhibitor

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PRODUCT CODE QTy PRICE Lys-Lys-Lys-Leu-Arg-Arg-Gln-Glu-Ala-Phe-Asp-Ala-Tyr[Lys3, Phe10, Try13]-Autocamtide-2-Related Inhibitory Peptide (AIP)

(M.W. 1652.9) C74H121N23O20 Synthetic Product Inhibitor for Calmodulin-Dependent Protein Kinase II

IKK-4374-v-20 °C

0.5 mg vial

115

A. Ishida and H. Fujisawa, J. Biol. Chem., 270, 2163 (1995). (AIP; Autocamtide-2-Related Inhibitory Peptide) A. Ishida, et al., FEBS Lett., 427, 115 (1998). (Original) • This compound is distributed through Peptide Institute, Inc. under the license of the Agency of Industrial Science & Technology.

Renin See Code IPA-4397-v and IPA-4397 on page 161.

Reverse Transcriptase InhibitorDoxorubicin-HCl

(M.W. 579.98) C27H29NO11 • HCl [25316-40-9]Inhibitor of Reverse Transcriptase and RNA Polymerase

IOX-3765-PI-20 °C

1 g 1000

β-Secretase InhibitorsLys-Thr-Glu-Glu-Ile-Ser-Glu-Val-Asn-Sta-Val-Ala-Glu-Phe

Sta(Statine): (3S,4S)-4-Amino-3-hydroxy-6-methylheptanoic acid(M.W. 1651.8) C73H118N16O27 Synthetic Product Inhibitor for β-Secretase

IBS-4378-v-20 °C

1 mg vial

4378-v

NH

OOH

250

S. Sinha, et al., Nature, 402, 537 (1999). (Original)

γ-Secretase Inhibitors(3,5-Difluorophenylacetyl)-Ala-Phg-OBut

(3,5-Difluorophenylacetyl)-l-alanyl-l-2-phenylglycine t-butyl ester (M.W. 432.46) C23H26N2O4F2 Synthetic Product Inhibitor for g-SecretaseH.F. Dovey, et al., , J. Neurochem., 76, 173 (2001).

IGS-3219-v-20 °C

5 mgvial

F

F

NH

NH

O

O

O

O

3219-v

125

(Original; Functional g-Secretase Inhibitor in Brain) A.Y. Kornilova, et al., J. Biol. Chem., 278, 16470 (2003). (Comparison of in Cells and Cell-Free Activity)

(3,5-Difluorophenylacetyl)-Ala-Phg-OtBuN-[N-(3,5-Difluorophenacetyl)-l-alanyl)]-l-phenylglycine t-butyl ester (M.W. 432.47) C23H26N2O4F2 Inhibitor for g-Secretase

IGS-3641-PI-20 °C

10 mg 150

H.F. Dovey, et al., J. Neurochem., 76, 173 (2001). (Original; Functional g-Secretase Inhibitor in Brain) A.Y. Kornilova, et al., J. Biol. Chem., 278, 16470 (2003). (Comparison of in Cells and Cell-Free Activity)

Page 25: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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RS AND SuBSTRATES

L-685,458[(2R,4R,5S)-2-Benzyl-5-(t-Butyloxycarbonylamino)-4-hydroxy-6-phenylhexanoyl]-l-leucyl-l-phenylalanine amide (M.W. 672.85) C39H52N4O6 Synthetic Product Inhibitor for g-Secretase

IGS-4394-v-20 °C

1 mg vial

NH

O NH

NH

NH2

O OO

OOH

4394-v

360

Y.-M. Li, M. Xu, M.-T. Lai, Q. Huang, J.L. Castro, J. DiMuzio-Mower, T. Harrison, C. Lellis, A. Nadin, J.G. Neduvelil, R.B. Register, M.K. Sardana, M.S. Shearman, A.L. Smith, X.-P. Shi, K.-C. Yin, J.A. Shafer, and S.J. Gardell, Nature, 405, 689 (2000). (Biochem.; g-Secretase Inhibitor) Y.-M. Li, M.-T. Lai, M. Xu, Q. Huang, J. DiMuzio-Mower, M.K. Sardana, X.-P. Shi, K.-C. Yin, J.A. Shafer, and S.J. Gardell, Proc. Natl. Acad. Sci. USA, 97, 6138 (2000). (Biochem; g-Secretase Inhibitor) M.S. Shearman, D. Beher, E.E. Clarke, H.D. Lewis, T. Harrison, P. Hunt, A. Nadin, A.L. Smith, G. Stevenson, and J.L. Castro, Biochemistry, 39, 8698 (2000). (Biochem; g-Secretase Inhibitor) G. Tian, C.D. Sobotka-Briner, J. Zysk, X. Liu, C. Birr, M.A. Sylvester, P.D. Edwards, C.D. Scott, and B.D. Greenberg, J. Biol. Chem., 277, 31499 (2002). (Biochem; Inhibition Mechanism)

Siastatin B See Code CAR-24002-v on page 224.SIMP Products See Collagenase Inhibitors on page 163.

Signal Peptide Peptidase Inhibitor(Z-Leu-Leu-NHCH2)2CO[(Z-LL)2 Ketone]

1,3-Bis[(benzyloxycarbonyl-l-leucyl-l-leucyl)amino]acetone (M.W. 809.00) C43H64N6O9 [313664-40-3] Synthetic Product Inhibitor for Signal Peptide Peptidase

IZL-3218-v-20 °C

5 mgvial

O

O

NH

NH

O

NH

O

O

NH

NH

NH

O

O

O

O

3218-v

90

A. Weihofen, M.K. Lemberg, H.L. Ploegh, M. Bogyo, and B. Martoglio, J. Biol. Chem., 275, 30951 (2000). (Original) A. Weihofen, K. Binns, M.K. Lemberg, K. Ashman, and B. Martoglio, Science, 296, 2215 (2002). (Signal Peptide Peptidase Inhibitor) A. Weihofen, M.K. Lemberg, E. Friedmann, H. Rueeger, A. Schmitz, P. Paganetti, G. Rovelli, and B. Martoglio, J. Biol. Chem., 278, 16528 (2003). (Signal Peptide Peptidase Inhibitory Activity)

Sodium Potassium ATPase Inhibitor-1 (Porcine) See Code PSP-4216-s on page 115.

Tripeptidyl Peptidase II InhibitorAla-Ala-Phe-CH2Cl

(l-alanyl-l-alanyl-l-phenylalanyl)chloromethane (M.W. 339.82) C16H22N3O3Cl [102129-66-8] Synthetic Product

IAA-3202-v-20 °C

5 mgvial

ONH

CINH

ONH2

O

3202-v

70

Inhibitor for Tripeptidyl Peptidase II (Component of Giant Protease with Some Proteasome Function), Chymotrypsin, and ChymaseR. Glas, M. Bogyo, J.S. McMaster, M. Gaczynska, and H.L. Ploegh, Nature, 392, 618 (1998). E. Geier, G. Pfeifer, M. Wilm, M. Lucchiari-Hartz, W. Baurmeister, K. Eichmann, and G. Niedermann, Science, 283, 978 (1999). L.A. Johnson, K.E. Moon, and M. Eisenberg, Biochem. Biophys. Acta, 953, 269 (1988)

Trypsin and Trypsin-like Protease Inhibitors See Code IAP-4062 Antipain on page 159, Code IAT-3830-PI Aprotinin on page 162, and Codes ILP-4041-v and ILP-4041 Leupeptin on page 160-161.

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166 Order Hotline 1-800-777-4779 502-266-8787

Ubiquitin Proteasome System Inhibitors Also see Code IAL-3678-PI Ac-Leu-Leu-Met-(aldehyde) on page 154, Code IAL-3671 Ac-Leu-Leu-Nle-H (aldehyde) [ALLM] on page 154, and Code IZL-3175-v Z-Leu-Leu-Leu-H (aldehyde) [MG-132] (for Proteasome) on page 162.

Epoxomicin(2R)-2-[Acetyl-(N-methyl-l-Isoleucyl)-l-isoleucyl-l-threonyl-l-Leucyl]-2-Methyloxirane(M.W. 554.72 ) C28H50N4O7 [134381-21-8] Synthetic Product Inhibitor for Proteasome

IEP-4381-v-20 °C

0.2 mgvial

4381-v

O

O

NO

NH

O

NH

OH

O

NH

O

250

L. Meng, R. Mohan, B.H.B. Kwok, M. Elofsson, N. Sin, and C.M. Crews, Proc. Natl. Acad. Sci. USA, 96, 10403 (1999). (Proteasome Inhibitor & Antiinflammatory Activity) N. Sin, K.B. Kim, M. Elofsson, L. Meng, H. Auth, B.H.B. Kwok, and C.M. Crews, Bioorg. Med. Chem. Lett., 9, 2283 (1999). (Proteasome Inhibitor) K.B. Kim, J. Myung, N. Sin, and C.M. Crews, Bioorg. Med. Chem. Lett., 9, 3335 (1999). (Proteasome Inhibitor) M. Groll, K.B. Kim, N. Kairies, R. Huber, and C.M. Crews, J. Am.Chem. Soc., 122, 1237 (2000). (Crystal Structure of Proteasome Complex)T. Aoyagi, T. Wada, H. Iinuma, K. Ogawa, F. Kojima, M. Nagai, H. Kuroda, A. Obayashi, and H. Umezawa, J. Appl. Biochem., 7, 388 (1985). (Pharmacol.) • This compound is distributed exclusively through Peptide Institute, Inc. under the license of the Microbial Chemistry Research Foundation.

LactacystinN-Acetyl-S-{(2R,3S,4R)-3-hydroxy-2-[(1S)-1-hydroxy-2-methylpropyl]-4-methyl-5-oxo-pyrolidine-2-carbonyl}-l-cysteine (M.W. 376.43) C15H24N2O7S [133343-34-7] Microbial Product Inhibitor for Proteasome

ILC-4368-v-20 °C

0.2 mgvial

4368-v

NH

OH

O

OH O

SNH

O

O OH

225

S. Omura, T. Fujimoto, K. Otoguro, K. Matsuzaki, R. Moriguchi, H. Tanaka, and Y. Sasaki, J. Antibiotics, 44, 113 (1991). (Original) S. Omura, K. Matsuzaki, T. Fujimoto, K. Kosuge, T. Furuya, S. Fujita, and A. Nakagawa, J. Antibiotics, 44, 117 (1991). (Original; Chem. Structure) G. Fenteany, R.F. Standaert, W.S. Lane, S. Choi, E.J. Corey, and S.L. Schreiber, Science, 268, 726 (1995). (Biochem.; Proteasome Inhibition) S. Imajoh-Ohmi, T. Kawaguchi, S. Sugiyama, K. Tanaka, S. Omura, and H. Kikuchi, Biochem. Biophys. Res. Commun., 217, 1070 (1995). (Biochem.; Apoptotic Effect) • This item is produced by Kyowa Medex Co., Ltd.

Ubiquitin AldehydeMet*-Gln-Ile-Phe-Val-Lys-Thr-Leu-Thr-Gly-Lys-Thr-Ile-Thr-Leu-Glu-Val-Glu-Pro-Ser-Asp-Thr-Ile-Glu-Asn-Val-Lys-Ala-Lys-Ile-Gln-Asp-Lys-Glu-Gly-Ile-Pro-Pro-Asp-Gln-Gln-Arg-Leu-Ile-Phe-Ala-Gly-Lys-Gln-Leu-Glu-Asp-Gly-Arg-Thr-Leu-Ser-Asp-Tyr-Asn-Ile-Gln-Lys-Glu-Ser-Thr-Leu-His-Leu-Val- Leu-Arg-Leu-Arg-Gly-Gly-H (aldehyde) * Met at position 1 is oxidized to Met(O). (M.W. 8564.70) C378H629N105O118S Semisynthetic ProductInhibitor for Deubiquitinating Enzyme

IUB-3207-v-20 °C

50 mgvial

250

J.R. Schaeffer and R.E. Cohen, Biochemistry, 35, 10886 (1996). F. Melandri, L. Grenier, L. Plamondon, W.P. Huskey, and R.L. Stein, Biochemistry, 35, 12893 (1996). S.H. Baek, K.S. Choi, Y.J. Yoo, J.M. Cho, R.T. Baker, K. Tanaka, and C.H. Chung, J. Biol. Chem., 272, 25560 (1997). L.C. Dang, F.D. Melandri, and R.L. Stein, Biochemistry, 37, 1868 (1998)

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Z-Ile-Glu(OBut)-Ala-Leu-H (aldehyde) [PSI]

Benzyloxycarbonyl-l-isoleucyl-[(2S)2-amino-4- (t-Butyloxycarbonyl)butanoyl]-l-alanyl-l-leucinal (M.W. 618.76) C32H50N4O8 [158442-41-2] Synthetic Product Inhibitor for Proteasome

IAT-3169-v-20 °C

5 mgvial

O

O

NH

O

NH

O O

O

NH

O

NH

H

O

3169-v

99

M.E. Figueiredo-Pereira, K.A. Berg, and S. Wilk, J. Neurochem., 63, 1578 (1994). E.B.-M. Traenckner, S. Wilk, and P.A. Baeuerle, EMBO J., 13, 5433 (1994). M.E. Figueiredo-Pereira, W-E. Chen, H-M. Yuan, and S. Wilk, Arch. Biochem. Biophys., 317, 69 (1995).

Z-Leu-Leu-Nva-H (aldehyde)[MG-115]

Benzyloxycarbonyl-l-leucyl-l-leucyl-l-norvalinal (M.W. 461.59) C25H39N3O5 [133407-86-0] Synthetic Product Inhibitor for Proteasome

IAT-3170-v-20 °C

5 mg vial

3170-v

O

O

NH

O

NH

O

NH

O

H

65

Y. Saito, S. Tsubuki, H. Ito, and S. Kawashima, Neurosci. Lett., 120, 1 (1990). A. Vinitsky, C. Michaud, J.C. Powers, and M. Orlowski, Biochemistry, 31, 9421 (1992). K.L. Rock, C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A.L. Goldberg, Cell, 78, 761 (1994). V.J. Palombella, O.J. Rando, A.L. Goldberg, and T. Maniatis, Cell, 78, 773 (1994). • This compound is distributed through Peptide Institute, Inc. under the license of Dr. H. Ito.

u-PA Urokinase Inhibitor See Code IAP-4062 Antipain on page 159.

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Inhibitors Actinonin

(Aminopeptidase M and Leucyl Aminopeptidase)

Amastatin (Aminopeptidases)

Arphamenine A (Aminopeptidase B)

Arphamenine B (Aminopeptidase B)

Collagenase Inhibitors (Collagen)

Diprotin A (Dipeptidyl Aminopeptidase IV)

Foroxymithine (Angiotensin I Converting Enzyme (ACE))

Leuhistin (Aminopeptidase M)

Phosphoramidon (Collagenase,Thermolysin and Enkephalinase (24.11))

Ubenimex (Bestatin) (Aminopeptidase B and Leucyl Aminopeptidase)

Others EDTA

a-Ketoamides

Divalent metal chelating reagents

8-Hydroxyisoquinolin

Captopril

Metalloproteases

Inhibitors Pepstatin A

(Renin, Cathepsin D)

Others Peptide Renin Inhibitors

Peptide HIV Inhibitors

Aspartyl Proteases

Inhibitors Antipain

(Cathepsin B)

Chymostatin (Cathepsin B and Papain)

E-64 (Thiol Proteases)

Leupeptin (Cathepsin B)

Others Peptidyl chloromethanes

Peptidyl aldehydes

Peptidyl diazomethanes

Cysteinyl Proteases

Inhibitors Aprotinin

(Kallikrein, Trypsin, Chymotrypsin and Plasmin)

Antipain (Trypsin)

Elastatinal (Elastase)

Chymostatin (Chymotrypsin)

Leupeptin (Trypsin, Plasmin)

Others Organophosphates

Peptidyl chloromethanes

Sulfonyl fluorides

Peptidyl aldehydes

Peptidyl borates

Seryl Proteases

Examples of Proteolytic Enzymes and Their Inhibitors

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PEPTIDES INTERNATIONAL

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ENZYME INHIBITO

RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Enzyme Substrates & Related CompoundsADAM-17 SubstratesAbz-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-Dap(Dnp)-NH2

SDP-3818-PI-20 °C

1 mg5 mg

75285

(Acetate Form) 2-Aminobenzoyl-l-leucyl-l-alanyl-l-glutaminyl-l-alanyl-l-valyl-l-arginyl-l-Seryl-l-Seryl-l-Seryl-l-arginyl- [Ne (2,4-dinitrophenyl)-l-2,3-Diaminopropionyl] amide (M.W. 1444.54) C59H93N23O20 Fluorescence-Quenching Substrate for ADAM17 / TNF-a Converting EnzymeG. Jin, X. Huang, R. Black, M. Wolfson, C. Rauch, H. McGregor, G. Ellestad, R. Cowling, Anal. Biochem., 302, 269 (2002).

Dabcyl-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-Edans

(Trifluoroacetate Form) (M.W. 1573.81) C70H104N22O18S [396716-14-6]TACE FRET Substrate IK.M.Mohler et al., Nature, 370, 218 (1994)A.J.H.Gearing et al., Nature, 370, 555 (1994)B.F.Becker et al., Biol. Chem., 383, 1821 (2002)

SFQ-3764-PI-20 °C

1 mg5 mg

235940

MOCAc-Lys-Pro-Leu-Gly-Leu-A2pr(Dnp)-Ala-Arg-NH2

(Trifluoroacetate Form)

A SMO-3226-v-20 °C

1 mg vial

105

(7-Methoxycoumarin-4-yl) acetyl-l-lysyl-l-prolyl-l-leucyl-glycyl-l-leucyl- [Nb-(2,4-dinitrophenyl)-l-2,3-diaminopropionyl]-l-alanyl-l-arginine amide (M.W. 1221.3) C55H80N16O16 Fluorescence-Quenching Substrate for Matrix Metalloproteinases and ADAM-17 / Tumor Necrosis Factor Converting Enzyme (TACE)U. Neumann, H. Kubota, K. Frei, V. Ganu, and D. Leppert, Anal. Biochem., 328, 166 (2004). A. Trifilieff, C. Walker, T. Keller, G. Kottirsch, and U. Neumann, Br. J. Pharmacol., 135, 1655 (2002). M.C. Riitano, H. Pfister, P. Engelhardt, U. Neumann, M. Reist, A. Zurbriggen, M. Stoffel, J. Peel, T. Jungi, P. Schawalder, and D.E. Spreng, Am. J. Vet. Res., 63, 1423 (2002).

MOCAc-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2

(Trifluoroacetate Form) (M.W. 1221.35) C55H80N16O16 Fluorescence-Quenching Substrate for MMPs, Cathepsin D and E, ADAM10, and ADAM17/TACE

SMO-3670-PI-20 °C

1 mg5 mg

80320

U. Neumann , H. Kubota, K. Frei, V. Ganu, and D. Leppert, Anal. Biochem., 328, 166 (2004).

NEW!

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ADAMTS-13 Substrates See page 210 for other FRETS Substrates.

FRETS-VWF73(Trifluoroacetate Form)

A SFR-3224-s-20 °C

0.1 mg vial

380

Asp-Arg-Glu-A2pr(Nma)-Ala-Pro-Asn- Leu-Val-Tyr-Met-Val-Thr-Gly- A2pr(Dnp)-Pro-Ala-Ser-Asp-Glu-Ile-Lys-Arg-Leu-Pro-Gly-Asp-Ile- Gln-Val-Val-Pro-Ile-Gly-Val-Gly-Pro-Asn-Ala-Asn-Val-Gln-Glu-Leu- Glu-Arg-Ile-Gly-Trp-Pro-Asn-Ala-Pro-Ile-Leu-Ile-Gln-Asp-Phe- Glu-Thr-Leu-Pro-Arg-Glu-Ala-Pro-Asp-Leu-Val-Leu-Gln-Arg A2pr(Nma): Nb-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid A2pr(Dnp): Nb-(2,4-dinitrophenyl)-2,3-diaminopropionic acid (M.W. 8314.30 ) C370H583N103O113S Purity: higher than 95% by HPLC Fluorescence-Quenching Substrate for ADAMTS-13K. Kokame, M. Matsumoto, Y. Fujimura, and T. Miyata, Blood, 103, 607 (2004). (VWF73 Sequence) K. Kokame, Y. Nobe, Y. Kokubo, A. Okayama, and T. Miyata, Br. J. Haematol., 129, 93 (2005). (FRETS-VWF73) • This compound is produced by Peptide Institute, Inc.under license of the National Cardiovascular Center in Japan

α-Amidating Enzyme SubstratesAc-Tyr-Val-Gly

Acetyl-l-tyrosyl-l-valyl-glycine (M.W. 379.41) C18H25N3O6 Substrate for a-Amidating Enzyme

AA SyG-3146-20 °C

0.1 g1 g

90625

Aminopeptidases SubstratesAla-MCA

(Tosylate Form)l-alanine 4-methylcoumaryl-7-amide(M.W. 246.26) C13H14N2O3 [77471-41-1] Substrate for Aminopeptidase.

AA MAM-3147-v-20 °C

5 mg vial

35

H. Umetsu, et al., Biosci. Biotechnol. Biochem., 68, 945 (2004).J.R. McDermott, et al., J. Neurochem., 45, 752 (1985)

Ala-pNAl-alanine p-nitroanilide(M.W. 209.20) C9H11N3O3 [1668-13-9]Substrate for Aminopeptidase

AA SAN-3068-20 °C

0.1 g1 g5 g

2575

315G. Peleiderer, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds.), Academic Press, New York, 1970, pp. 514-521.

Leu-MCA(Tosylate Form) l-Leucine 4-methylcoumaryl-7-amide (M.W. 288.34) C16H20N2O3 Substrate for Aminopeptidase

AA MLM-3091-v-20 °C

5 mgvial

35

K. Saifuku, T. Sekine, T. Namihisa, T. Takahashi, and Y. Kanaoka, Clin. Chim. Acta, 84, 85 (1978).

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Leu-NH2 • HCI

l-Leucine amide monohydrochloride (M.W. 130.19 • 36.46) C6H14N2O • HCI [10466-61-2] Substrate for Aminopeptidase

AA SLN-3027-20 °C

0.1 g1 g

2550

F.H. Carpenter and J.M.Vahl, J. Biol. Chem., 248, 294 (1973). T. Sopanen and J. Mikola, Plant Physiol., 55, 809 (1975). H.F.M. Hermes, et al., Applied and Environm. Microbiol., 59, 4330 (1993).

Leu-pNAl-leucine p-nitroanilide (M.W. 251.28) C12H17N3O3 [4178-93-2] Substrate for Aminopeptidase

AA SLN-3014-20 °C

0.1 g1 g5 g

2250

165G. Peleiderer, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds.), Academic Press, New York, 1970, pp. 514-521.

Lys-MCA(Hydrochloride Form) l-Lysine 4-methylcoumaryl-7-amide (M.W. 303.36) C16H21N3O3 Substrate for Aminopeptidase

A MKM-3132-v-20 °C

5 mg vial

50

H. Araki, et al, J. Biochem., 129, 279 (2001).

Met-Leu-pNA(Hydrochloride Salt) l-methionyl-l-leucine p-nitroanilide (M.W. 382.49 • 36.46) C17H26N4O4S • HClY. Wei and D. Pei, Anal. Biochem., 250, 29 (1997).

SML-3622-PI-20 °C

5 mg25 mg

70260

Met-MCA(Tosylate Form) l-Methionine 4-methylcoumaryl-7-amide (M.W. 306.38) C15H18N2O3S Substrate for Aminopeptidase

A MMM-3149-v-20 °C

5 mg vial

45

Phe-MCA(Tosylate Form) l-phenylalanine 4-methylcoumaryl-7-amide (M.W. 322.36) C19H18N2O3 [98516-72-4] Substrate for Aminopeptidase

AA MFM-3148-v-20 °C

5 mg vial

35

Y. Yanigisawa, et al., Biochem. Mol. Med.,59, 161 (1996).

Amyloid A4-Generating Enzyme SubstrateSuc-Ile-Ala-MCA

Succinyl-l-isoleucyl-l-alanine 4-methylcouma-ryl-7-amide (M.W. 459.49) C23H29N3O7 [126103-95-5] Substrate for Amyloid A4-Generating Enzyme

A MIA-3158-v-20 °C

5 mg vial

55

S. Ishiura, T. Tsukahara, T. Tabira, T. Shimizu, K. Arahata, and H. Sugita, FEBS Lett., 260, 131 (1990). S. Ishiura, T. Nishikawa, T. Tsukahara, T. Momoi, H. Ito, K. Suzuki, and H. Sugita, Neurosci. Lett., 115, 329 (1990).

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Z-Val-Lys-Met-MCA(Hydrochloride Form)

A MVM-3156-v-20 °C

5 mg vial

70

Benzyloxycarbonyl-l-valyl-l-lysyl-l-methionine 4-methylcoumaryl-7-amide (M.W. 667.82) C34H45N5O7S [141223-71-4] Substrate for Amyloid A4-Generating Enzyme and ProteasomeS. Ishiura, T. Nishikawa, T. Tsukahara, T. Momoi, H. Ito, K. Suzuki, and H. Sugita, Neurosci. Lett., 115, 329 (1990).

Angiotensin I Converting Enzyme I SubstratesAbz-Gly-Phe(NO2)-Pro-OH

(M.W. 483.48) C23H25N5O7 [67482-93-3]Substrate for ACE (Angiotensin-I Converting Enzyme)

SFQ-3937-PI -20 °C

5 mg25 mg

45160

A. Carmel and A. Yaron, Eur. J. Biochem., 87, 265 (1978).

Bz-Gly-Ala-Pro[Hippuryl-alanyl-proline]

Benzoyl-glycyl-l-alanyl-l-proline (M.W. 347.37) C17H21N3O5 [73167-84-7]

AA SGP-3126-20 °C

0.1 g1 g

50300

Substrate for ACE (Angiotensin I Converting Enzyme)H.S Cheung, F.L. Wang, M.A. Ondetti, E.F. Sabo, and D. W. Cushman, J. Biol. Chem., 255, 401 ( 1980).

Bz-Gly-Gly-Gly[Hippuryl-glycyl-glycine]

Benzoylglycylglycylglycine (M.W. 293.28) C13H15N3O5 [31384-90-4]

AA SGG-3128-20 °C

0.1 g1 g

35160

Substrate for ACE (Angiotensin l Converting Enzyme)H.Y.T. Yang, E.G. Erdos, and Y. Levin, J. Pharmacol. Exp. Ther., 177, 291 (1971). T. Nakajima, G. Oshima, H.S.J. Yeh, R. Igic, and E.G. Erdos, Biochim. Biophys. Acta., 315, 430 (1973). G. Oshima, K. Nagasawa, and J. Kato, J. Biochem. (Tokyo), 80, 477 (1976).

Bz-Gly-His-Leu • H2O[Hippuryl-histidyl-leucine]

Benzoylglycyl-l-histidyl-l-leucine (M.W. 429.47 • 18.02) C21H27N5O5 • H2O [31373-65-6]

AA SGL-3064-20 °C

0.1 g1 g

50300

Substrate for ACE (Angiotensin I Converting Enzyme)D.W. Cushman and H.S. Cheung, Biochem. Pharmacol., 20, 1637 (1971).

Nma-Phe-His-Lys(Dnp) [2-(Methylamino)benzoyl-L-phenylalanyl]-L-histidyl- Nε-(2,4-dinitrophenyl)-L-lysine (M.W. 729.74) C35H39N9O9

SNP-3233-v-20 °C

1 mg vial

86

Fluorescence-Quenching Substrate for Angiotensin I Converting Enzyme and Carboxypeptidase Y

S. Takahashi, H. Ono, T. Gotoh, K. Yoshizawa-Kumagaye, and T. Sugiyama, Biomed. Res., 32, 407 (2011).

Angiotensin I Converting Enzyme II SubstratesAbz-Gly-Phe-Ser-Pro-Tyr(NO2)-OH

(M.W. 733.74) C35H39N7O11Fluorescence-Quenching Substrate for ACE2 (TBC5180)

SFQ-3817-PI-20 °C

1 mg5 mg

45160

Z.-H. Yan, K.-J. Ren, Y. Wang, S. Chen, T.A. Brock, and A. Rege, Anal. Biochem., 312, 141 (2003).

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Abz-Ser-Pro-Tyr(NO2)-OH

(M.W. 529.51) C24H27N5O9 Fluorescence-Quenching Substrate for ACE2 (TBC5182)

SFQ-3819-PI-20 °C

1 mg5 mg

45160

Z.-H. Yan, K.-J. Ren, Y. Wang, S. Chen, T.A. Brock, and A. Rege, Anal. Biochem., 312, 141 (2003).

ANP (Rat) Precursor Processing Enzyme SubstrateBoc-Ala-Gly-Pro-Arg-MCA

t-Butyloxycarbonyl-l-alanyl-glycyl-l-prolyl-l-arginine 4-methylcoumaryl-7-amide(M.W. 656.73) C31H44N8O8 [118850-78-5]

A MAR-3144-v-20 °C

5 mvial

70

Substrate for ANP (Rat) Precursor Processing EnzymeT. Imada, R. Takayanagi, and T. Inagami, Biochem. Biophys. Res. Commun., 143, 587 (1987). T. Imada, R. Takayanagi, and T. Inagami, Biol. Chem. Hoppe-Seyler Suppl., 369, 113 (1988).

d-Aspartyl Endopeptidase SubstrateSuc-d-Asp-MCA

Succinyl-d-Aspartic acid a-(4-methylcoumaryl-7-amide) (M.W. 390.34) C18H18N2O8 Selective Substrate for d-Aspartyl Endopeptidase

AA MCA-3222-v-20 °C

5 mvial

80

T. Kinouchi, S. Ishiura, Y. Mabuchi, Y. Urakami-Manaka, H. Nishio, Y. Nishiuchi, M. Tsunemi, K. Takada, M. Watanabe, M. Ikeda, H. Matsui, S. Tomioka, H. Kawahara, T. Hamamoto, K. Suzuki, and Y. Kagawa, Biochem. Biophys. Res. Commun., 314, 730 (2004).

dl-BAPA See Code SRN-3013 Benzoyl-dl-arginine p-Nitroanilide Hydrochloride on page 204.l-BAPA See Code SRN-3057 Benzoyl-l-arginine p-Nitroanilide Hydrochloride on page 182.Biotinyl-Asp-Glu-Val-Asp-H (aldehyde) See Code IBA-3173-v on page 158.

Boc-Glu(OBzl)-Gly-Arg-MCA(Hydrochloride Form)

A MEG-3115-v-20 °C

5 mvial

65

t-Butyloxycarbonyl-[(2S)-2-amino-4-(benzyloxycarbonyl)butanoyl] glycyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 707.77) C35H45N7O9 [73554-94-6]S. Iwanaga, T. Morita, H. Kato, T. Harada, N. Adachi, T. Sugo, I. Maruyama, K. Takada, T. Kimura, and S. Sakakibara, KINlNS-II: Biochemistry, Pathophysiology, and Clinical Aspects, (S. Fujii, H. Moriya, and T. Suzuki, Eds.), Plenum Publishing Co., 1979, p. 147-163.

Bz-Ala-OMeBenzoyl-l-alanine methyl ester (M.W. 207.23) C11H13NO3 [7244-67-9]

AA SAM-3084-20 °C

0.1 g1 g

25

Bz-Gly-Arg[Hippuryl-arginine]

Benzoyl-glycyl-l-arginine (M.W. 335.36) C15H21N5O4 [744-46-7]

AA SGR-3059-20 °C

0.1 g1 g

30125

Bz-Gly-Lys[Hippuryl-lysine]

Benzoylglycyl-l-lysine (M.W. 307.34) C15H21N3O4 [740-63-6]

AA SGK-3047-20 °C

0.1 g1 g

32145

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Calpain SubstratesCalpain is a calcium-activated cysteine protease that participates in membrane remodeling, apoptosis, and signal transduction. Deregulation of calpain activity has been linked with cell death and tissue damage associated with Alzheimer’s Disease, myocardial infarction, stroke, and brain trauma.Current calpain substrates are not optimal, and it has been difficult to determine the best cleavage sequence due to the broad substrate specificity of calpains. However, Cuerrier, et al. was able to employ a unique approach in which they designed and digested a N-terminal acetylated degenerate library to determine substrate specificity at primed positions for µ-calpain.1 Based on these findings, a second partially degenerate library was made to determine specificity at unprimed positions. The resulting FRET substrate, H-Glu(Edans)-Pro-Leu-Phe-Ala-Glu-Arg-Lys(Dabcyl)-OH (SFQ-3914-PI) is more sensitive to hydrolysis in com-parison to other substrates, including the popular SLY-MCA. It should prove more sensitive in measuring µ-calpain activity.1. D. Cuerrier, T. Moldoveanu, P.L. Davies, J. Biol. Chem., 280, 40632 (2005).

Boc-Val-Leu-Lys-MCAt-Butyloxycarbonyl-l-valyl-l-leucyl-l-lysine 4-methylcoumaryl-7-amide (M.W. 615.76) C32H49N5O7 [73554-84-4] Substrate for Plasmin and Calpain

A MVL-3104-v-20 °C

5 mgvial

75

H. Kato, N. Adachi, Y. Ohno, S. Iwanaga, K. Takada, and S. Sakakibara, J. Biochem., 88, 183 (1980). T. Sasaki, T. Kikuchi, N. Yumoto, N. Yoshimura, and T. Murachi, J. Biol. Chem., 259, 12489 (1984).

H-Glu(Edans)-Pro-Leu-Phe-Ala-Glu-Arg-Lys(Dabcyl)-OH

(Acetate Form)(M.W. 1488.74) C72H97N17O16SFRET Substrate for Calpain 1

SFQ-3914-PI -20 °C

1 mg 129

Suc-Ala-Leu-Pro-Phe-pNASuccinyl-l-alanyl-l-leucyl-l-prolyl-l-phenylalanine p-nitroanilide (M.W. 666.72) C33H42N6O9

A SAF-3162-v-20 °C

10 mgvial

130

Substrate for PPlase (Peptidyl-prolyl cis-trans Isomerase)J.L. Kofron, P. Kuzmic, V. Kishore, E. Colon-Bonilla, and D.H. Rich, Biochemistry, 30, 6127 (1991).

Suc-Leu-Leu-Val-Tyr-MCASuccinyl-l-leucyl-l-leucyl-l-valyl-l-tyrosine 4-methylcoumaryl-7-amide (M.W. 763.88) C40H53N5O10 [94367-21-2]

A MLL-3120-v-20 °C

5 mgvial

80

Substrate for Chymotrypsin, Ingensin / Proteasome, and CalpainH. Sawada, H. Yokasawa, M. Hoshi, and S. Ishii, Experientia, 39, 377 (1983). T. Sasaki, T. Kikuchi, N. Yumoto, N. Yoshimura, and T. Murachi, J. Biol. Chem., 259, 12849 (1984). S. Ishiura, M. Sano, K. Kamakura, and H. Sugita, FEBS Lett., 189, 119 (1985). T. Tsukahara, S. Ishiura, and H. Sugita, Eur. J. Biochem., 177, 261, (1988).

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Carboxypeptidase A SubstratesAc-Phe-Thiaphe-OH

N-Acetyl-l-phenylalanyl-l-3-thiaphenylalanineSTP-3621-PI

-20 °C

5 mg25 mg

95395

Dipeptide Mimetic Substrate for Carboxypeptidase A (M.W. 372.45) C19H20N2O4SP. Shamamian, S. Marcus, E. Deutsch, T. Maldonado, A. Liu, J. Stewart, K. Eng, and C. Gilvarg, Presented at the Annual Meeting of the Society for Surgery of the Alimentary Tract, May 1998. K.S. Brown, W.D. Kingsbury, N.M. Hall, G.L. Dunn, and C. Gilvarg, Anal. Biochem., 161, 219 (1987). S.Y. Hwang, W.D. Kingsbury, N.M. Hall, D.R. Jakas, G.L. Dunn, and C. Gilvarg, Anal. Biochem., 154, 552 (1986).

Carnosine Synthase Substrate See Code OAH-3085 β-Ala-His on page 214. Caspase Substrates(Asp-Glu-Val-Asp)2-Rh110(DEVD)2-Rh110

(M.W. 1515.48) C72H78N10O27 Substrate for Caspase 3 and Caspase 7

SDR-3775-PI-20 °C

1 mg 5 mg

27108

P.D. Sanchez-Gonzalez, et al., Toxicol. Lett, 203, 154 (2011).V. Gurtu, et al., Anal. Biochem, 251, 98 (1997).L.M. Martins, et al., J. Biol. Chem., 272, 7421 (1997).J Biol Chem., 275, 288(2000).Biochemistry, 38, 13906(1999).

Ac-Asp-Asn-Leu-Asp-MCA[Ac-DNLD-MCA]

Acetyl-L-aspartyl-L-asparaginyl-L-leucyl-L-aspartic-acid a-(4-methylcoumaryl-7-amide) (M.W. 674.66) C30H38N6O12 Synthetic Product

A MCA-3220-v-20 °C

5 mg vial

90

Selective Substrate for Caspase-3 Designed by in silico Screening SystemA. Yoshimori, R. Takasawa, and S. Tanuma, Bio. Pharm. Bull., 27, 968 (2004). • This compound is produced by Peptide Institute, Inc. under the license of Institute for Theoretical Medicine, Inc.

Ac-Asp-Gln-Thr-Asp-MCA[Ac-DQTD-MCA]

Acetyl-l-aspartyl-l-glutaminyl-l-threonyl-l-aspartic acid a-(4-methylcoumaryl-7-amide) (M.W. 676.63) C29H36N6O13 Substrate for Caspase-7/3

A MCA-3193-v-20 °C

5 mg vial

115

(Deduced from the Cleavage Site of Focal Adhesion Kinase and Gelsolin)L.-P. Wen, et al., Science, 278, 294 (1997).

Ac-Asp-Glu-Val-Asp-MCA[Ac-DEVD-MCA]

Acetyl-l-aspartyl-l-glutamyl-l-valyl-l-aspartic acid a-(4-methylcoumaryl-7-amide) (M.W. 675.64) C30H37N5O13 [169332-61-0] Substrate for Caspase-3/7/8

A SAP-3171-v-20 °C

5 mg vial

90

D.W. Nicholson, et al., Nature, 376, 37 (1995). N.A. Thornberry, et al., J. Biol. Chem., 272, 17907 (1997).

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Ac-Ile-Glu-Thr-Asp-MCA[Ac-IETD-MCA]

A MCA-3195-v-20 °C

5 mg vial

125

Acetyl-l-isoleucyl-l-glutamyl-l-threonyl-l-aspartic acid a-(4-methylcoumaryl-7-amide) (M.W. 675.68) C31H41N5O12 Substrate for Procaspase-3 Cleaving Enzyme (Caspase-8/6 and Granzyme-B) (Deduced from the Cleavage Site of Procaspase-3)N.A. Thornberry, et al., J. Biol. Chem., 272, 17907 (1997).

Ac-Leu-Glu-His-Asp-MCA[Ac-LEHD-MCA]

A MCA-3198-v-20 °C

5 mgvial

125

Acetyl-l-leucyl-l-glutamyl-l-histidyl-l-aspartic acid a- (4-methylcoumaryl-7-amide) (M.W. 711.72) C33H41N7O11 [292633-16-0] Substrate for Caspase-9

N.A. Thornberry, et al., J. Biol. Chem., 272, 17907 (1997).

Ac-Val-Asp-Val-Ala-Asp-MCA[Ac-VDVAD-MCA]

Acetyl-l-valyl-l-aspartyl-l-valyl-l-alanyl-l-aspartic acid a-(4-methylcoumaryl-7-amide) (M.W. 716.74) C33H44N6O12 Substrate for Caspase-2

A MCA-3203-v-20 °C

5 mgvial

125

R.V. Talanian, C. Quinlan, S. Trautz, M.C. Hackett, J.A. Mankovich, D. Banach, T. Ghayur, K.D. Brady, and W.W. Wong, J. Biol. Chem. 272, 9677 (1997).

Ac-Val-Glu-Ile-Asp-MCA[Ac-VEID-MCA]

Acetyl-l-valyl-l-glutamyl-l-isoleucyl-l-aspartic acid a-(4-methylcoumaryl-7-amide) (M.W. 673.71) C32H43N5O11 [219137-97-0] Substrate for Caspase-6

A MVA-3181-v-20 °C

5 mgvial

90

A. Takahashi, P.J. Goldschmidt-Clermont, E.S. Alnemri, T. Fernandes-Alnemri, K. Yoshizawa-Kumagaye, K. Nakajima, M. Sasada, G.G. Poirier, and W.C. Earnshaw, Exp. Cell Res., 231, 123 (1997). A. Takahashi, H. Hirata, S. Yonehara, Y. Imai, K.-K. Lee, R.W. Moyer, P.C. Turner, P.W. Mesner, T. Okazaki, H. Sawai, S. Kishi, K. Yamamoto, M. Okuma, and M. Sasada, Oncogene, 14, 2741 (1997).

Ac-Trp-Glu-His-Asp-MCA[Ac-WEHD-MCA]

Acetyl-l-tryptophyl-l-glutamyl-l-histidyl-l-aspartic acid a-(4-methylcoumaryl-7-amide) (M.W. 784.77) C38H40N8O11 [189275-74-9] Substrate for Caspase-1/

A MCA-3186-v-20 °C

5 mgvial

125

T.A. Rano, T. Timkey, E.P. Peterson, J. Rotonda, D.W. Nicholson, J.W. Becker, K.T. Chapman, and N.A. Thornberry, Chem. Biol., 4, 149 (1997). N.A. Thornberry, T.A. Rano, E.P. Peterson, D.M. Rasper, T. Timkey, M. Garcia-Calvo, V.M. Houtzager, P.A. Nordstrom, S. Roy, J.P. Vaillancourt, K.T. Chapman, and D.W. Nicholson, J. Biol. Chem., 272, 17907 (1997). J. Mikolajczyk, F.L. Scott, S. Krajewski, D.P. Sutherlin, and G.S. Salvesen, Biochemistry, 43, 10560 (2004).

Ac-Tyr-Val-Ala-Asp-MCA[Ac-yVAD-MCA]

A MAy-3161-v-20 °C

5 mg 5 mg

95

Acetyl-l-tyrosyl-l-valyl-l-alanyl-l-aspartic acid a-(4-methylcoumaryl-7-amide) (M.W. 665.69) C33H39N5O10 [149231-65-2] Substrate for Caspase-1N.A. Thornberry, et al., Nature, 356, 768 (1992).

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE MOCAc-Asp-Glu-Val-Asp-Ala-Pro-Lys(Dnp)-NH2 [MOCAc-DEVDAPK(Dnp)-NH2]

A MOC-3184-v-20 °C

1 mg vial

185

(7-Methoxycoumarin-4-yl) acetyl-l-aspartyl-l-glutamyl-l-valyl-l-aspartyl-l- alanyl-l-prolyl-[Ne-(2,4-dinitrophenyl)-l-lysine] amide (M.W. 1154.1) C50H63N11O21 Fluorescence-Quenching Substrate for Caspase-3 M. Enari, R.V. Talanian, W.W. Wong, and S. Nagata, Nature, 380, 723, (1996).

MOCAc-Tyr-Val-Ala-Asp-Ala-Pro-Lys(Dnp)-NH2 [MOCAc-yVADAPK(Dnp)-NH2]

A MOC-3183-v-20 °C

1 mg vial

185

(7-Methoxycoumarin-4-yl) acetyl-l-tyrosyl-l-valyl-l-alanyl-l-aspartyl-l- alanyl-l-prolyl-Ne-(2,4-dinitrophenyl)-l-lysine amide (M.W. 1144.1) C53H65N11O18 Fluorescence-Quenching Substrate for Caspase-1 M. Enari, R.V. Talanian, W.W. Wong, and S. Nagata, Nature, 380, 723, (1996).

(Z-Asp-Glu-Val-Asp)2-Rh110(Z-DEVD)2-Rh110

(M.W. 1515.48) C72H78N10O27Substrate for caspase 3 and caspase 7

SDR-3727-PI-20 °C

1 mg5 mg

27108

P.D. Sanchez-Gonzalez et al. Toxicol. Lett, 203, 154 (2011).V. Gurtu et al, anal. Biochem, 251, 98 (1997).L.M. Martins et al, J. Biol. Chem. 272, 7421 (1997).

Cathepsin and Thiol Protease SubstratesAbz-Glu-Pro-Phe-Trp-Glu-Asp-Gln-EDDnp[Abz-EPFWEDQ-EDDnp]

(Ammonium Form)

SFR-3231-v-20 °C

1 mg vial

125

2-Aminobenzoyl-l-glutamyl-l-prolyl-l-phenylalanyl-l-tryptophyl-l-glutamyl- l-aspartyl-l-glutamine 2-(2,4-dinitrophenyl)aminoethyl-amide(M.W. 1277.25) C59H68N14O19Fluorescence-Quenching Substrate for Human Neutrophil Cathepsin GS. Attucci, et al., Biochem. J., 366, 965 (2002).B. Korkmaz, et al., Nat. Protoc., 3, 991(2008).

Arg-MCA(Hydrochloride Form)l-arginine 4-methylcoumaryl-7-amide (M.W. 331.37) C16H21N5O3 [65286-27-3]Substrate for Cathepsin H

AA MAR-3113-v -20 °C

5 mg vial

50

Y. Kanaoka, T. Takahashi, H. Nakayama, K. Takada, T. Kimura, and S. Sakakibara, Chem. Pharm. Bull., 25, 3126 (1977).

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PRODUCT GRADE CODE QTy PRICE

Bz-l-Arg-pNA • HCI [l-BAPA]

AA SRN-3057-20 °C

0.1 g5 g

30115

Benzoyl-l-arginine p-nitroanilide monohydrochloride (M.W. 398.42 • 36.46) C19H22N6O4 • HCI [21653-40-7] Substrate for Trypsin-like Proteases and PapainK.A. Walsh, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds.), Academic Press, New York, 1970, pp. 41-63. R. Arnon, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds.), Academic Press, New York, 1970, pp. 226-244. G.A. Grant, A.Z. Eisen, and R.A. Bradshaw, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, ed.), Academic Press, New York, 1981, pp. 722-734.

Gly-Gly-Tyr-Arg • AcOH • 2H2OGlycyl-glycyl-l-tyrosyl-l-arginine

A OGG-3119-20 °C

0.1 g1 g

70350

(M.W. 451 • 60.05 • 36.03) C19H29N7O6 • CH3COOH • 2H2O [70195-20-9] Affinity Ligand for Papain M.O. Funk, Y. Nakagawa, J. Skochdopole, and E.T. Kaiser, Int. J. Peptide Protein Res., 13, 296 (1979).

MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-d-Arg-NH2

A SMO-3200-v-20 °C

1 mgvial

200

(7-Methoxycoumarin-4-yl) acetyl-glycyl-l-lysyl-l-Proyl-l-isoleucyl-l-Leucyl-l-phenylalanyl-l-phenylalanyl-l-arginyl-l-leucyl-[Ne-(2,4-dinitrophenyl)-l-lysyl]-d-arginine amide (M.W. 1756.0) C85H122N22O19 Fluorescence-Quenching Substrate for Cathepsin D/EY. Yasuda, T. Kageyama, A. Akamine, M. Shibata, E. Kominami, Y. Uchiyama, and K. Yamamoto, J. Biochem., 125, 1137 (1999).

MOCAc-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 See Code SMO-3670-PI on page 173.

MOCAc-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-d-Arg-NH2 [KyS-1]

(Trifluoroacetate Form)

A SMO-3225-v-20 °C

1 mgvial

135

7-Methoxycoumarin-4-yl) acetyl-glycyl-l-seryl-l-prolyl-l-alanyl-l-phenylalanyl-l- leucyl-l-alanyl-[Ne-(2,4-dinitrophenyl)-l-lysyl]-d-arginine amide (M.W. 1327.4) C61H82N16O18 Fluorescence-Quenching Substrate for Cathepsin E K. Yamamoto, Japanese Patent Publication No.2003-246798. • This compound is produced by Peptide Institute, Inc. under the license of Kyushu TLO Co., Ltd.

Pyr-Phe-Leu-pNAl-Pyroglutamyl-l-phenylalanyl-l-leucine-p-nitroanilide (M.W. 509.55) C26H31N5O6 [85901-57-1] Substrate for Thiol Protease

AA SPL-3130-20 °C

0.1 g1 g

55340

l.Y. Filippova, E.N. Lysogorskaya, E.S. Oksenoit, G.N. Rudenskaya, and V.M. Stepanov, Anal. Biochem., 143, 293 (1984).

Z-Arg-Arg-MCA(Hydrochloride Form)

A MRR-3123-v-20 °C

5 mg vial

55

Benzyloxycarbonyl-l-arginyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 621.69) C30H39N9O6 [88937-61-5] Substrate for Cathepsin BA.J. Barrett and H. Kirschke, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, Ed.), Academic Press, New York, 1981, pp. 535.

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Z-Gly-Pro-Arg-MCA

(Hydrochloride Form) AA MCA-3208-v

-20 °C

5 mgvial

65

Benzyloxycarbonylglycyl-l-prolyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 619.67) C31H37N7O7 [201928-42-9] Substrate for Cathepsin K

K. Aibe, H. Yazawa, K. Abe, K. Teramura, M. Kumegawa, H. Kawashima, and K. Honda, Biol. Pharm. Bull., 19, 1026 (1996). F. Bühling, A. Gerber, C. Häckel, S. Krüger, T. Köhnlein, D. Brömme, D. Reinhold, S. Ansorge, and T. Welte, Am. J. Respir. Cell Mol. Biol., 20, 612 (1999).

Z-Glu-TyrBenzyloxycarbonyl-l-glutamyl-l-tyrosine (M.W. 444.43) C22H24N2O8 [988-75-0]

AA SEy-3018-20 °C

0.1 g1 g

2575

Z-Leu-Arg-MCA(Hydrochloride Form)

AA MCA-3210-v-20 °C

5 mgvial

65

Benzyloxycarbonyl-l-leucyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 578.66) C30H38N6O6 Substrate for Cathepsin K/S/VD. Brömme, K. Okamoto, B.B. Wang, and S. Biroc, J. Biol. Chem., 271, 2126 (1996). D. Brömme, Z. Li, M. Barnes, and E. Mehler, Biochemistry, 38, 2377 (1999).

Z-Phe-Arg-MCA(Hydrochloride form)

AA MFR-3095-v-20 °C

5 mgvial

50

Benzyloxycarbonyl-l-phenylalanyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 612.68) C33H36N6O6 [65147-22-0] Substrate for Plasma Kallikrein, Cathespin B/L, and Arg-Gingipain

T. Morita, H. Kato, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, J. Biochem., 82, 1495 (1977). A.J. Barret, J. Biochem, 187, 909 (1980).

Z-Val-Val-Arg-MCA(Hydrochloride Form)

AA MCA-3211-v-20 °C

5 mgvial

75

Benzyloxycarbonyl-l-valyl-l-valyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 663.76) C34H45N7O7 Substrate for Cathepsin S/LD. Brömme, A. Steinert, S. Friebe, S. Fittkau, B. Wiederanders, and H. Kirschke, Biochem. J., 264, 475 (1989). H. Kirschke and B. Wiederanders, In, Proteolytic Enzymes: Serine and Cysteine Peptidases, Methods in Enzymology, Vol. 244, (A.J. Barret, Ed.), Academic Press, New York, 1994, pp. 500-511.

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Cellular Prion Protein SubstrateCellular prion protein (PrPc) in normal brains is found at the cell membrane where it is cleaved by ADAM10 and TACE between His111 and Met112 to produce a secreted N-terminal (N1) fragment. A recent study developed an original FRETS substrate, Abz-Thr-Asn-Met-Lys-His-Met-Ala-Gly-Ala-Ala-Gln-EDDnp (SFQ-3916-PI), that comprises PrPc amino acid sequence 107-116 and contains the His111-Met112 cleav-age site.1 Hydrolytic cleavage was successfully measured when this new substrate was incubated with brain homogenates and intact cells, and activity was attenuated by TACE and ADAM10 inhibitors. Substrate hydrolysis was also attenuated in cells defi-cient in ADAM10 and TACE while cells overexpressing ADAM10 and TACE exhibited enhanced substrate hydrolysis. However, TACE and ADAM10 only partially inhibited Prpc in these studies. Therefore, this novel substrate should prove helpful in identify-ing additional enzymes involved in normal PrPc metabolism.1. M.A. Cissé, C. Gandreuil, J.-F. Hernandez, J. Martinez, F. Checler, and B. Vincent, Biochem. and Biophys. Res. Commun., 347, 254 (2006).

Abz-Thr-Asn-Met-Lys-His-Met-Ala-Gly-Ala-Ala-Gln-EDDnp

(M.W. 1486.66) C61H91N21O19S2Fluorescence-Quenching Substrate for Cellular Prion Protein (PrPc)

SFQ-3916-PI -20 °C

1 mg5 mg

75285

Chymotrypsin and Chymotrypsin-like Protease SubstratesAc-Phe-OEt

Acetyl-l-phenylalanine ethyl ester (M.W. 235.28) C13H17NO3 [2361-96-8]

AA SFE-3006-20 °C

0.1 g1 g5 g

203060

Ac-Trp-OEtAcetyl-l-tryptophan ethyl ester (M.W. 274.32) C15H18N2O3 [2382-80-1]

AA SWE-30344 °C

0.1 g1 g

2255

Ac-Tyr-NH2Acetyl-l-tyrosine amide (M.W. 222.24) C11H14N2O3 [1948-71-6]

A SyA-3009-20 °C

0.1 g1 g

2540

Ac-Tyr-OEt • H2OAcetyl-l-tyrosine ethyl ester monohydrate

AA SyE-3008-20 °C

0.1 g1 g

2530

(M.W. 251.28 • 18.02) C13H17NO4 • H2O [840-97-1]] Substrate for Chymotrypsin and C1s

P.E. Wilcox, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds), Academic Press, New York, 1970, pp. 64-108. R.B. Sim, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, Ed.), Academic Press, New York, 1981, pp. 26-42.

Bz-Tyr-pNABenzoyl-l-tyrosine p-nitroanilide (M.W. 405.40) C22H19N3O5 [6154-45-6] Substrate for Chymotrypsin

A SyN-3015-20 °C

0.1 g1 g

32205

G.A. Grant, A.Z. Eisen, and R.A. Bradshaw, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, Ed.), Academic Press, New York, 1981, pp. 722-734.

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Bz-Tyr-OEt

Benzoyl-l-tyrosine ethyl ester (M.W. 313.35) C18H19NO4 [3483-82-7] Substrate for Chymotrypsin

AA SyE-3010-20 °C

0.1 g1 g

2030

P.E. Wilcox, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds.), Academic Press, New York, 1970, pp. 64-108.

Glt-Ala-Ala-Phe-MCAGlutaryl-l-alanyl-l-alanyl-l-phenylalanine 4-methylcoumaryl-7-amide (M.W. 578.61) C30H34N4O8 Substrate for Chymotrypsin

A MAF-3154-v-20 °C

5 mg vial

70

MeO-Suc-Arg-Pro-Tyr-MCA(Acetate Form) N-Methoxy-succinyl-l-arginyl-l-prolyl-l-tyrosine-4-methylcoumaryl-7-amide (M.W. 668.71) C35H43N7O9 Substrate for Chymotrypsin

SAP-3885-PI-20 °C

5 mg25 mg

95395

B.P. Berdal, O. Olsvik, S. Myhre, and T. Omland, J. Clin. Microb., 16, 452 (1982).

MeO-Suc-Arg-Pro-Tyr-pNAN-Methoxy-succinyl-l-arginyl-l-prolyl-l-tyrosine-p-nitroanilide (M.W. 705.35) C31H40N8O9 Substrate for Chymotrypsin

SAP-3882-PI-20 °C

5 mg25 mg

95395

B.P. Berdal, O. Olsvik, S. Myhre, and T. Omland, J. Clin. Microb., 16, 452 (1982).

Suc-Ala-Ala-Pro-Phe-MCASuccinyl-l-alanyl-l-alanyl-l-prolyl-l-phenylalanine 4-methylcoumaryl-7-amide (M.W. 661.70) C34H39N5O9 [88467-45-2] Substrate for Chymotrypsin

A MAA-3114-v-20 °C

5 mg vial

80

S. Sawada, H. Yokasawa, M. Hoshi and S. Ishii, Experientia, 39, 377 (1983).

Suc-Ala-Leu-Pro-Phe-pNA See Code MLL-3120-v on page 178.

Suc-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-MCA

A MRP-3110-v-20 °C

1 mg vial

70

Succinyl-l-arginyl-l-prolyl-l-phenylalanyl-l-histidyl-l-leucyl-l- leucyl-l-valyl-l-tyrosine 4-methylcoumaryl-7-amide (M.W. 1301.5) C66H88N14O14 [76524-84-0] Substrate for Renin and Proteinase AK. Murakami, T. Ohsawa, S. Hirose, K. Takada, and S. Sakakibara, Anal. Biochem., 110, 232 (1981). H. Yokosawa, H. Ito, S. Murata, and S. Ishii, Anal. Biochem., 134, 210 (1983).

Suc-lle-Ile-Trp-MCASuccinyl-l-isoleucyl-l-isoleucyl-l-tryptophan 4-methylcoumaryl-7-amide (M.W. 687.78) C37H45N5O8 [133525-12-9]

A MIW-3150-v-20 °C

5 mg vial

80

Page 42: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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PRODUCT GRADE CODE QTy PRICE

Coagulation Factor SubstratesBoc-Asp(OBzl)-Pro-Arg-MCA

t-Butyloxycarbonyl-[(2S)-2-amino-3-benzyloxy-carbonyl)propionyl]-l-prolyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 733.81) C37H47N7O9 [113866-00-5] Substrate for a-Thrombin

AA MDR-3139-v-20 °C

5 mgvial

65

S. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, Eur. J. Biochem., 172, 17 (1988).

Boc-Gln-Gly-Arg-MCAt-Butyloxycarbonyl-l-glutaminyl-glycyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 616.67) C28H40N8O8 Substrate for Factor Xlla

A MQR-3136-v-20 °C

5 mgvial

65

S. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, Eur. J. Biochem., 172, 17 (1988).

Boc-Glu(OBzl)-Ala-Arg-MCA AA MER-3134-v-20 °C

5 mgvial

65t-Butyloxycarbonyl-[(2S)-2-amino-4-(benzyloxycarbonyl)butanoyl]-l-alanyl-l-arginine4-methylcoumaryl-7-amide(M.W. 721.80) C36H47N7O9 [113866-16-3] Substrate for Factor XIaS. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, Eur. J. Biochem., 172, 17 (1988).

Boc-lle-Glu-Gly-Arg-MCAt-Butyloxycarbonyl-l-isoleucyl-l-glutamylglycyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 730.81) C34H50N8O10 [65147-06-0] Substrate for Factor Xa

A MlE-3094-v-20 °C

5 mgvial

70

T. Morita, H. Kato, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, J. Biochem., 82, 1495 (1977).

Boc-Leu-Ser-Thr-Arg-MCAt-Butyloxycarbonyl-l-leucyl-l-seryl-l-threonyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 732.82) C34H52N8O10 [73554-93-5] Substrate for Activated Protein C

A MLS-3112-v-20 °C

5 mgvial

75

Y. Ohno, H. Kato, T. Morita, S. Iwanaga, K. Takada, S. Sakakibara, and J. Stenflo, J. Biochem., 90, 1387 (1981).

Boc-Leu-Ser-Thr-Arg-pNA • AcOH • H2O

A SLR-3125-20 °C

25 mg100 mg

255690

t-Butyloxycarbonyl-l-leucyl-l-Seryl-l-threonyl-l-arginine p-nitroanilide (M.W. 695.76 • 60.05 • 18.02) C30H49N9O10 • CH3COOH • H2O Substrate for Activated Protein C

Boc-Leu-Thr-Arg-MCAt-Butyloxycarbonyl-l-leucyl-l-threonyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 645.75) C31H47N7O8Substrate for Factor VIIa-Tf

A MLT-3106-v-20 °C

5 mgvial

65

Y. Shigematsu, T. Miyata, S. Higashi, T. Miki, J.E. Sadler, and S. Iwanaga, J. Biol. Chem., 267, 21329 (1992).

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Boc-Val-Pro-Arg-MCA

t-Butyloxycarbonyl-l-valyl-l-prolyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 627.73) C31H45N7O7 [65147-04-8] Substrate for a-Thrombin

AA MVP-3093-v-20 °C

5 mgvial

65

T. Morita, H. Kato, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, J. Biochem., 82, 1495 (1977). S. Kawabata, T. Morita, S. Iwanaga, and H. Igarashi, J. Biochem., 97, 1073 (1985).

Z-Pyr-Gly-Arg-MCA(Hydrochloride Form)

A MPR-3138-v-20 °C

5 mgvial

70

Benzyloxycarbonyl-l-pyroglutamyl-glycyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 633.65) C31H35N7O8 Substrate for Factor Xa

S. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, Eur. J. Biochem., 172, 17 (1988).

Collagenase / MMP / Stromelysin SubstratesAlso see Code SDP-3818-PI Abz-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-Dap(Dnp)-NH2 on page 173 and Code SMO-3226-v MOCAc-Lys-Pro-Leu-Gly-Leu-A2pr(Dnp)-Ala-Arg-NH2 on page 173.

Dnp-Gln-Gly-Ile-Ala-Gly-Gln-d-Arg2,4-dinitrophenyl-l-glutaminyl-glycyl-l-isoleucyl-l-alanyl-glycyl-l-glutaminyl-d-arginine (M.W. 894.89 ) C35H54N14O14

B SDQ-3088-v-20 °C

2.5 mgvial

105

Reference Substrate for Collagenase Assay with code SDP-3087-vY. Masui, T. Takemoto, S. Sakakibara, H. Hori, and Y. Nagai, Biochem. Med., 17, 215 (1977).

Dnp-Gly-Pro-Leu-Gly-Met-Arg-Gly-Leu-NH2(Trifluoroacetate Form) 2,4-dinitrophenyl-glycyl-l-prolyl-l-leucyl-glycyl-l-methionyl-l-arginyl-glycyl-leucine amide (M.W. 965.11) C40H64N14O12S Substrate for Collagenase 3 / MMP-13

SDP-3816-PI-20 °C

1 mg5 mg

45175

S.J. Deng, D.M. Bickett, J.L. Mitchell, M.H. Lambert, R.K. Blackburn, H.L. Carter, III, J. Neugebauer, G. Pahel, M.P. Weiner, M.L. Moss, J. Biol. Chem., 275, 31422-31427 (2000).

Dnp-Pro-Cha-Gly-Cys(Me)-His-Ala- Lys(NMa)-NH2

2,4-dinitrophenyl-l-prolyl-l-cyclohexylalanyl-glycyl-S-methyl-l-cysteinyl-l-histidyl-l-alanyl-Ne-methylanthranoyl-l-lysine amide (M.W. 1077.24) C49H68N14O12S Substrate for Collagenase

SDP-3815-PI-20 °C

2.5 mg5 mg

165275

J. Berman, M. Green, E. Sugg, R. Anderegg, D.S. Millington, D.L. Norwood, J. McGeehan and J. Wiseman, J. Biol. Chem., 267, 1434 (1992).

Dnp-Pro-Gln-Gly2,4-dinitrophenyl-l-prolyl-l-glutaminyl-glycine (M.W. 466.40) C18H22N6O9 [65080-33-3]

AA SDP-3089-20 °C

0.1 g1 g

85495

Reference Compound to Measure Collagenase Activity with SDP-3087-v

Dnp-Pro-Leu-Gly2,4-dinitrophenyl-l-prolyl-l-leucylglycine (M.W. 451.43) C19H25N5O8

AA SDP-3082-20 °C

0.1 g1 g

60360

Reference Compound to Measure Collagenase Activity with SDP-3073-v

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184 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT GRADE CODE QTy PRICE

Dnp-Pro-Leu-Gly-Leu-Trp-Ala-d-Arg-NH22,4-dinitrophenyl-l-prolyl-l-leucylglycyl-l-leucyl-l-tryptophyl-l-alanyl-d-arginine amide (M.W. 977.10) C45H64N14O11 Substrate for Collagenase/Gelatinase

SDP-3820-PI-20 °C

2.5 mg5 mg

95175

M.S. Stack and R.D. Gray, J. Biol. Chem., 264, 4277 (1989). K. Darlak, R.B. Miller, M.S. Stack, A.F. Spatola, and R.D. Gray, J. Biol. Chem., 265, 5199 (1990).

Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-d-Arg

2,4-dinitrophenyl-l-prolyl-l-glutaminylglycyl-l-lsoleucyl-l-alanyl-glycyl-l-glutaminyl-d-arginine (M.W. 992.00) C40H61N15O15 [63014-08-4] Substrate for Animal Collagenase

B SDP-3087-v-20 °C

2.5 mg via

110

Y. Masui, T. Takemoto, S. Sakakibara, H. Hori, and Y. Nagai, Biochem. Med., 17, 215 (1977).

Dnp-Pro-Leu-Gly-Ile-Ala-Gly-Arg-NH2

2,4-dinitrophenyl-l-prolyl-l-leucylglycyl-l-isoleucyl-l-alanyl-glycyl-l-arginine amide (M.W. 847.92) C36H57N13O11 Substrate for Animal Collagenase

A SDP-3073-v-20 °C

2.5 mg vial

99

Y. Masui, T. Takemoto, S. Sakakibara, H. Hori, and Y. Nagai, Biochem. Med., 17, 215 (1977).

MOCAc-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 See Code SMO-3670-PI on page 173.MOCAc-Lys-Pro-Leu-Gly-Leu-A2pr(Dnp)-Ala-Arg-NH2 See Code SMO-3226-v on page 173.

MOCAc-Pro-Cha-Gly-Nva-His-Ala-Dap(Dnp)-NH2.

SMO-3682-PI-20 °C

1 mg 65

(7-Methoxycoumarin-4-yl)acetyl-l-prolyl-l-cyclohexylalanyl-glycyl-l-norvalyl- l-histidinyl-l-alanyl-Nb-(2,4-dinitrophenyl)-l-2,3-diaminopropionic amide (M.W. 1100.16) C51H65N13O15 Fluorescence-Quenching Substrate for MMP 13J.L. Lauer-Fields, T. Broder, T. Sritharan, L. Chung, H. Nagase, and G.B. Fields, Biochemistry, 40, 5795 (2001)

MOCAc-Pro-Leu-Gly-Leu-A2pr(Dnp)-Ala-Arg-NH2

A MOC-3163-v-20 °C

1 mgvial

75

(7-Methoxycoumarin-4-yl) acetyl-l-prolyl-l-leucyl-glycyl-l-leucyl-[Nb- (2,4-dinitrophenyl)-l-2,3-diaminopropionyl]-l-alanyl-l-arginine amide (M.W. 1093.1) C49H68N14O15 [140430-53-1] Fluorescence-Quenching Substrate for Matrix MetalloproteinasesC.G. Knight, F. Willenbrock, and G. Murphy, FEBS Lett., 296, 263 (1992).

MOCAc-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 [NFF-3]

B SMO-3168-v-20 °C

1 mgvial

125

(7-Methoxycoumarin-4-yl) acetyl-l-arginyl-l-prolyl-l-lysyl-l-prolyl-l-valyl-l-glutamyl-l- norvalyl-l-tryptophyl-l-arginyl-[Ne-(2,4-dinitrophenyl)-l-lysine] amide (M.W. 1675.8) C78H110N22O20 [158584-09-9] Fluorescence-Quenching Substrate for Matrix Metalloproteinase-3 (Stromelysin 1)H. Nagase, C.G. Fields, and G.B. Fields, J. Biol. Chem., 269, 20952 (1994). • This product is sold under license with the University of Minnesota.

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE MOCAc-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys(Dnp)-NH2 [NFF-2]

B SMO-3167-v-20 °C

1 mgvial

125

(7-Methoxycoumarin-4-yl) acetyl-l-arginyl-l-prolyl-l-lysyl-l-prolyl-l-tyrosyl-l-alanyl-l-norvalyl-l- tryptophyl-l-methionyl-[Ne-(2,4-dinitrophenyl)-l-lysine] amide (M.W. 1656.9) C79H105N19O19S [158584-08-8] Fluorescence-Quenching Substrate for Matrix MetalloproteinasesH. Nagase, C.G. Fields, and G.B. Fields, J. Biol. Chem., 269, 20952 (1994). • This product is sold under license with the University of Minnesota.

Suc-Gly-Pro-Leu-Gly-Pro-MCASuccinyl-glycyl-l-prolyl-l-leucyl-glycyl-l-proline 4-methylcoumaryl-7-amide (M.W. 696.75) C34H44N6O10 [72698-36-3] Substrate for Collagenase-like Peptidase

A MGP-3108-v-20 °C

5 mgvial

75

K. Kojima, H. Kinoshita, T. Kato, T. Nagatsu, K. Takada, and S. Sakakibara, Anal. Biochem., 100, 43 (1979).

Z-Gly-Pro-Leu-Gly-Pro • H2O • AcOEtBenzyloxycarbonylglycyl-l-prolyl-l-leucyl-glycyl-l-proline • monohydrate mono (ethyl acetate)

AA SGP-3029-20 °C

0.1 g1 g

90625

(M.W. 573.64 • 18.02 • 88.11) C28H39N5O8 • H2O • CH3COOC2H5 [2646-61-9] Crystalline: Substrate for Bacterial CollagenaseY. Nagai, S. Sakakibara, H. Noda, and S. Akabori, Biochim. Biophys. Acta., 37, 567 (1960).

Z-Phe-Tyr-LeuBenzyloxycarbonyl-l-phenylalanyl-l-tyrosyl-l-leucine (M.W. 575.65) C32H37N3O7 Substrate for Metalloproteinase

AA SFL-3131-20 °C

0.1 g1 g

40160

Deformylase Substrates4-Methoxyphenylazoformyl-Phe [AAFP]

(Potassium Form) N-(4-Methoxyphenylazoformyl)-l-phenylalanine (M.W. 327.33) C17H17N3O4 [396717-86-5] Substrate for Carboxypeptidase A

B SAA-3197-v-20 °C

5 mgvial

40

W.L. Mock, Y. Liu, and D.J. Stanford, Anal. Biochem., 239, 218 (1996).

For-Met-Leu-pNAN-Formyl-l-methionyl-l-leucine p-nitroanilide (M.W. 410.50) C18H26N4O5SY. Wei and D. Pei, Anal. Biochem., 250, 29 (1997).

SFM-3624-PI-20 °C

5 mg25 mg

80295

Dengue Fever Virus Protein SubstratesAbz-Lys-Lys-Gln-Arg-Ala-Gly-Val-Leu-Tyr(NO2)-NH2

Abz-KKQRAGVLY(NO2)-NH2(M.W. 1225.43) C55H88N18O14

SFQ-3958-PI -20 °C

1 mg5 mg

45195

Substrate for for Dengue Virus Non-Structural Protein 3 (NS3) Serine ProteaseP. Niyomrattanakit, S. Yahorava, I. Mutule, F. Muturlis, R. Petrovska, P. Prusis, G. Katzenmeier, and J.E.S. Wikberg, Biochem. J., 397, 203-211 (2006).

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186 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT GRADE CODE QTy PRICE

Benzoyl-Nle-Lys-Arg-Arg-MCA (M.W.. 833.01) C41H60N12O7Dengue Fever Virus Protein Substrate

MCA-3923-PI -20 °C

5 mg 95

J. Li, et al., J. Biol. Chem., 280, 28766 (2005).

Dengue Virus Non-Structural Protein 3 (NS3) Serine Protease SubstrateAbz-Arg-Arg-Arg-Arg-Ser-Ala-Gly-Tyr(NO2)-NH2

(M.W. 1184.30) C48H77N23O13Substrate for NS3 Serine Protease

SFQ-3957-PI -20 °C

1 mg5 mg

45195

Dipeptidyl-Amino Peptidase SubstratesGly-Pro-MCA

(Tosylate Form)AA MGP-3090-v

-20 °C

5 mgvial

40

Glycyl-l-proline 4-methylcoumaryl-7-amide (M.W. 329.35) C17H19N3O4 [67341-42-8] Substrate for X-prolyl Dipeptidyl-Aminopeptidase

T. Kato, T. Nagatsu, T. Kimura, and S. Sakakibara, Biochem. Med., 19, 351 (1978).

Gly-Pro-pNA • Tos [GPNT]

Glycyl-l-proline p-nitroanilide monotosylate

AA SGP-3074-v-20 °C

10 mg vial

32

(M.W. 292.29 • 172.20) C13H16N4O4 • C7H8O3S [65096-46-0] Substrate for X-prolyl Dipeptidyl-Aminopeptidase

T. Nagatsu, et al., Anal. Biochem., 74, 466 (1976). K. Fujita, M. Hirano, J. Ochiai, M.M. Funabashi, I. Nagatsu, T. Nagatsu and S. Sakakibara, Clin. Chim. Acta, 88, 15 (1978).

Lys-Ala-MCA(Tartarate Form) l-Lysyl-l-alanine 4-methylcoumaryl-7-amide (M.W. 374.43) C19H26N4O4 Substrate for Dipeptidyl-Aminopeptidase II

A MKA-3124-v-20 °C

5 mgvial

50

D. Mantle, M.F. Hardy, B. Lauffart, J.R. McDermott, A.I. Smith, and R.J.T. Pennington, Biochem. J., 211, 567 (1983).

Elastase SubstratesAbz-Ala-Pro-Glu-Glu-Ile-Met-Arg-Arg-Gln-EDDnp

[Abz-APEEIMRRQ-EDDnp](Trifluoroacetate Form)

SNE-3230-v-20 °C

1 mgvial

110

2-Aminobenzoyl-l-alanyl-l-prolyl-l-glutamyl-l-glutamyl-l-isoleucyl-l-methionyl-l-arginyl-l-arginyl-l-glutamine 2-(2,4-dinitrophenyl)aminoethylamide(M.W. 1456.59) C61H93N21O19SFluorescence-Quenching Substrate for Human Neutrophil ElastaseB. Korkmaz, S. Attucci, T. Moreau, E. Godat, L. Juliano, and F. Gauthier, Am. J. Respir. Cell Mol. Biol., 30, 801 (2004).B. Korkmaz, S. Attucci, M.A. Juliano, T. Kalupov, M.-L. Jourdan, L. Juliano, and F. Gauthier, Nat. Protoc., 3, 991 (2008).

Glt-Ala-Ala-Pro-Leu-pNA • H2OGlutaryl-l-alanyl-l-alanyl-l-prolyl-l-leucine-p-nitroanilide (M.W. 604.65 • 18.02) C28H40N6O9 • H2O Substrate for Pancreatic Elastase

AA SGL-3129-20 °C

0.1 g1 g

90625

E.G. Del Mar, C. Largman, J.W. Brodrick, M. Fassett, and M.C. Geokas, Biochemistry, 19, 468 (1980).

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Pyr-Pro-Val-pNA

l-Pyroglutamyl-l-prolyl-l-valine p-nitroanilide (M.W. 445.47) C21H27N5O6 [83329-36-3]

SAP-3228-v-20 °C

5 mg vial

75

Selective Substrate for Human Granulocyte Elastase J.A. Kramps, Ch. van Twisk and A.C. van der Linden, Scand. J. Clin. Lab. Investig., 43, 427 (1983).L. Persson, J. Bergström, H. Ito, and A. Gustafsson, J. Periodontol., 72, 90 (2001).I. Groth and S. Alban, Planta Med., 74, 852 (2008).

Suc-Ala-Ala-Ala-MCASuccinyl-l-alanyl-l-alanyl-l-alanine 4-methyl-coumaryl-7-amide (M.W. 488.49) C23H28N4O8 [73617-90-0] Substrate for Elastase

AA MAA-3133-v-20 °C

5 mg vial

75

R.A. Mumford, et. al., J. Biol. Chem., 255, 2227 (1980).

Suc-Ala-Ala-Ala-pNA [STANA]

Succinyl-l-alanyl-l-alanyl-l-alanine p-nitroan-ilide (M.W. 451.43) C19H25N5O8 [52299-14-6]

AA SAA-3071-v-20 °C

5 mg vial

25

Suc-Ala-Ala-Ala-pNA (Bulk) [STANA]

Succinyl-l-alanyl-l-alanyl-l-alanine-p-Nitroanilide (M.W. 451.43) C19H25N5O8 [52299-14-6] Substrate for Elastase

AA SAA-3071-20 °C

0.1 g1 g

50300

J. Bieth, B. Spiess, and C.G. Wermuth, Biochem. Med., 11, 350 (1974).

Suc(OMe)-Ala-Ala-Pro-Val-MCAN-Methoxysuccinyl-l-alanyl-l alanyl-l-prolyl-l-valine 4-methylcoumaryl-7-amide (M.W. 627.69) C31H41N5O9 [72252-90-5]

AA MAV-3153-v-20 °C

5 mg vial

80

Substrate for Human Leukocyte / Porcine Pancreatic ElastaseM.J. Castrillo, K. Nakajima, M. Zimmerman, and J.C. Powers, Anal. Biochem., 99, 53 (1979).

Suc-Ala-Ala-Pro-Abu-pNA(M.W. 562.58) C25H34N6O9 Substrate for Pancreatic Elastase

SAP-3667-PI-20 °C

5 mg25 mg

49195

C.L. Largman, Biochemistry, 22, 3763 (1983). E.G. Del Mar, C. Largman, J.W. Brodick, M. Fassett, and M.C. Geokas, Biochemistry, 19, 468 (1980).

Suc-Ala-Ala-Pro-Gly-pNA(M.W. 534.53) C23H30N6O9 Substrate for Pancreatic Elastase

SAP-3666-PI-20 °C

5 mg25 mg

49195

C.L. Largman, Biochemistry, 22, 3763 (1983). E.G. Del Mar, C. Largman, J.W. Brodick, M. Fassett, and M.C. Geokas, Biochemistry, 19, 468 (1980).

Suc-Ala-Ala-Pro-Trp-pNA (M.W. 663.69) C32H37N7O9 Substrate for Pancreatic Elastase

SAP-3668-PI-20 °C

5 mg25 mg

49195

C.L. Largman, Biochemistry, 22, 3763 (1983). E.G. Del Mar, C. Largman, J.W. Brodick, M. Fassett, and M.C. Geokas, Biochemistry, 19, 468 (1980).

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188 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT GRADE CODE QTy PRICE

Suc-Ala-Pro-Ala-MCASuccinyl-l-alanyl-l-prolyl-l-alanine 4-methyl-coumaryl-7-amide (M.W. 514.53) C25H30N4O8 [88467-44-1] Substrate for Elastase

A MAP-3100-v-20 °C

5 mg vial

80

G. Oshima, K. Akashi, and M. Yamada, Arch. Biochem. Biophys, 233, 212 (1984).

Suc-Ala-Pro-Ala-pNASuccinyl-l-alanyl-l-prolyl-l-alanine p-nitroanilide (M.W. 477.47) C21H27N5O8 Substrate for Elastase

AA SAP-3118-20 °C

0.1 g1 g

55340

Furin and Carboxyl Side of Paired Basic Residue Cleaving Enzyme SubstratesBoc-Gln-Arg-Arg-MCA

t-Butyloxycarbonyl-l-glutaminyl-l-arginyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 715.80) C32H49N11O8 [109376-05-8]

A MQR-3122-v-20 °C

5 mg vial

70

Substrate for Carboxyl Side of Paired Basic Residue Cleaving EnzymeK. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun., 144, 807 (1987).

Pyr-Arg-Thr-Lys-Arg-MCAl-Pyroglutamyl-l-arginyl-l-threonyl-l-lysyl- l-arginine 4-methylcoumaryl-7-amide (M.W. 827.93) C37H57N13O9 [155575-02-3] Substrate for Furin

A MPR-3159-v-20 °C

5 mg vial

85

K. Hatsuzawa, M. Nagahama, S. Takahashi, K. Takada, K. Murakami, and K. Nakayama, J. Biol. Chem., 267, 16094 (1992).

Boc-Arg-Val-Arg-Arg-MCA A MRR-3155-v-20 °C

5 mg vial

85t-Butyloxycarbonyl-l-arginyl-l-valyl-l-arginyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 842.99) C38H62N14O8 Substrate for FurinK. Hatsuzawa, K. Murakami, and K. Nakayama, J. Biochem., 111, 296 (1992). K. Hatsuzawa, M. Nagahara, S. Takahashi, K. Takada, K. Murakami, and K. Nakayama, J. Biol. Chem., 267, 16094, (1992).

Boc-Gly-Arg-Arg-MCAt-Butyloxycarbonyl-glycyl-l-arginyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 644.72) C29H44N10O7 [113866-14-1]

A MGR-3142-v-20 °C

5 mg vial

70

Substrate for Carboxyl Side of Paired Basic Residue Cleaving EnzymeK. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res Commun., 144, 807 (1987).

Boc-Gly-Lys-Arg-MCAt-Butyloxycarbonyl-glycyl-l-lysyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 616.71) C29H44N8O7 [109358-48-7]

A MGK-3143-v-20 °C

5 mg vial

70

Substrate for Carboxyl Side of Paired Basic Residue Cleaving EnzymeK. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun., 144, 807 (1987).

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Boc-Leu-Arg-Arg-MCA

t-Butyloxycarbonyl-l-leucyl-l-arginyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 700.83) C33H52N10O7

A MLR-3140-v-20 °C

5 mg vial

70

Substrate for Carboxyl Side of Paired Basic Residue Cleaving Enzyme and ProteasomeK. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun., 144, 807 (1987). M. Aki, N. Shimbara, M. Takashina, K. Akiyama, S. Kagawa, T. Tamura, N. Tanahashi, T. Yoshimura, K. Tanaka, and A. Ichihara, J. Biochem., 115, 257 (1994).

Boc-Leu-Lys-Arg-MCAt-Butyloxycarbonyl-l-leucyl-l-lysyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 672.82) C33H52N8O7 [109358-47-6]

A MLK-3141-v-20 °C

5 mg vial

70

Substrate for Carboxyl Side of Paired Basic Residue Cleaving EnzymeK. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun., 144, 807 (1987).

GDP-l-Fuc Substrates See Code SGS-23004-s on page 228.

Gingipain SubstratesBoc-Phe-Ser-Arg-MCA

t-Butyloxycarbonyl-l-phenylalanyl-l-seryl-l-arginine 4-methylcoumaryl-7-amide (M.W. 665.74) C33H43N7O8 [73554-90-2]

AA MFS-3107-v-20 °C

5 mg vial

65

Substrate for Trypsin, Tryptase, 73K Protease, and Arg-GingipainS. Iwanaga, T. Morita, H. Kato, T. Harada, N. Adachi, T. Sugo, I. Maruyama, K. Takada, T. Kimura and S. Sakakibara, KININS-II: Biochemistry, Pathophysiology, and Clinical Aspects, (S. Fujii, H. Moriya and T. Suzuki, eds.), Plenum Publishing Co., 1979. pp. 147-163. M. Muramatsu, T. Itoh, M. Takei, and K. Endo, Biol. Chem. Hoppe-Seyler, 369, 617, (1988). A. Molla, T. Yamamoto, and H. Maeda, J. Biochem., 104, 616 (1988).

Z-His-Glu-Lys-MCA(Hydrochloride Form)

AA MCA-3215-v-20 °C

5 mg vial

80

Benzyloxycarbonyl-L-histidyl-L-glutamyl-L-lysine 4-methylcoumaryl-7-amide (M.W. 703.74) C35H41N7O9 Substrate for Lys-GingipainN. Abe, A. Baba, T. Kadowaki, K. Okamoto, S. Okazaki, T. Asao, and K. Yamamoto, J. Biochem., 128, 877 (2000).

Z-Phe-Arg-MCA See Code MFR-3095-v on page 183.

Glu-Glul-glutamyl-l-glutamic acid (M.W. 276.24) C10H16N2O7 [3929-61-1]

A OEE-3080-20 °C

0.1 g1 g

40200

Glu-pNA • H2Ol-Glutamic acid a-p-nitroanilide (M.W. 267.24 • 18.02) C11H13N3O5 • H2O

A SEN-3067-20 °C

0.1 g1 g

3090

Glu(Cys-Gly) [Glutathione; GSH]

g-l-glutamyl-l-cysteinylglycine (M.W. 307.32) C10H17N3O6S [70-18-8]

B OEG-3050-20 °C

1 g5 g

25 g

223570

Glutathione See Code OEG-3050 Glu(Cys-Gly) above.

Page 50: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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190 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT GRADE CODE QTy PRICE

Gly-GlyGlycylglycine (M.W. 132.12) C4H8N2O3 [556-50-3]

AA OGG-3028-20 °C

5 g25 g

100 g

253570

Gly-Gly-GlyGlycylglycylglycine (M.W. 189.17) C6H11N3O4 [556-33-2]

AA OGG-3061-20 °C

1 g5 g

25 g

3080

315

Gly-Gly-HisGlycylglycyl-l-histidine (M.W. 269.26) C10H15N5O4 [93404-95-6] Cu-Binding Peptide

A OGH-3076-20 °C

0.1 g1 g

50350

S. Lau, T.P.A. Kruch, and B. Sarkar, J. Biol. Chem., 249, 5878 (1974).

Gly-LeuGlycyl-l-leucine (M.W. 188.22) C8H16N2O3 [869-19-2]

AA OGL-3022-20 °C

0.1 g1 g5 g

2540

105

Gly-PheGlycyl-l-phenylalanine (M.W. 222.24) C11H14N2O3 [3321-03-7]

AA OGF-3053-20 °C

0.1 g1 g

2240

Gly-Phe-NH2 • AcOHGlycyl-l-phenylalanine amide (M.W. 221.26 • 60.05) C11H15N3O2 • CH3COOH [13467-26-0]

AA OGF-3023-20 °C

0.1 g1 g

3080

Gly-ProGlycyl-l-proline (M.W. 172.18) C7H12N2O3 [704-15-4]

AA OGP-3052-20 °C

0.1 g1 g

3060

GPNT See Code SGP-3074-v Glycyl-l-proline p-Nitroanilide • Tosylate on page 190.

γ-Glutamyl Trans-peptidase SubstrateGlu(pNA) • H2O

l-Glutamic acid g-p-nitroanilide (M.W. 267.24 • 18.02) C11H13N3O5 • H2O [122864-94-2] Substrate for g-Glutamyl Transpeptidase

A SEN-3066-20 °C

0.1 g1 g5 g

2555

205

Glycogen Synthase Kinase 3B Substrates[Ala353,357]-Presenilin 1 (349-361)

H-Gly-Pro-His-Arg-Ala-Thr-Pro-Glu-Ala-Arg-Ala-Ala-Val-OH (M.W. 1332.50) C56H93N21O17

SPR-3630-PI-20 °C

1 mg 59

Negative Control of Glycogen Synthase Kinase-3b SubstrateF. Kirschenbaum, S.-C. Hsu, B. Cordell, and J.V. McCarthy, J. Biol. Chem., 276, 7366-7375 (2000).

Presenilin 1 (349-361)H-Gly-Pro-His-Arg-Ser-Thr-Pro-Glu-Ser-Arg-Ala-Ala-Val-OH (M.W. 1364.49) C56H93N21O19

SPR-3629-PI-20 °C

1 mg 59

Glycogen Synthase Kinase-3b Substrate (GSK-3b Substrate)F. Kirschenbaum, S.-C. Hsu, B. Cordell, and J.V. McCarthy, J. Biol. Chem., 276, 7366-7375 (2000).

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE

Hepatitis C Protease SubstrateAc-Asp-Glu-Asp(Edans)-Glu-Glu-Abu-l-Lactoyl-Ser-Lys(Dabcyl)-NH2

(M.W. 1548.62) C68H89N15O25S [188530-20-3]FRET Substrate for Hepatitis C proteaseC. Lin, et al., J. Biol. Chem., 10, 1074 (2004).N. Kakiuchi, et al., J. Virol. Methods, 80, 77 (1999).Y. Liu, et al., Anal. Biochem., 267, 331 (1999).M. Taliani, et al., Anal. Biochem., 240, 60 (1996).

SFQ-3730-PI-20 °C

1 mg5 mg

4121648

Hepatocyte Growth Factor-Activator (HGF-A) SubstrateAc-Lys-Thr-Lys-Gln-Leu-Arg-MCA[Ac-KTKQLR-MCA]

Acetyl-l-lysyl-l-threonyl-l-lysyl-l-glutaminyl-l-leucyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 972.14) C45H73N13O11

AA MCA-3185-v-20 °C

5 mg vial

150

Substrate for Hepatocyte Growth Factor-Activator (HGF-A)K. Mizuno, Y. Tanoue, I. Okano, T. Harano, K. Takada, and T. Nakamura, Biochem. Biophys. Res. Commun., 198, 1161 (1994).

Hippuryl-alanyl-proline See Code SGP-3126 Bz-Gly-Ala-Pro on page 176.Hippuryl-arginine See Code SGR-3059 Benzoyl-glycyl-l-arginine on page 177.Hippuryl-glycyl-glycine See Code SGG-3128 Bz-Gly-Gly-Gly on page 176.Hippuryl-histidyl-leucine See Code SGL-3064 Benzoyl-glycyl-l-histidyl-l-leucine on page 176.Hippuryl-lysine See Code SGK-3047 Benzoyl-glycyl-l-lysine on page 177.

His-Leul-histidyl-l-leucine (M.W. 268.31) C12H20N4O3 [7763-65-7]

AA OHL-3065-20 °C

0.1 g1 g

30105

Histone Deacetylase SubstratesAc-Arg-Gly-Lys(Ac)-MCAAc-RGK(Ac)-MCA

(Trifluoroacetate Form) (M.W. 600.68) C28H40N8O7 [660846-97-9] Substrate for Histone Deacetylase D. Wegener, et al., Chem. Biol., 10, 61 (2003).

SRK-3728-PI -20 °C

1 mg5 mg

100400

Ac-Arg-Gly-Lys-MCAAc-RGK-MCA

(Trifluoroacetate Form) (M.W. 558.64) C26H38N8O6 [660846-99-1] Substrate for Histone Deacetylase D. Wegener, et al., Chem. Biol., 10, 61 (2003).

SHD-3748-PI -20 °C

1 mg5 mg

30120

Boc-Lys(TFA)-MCA(M.W. 499.49) C23H28F3N3O6 [97885-44-4] Substrate for Histone Deacetylase D. Riester, et al., Biochem. Biophys. Res. Commun., 324, 1116 (2004).A . Lahm, et al., Proc. Natl. Acad. Sci. U.S.A., 104, 17335 (2004).

SKT-3750-PI -20 °C

25 mg50 mg

100 mg

78120200

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PRODUCT GRADE CODE QTy PRICE

HIV-1 Protease SubstratesDabcyl-γ-Abu-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-Edans

(Trifluoroacetate Form)

SFQ-3763-PI-20 °C

1 mg5 mg

240960

(M.W. 1532.75) C73H97N17O18S [127134-13-8]FRET Substrate for HIV ProteaseE.D.Matayoshi, et al., Science, 247, 954 (1990)M.W. Pennington, et al., Peptides 1992, Proceedings of the 22nd European Peptide Symposium, Interlaken, Switzerland, p. 936, (C.H.Schneider and A.N.Eberle, eds.) Escom, Leiden, (1993)U. Nillroth, et al., Antimicrob. Agents Chemother., 41, 2383 (1997)L.Bannwarth, et al., J. Med. Chem., 49, 4657 (2006)

Ser-Gln-Asn-Tyr-Pro-Ile-Val(M.W. 819.90) C37H57N9O12 Substrate for HIV-1 Protease

AA SSV-4236-v

-20 °C

5 mg vial

175

S. Billich, M.-T. Knoop, J. Hansen, P. Strop, J. Sedlacek, R. Mertz, and K. Moeliling, J. Biol. Chem., 263, 17905 (1988). P.L. Darke, R.F. Nutt, S.F. Brady, V.M. Garsky, T.M. Ciccarone, C.-T. Leu, P.K. Lumma, R.M. Freidinger, D.F. Veber, and I.S. Sigal, Biochem. Biophys. Res. Commun., 156, 297 (1988). P.L. Darke, et al., J. Biol. Chem., 264, 2307 (1989).

Horseshoe Crab Clotting Enzyme SubstrateBoc-Leu-Gly-Arg-MCA

(Hydrochloride Form) t-Butyloxycarbonyl-l-leucyl-glycyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 601.69) C29H43N7O7 [65147-09-3] Substrate for Horseshoe Crab Clotting Enzyme

AA MLG-3102-v-20 °C

5 mg vial

65

S. Iwanaga, T. Morita, T.Harada, S. Nakamura, M. Niwa, K. Takada, T. Kimura and S. Sakakibara, Haemostasis, 7, 183 (1978).

Human Rhino-virus-14 (HRV)3C Protease SubstrateSuc-Glu-Ala-Leu-Phe-Gln-pNA

Succinyl-l-glutamyl-l-alanyl-l-leucyl-l- phenylalanyl-l-Glutamine p-Nitroanilide (M.W. 826.87) C38H50N8O13 Substrate for 3C Human Rhinovirus-14 (HRV14)

SAP-3693-PI-20 °C

5 mg25 mg

49195

Q. M. Wang, R.B. Johnson, G.A. Cox, E.C. Villarreal, and R.J. Loncharich, Anal. Biochem., 252, 238 (1997). Q.M. Wang, R.B. Johnson, L.N. Jungheim, J.D. Cohen, and E.C. Villarreal, Antimicrobial Agents and Chemot., 42, 916 (1998).

Kallikrein SubstratesH-D-Val-Leu-Arg-AFC

(M.W. 597.64) C27H38F3N7O5 Fluorogenic Substrate for Kallikrein

SFC-3774-PI-20 °C

1 mg5 mg

40160

DK Shori, et al., Biochem. Pharmacol., 43, 1209 (1992). Z Lojda, et al., Acta Histochem., 98, 215 (1996). H.T. Johansen, et al., Anal. Biochem., 273, 278 (1999).

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Pro-Phe-Arg-MCA

(Hydrochloride Form)A MPF-3096-v

-20 °C

5 mgvial

70

l-prolyl-l-phenylalanyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 575.66) C30H37N7O5 [115918-56-4]Substrate for Pancreatic / Urinary Kallikrein and ProteasomeT. Morita, H. Kato, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, J. Biochem., 82, 1495 (1977). V. Ustrell, G. Pratt, and M. Rechesteiner, Proc. Natl. Acad. Sci. USA, 92, 584 (1995).

Z-Phe-Arg-MCA See Code MFR-3095-v on page 183.

Human Kallikrein 6 SubstrateHuman kallikrein 6 (hK6) is greatly expressed in the central nervous system. It was shown to degrade myelin-associated proteins and is expressed in cells localized at sites of demyelination, suggesting hK6 plays a role in demyelinating diseases such as multiple sclerosis (MS).1,2 In addition, hK6 is attenuated in brain extracts of Alzheimer patients.3,4 Discovery of specific hK6 substrates would help to determine the functional role of this enzyme. Angelo et al. recently screened a number of potential FRETS-based hK6 substrates that were constructed based on a known hK1 substrate and found Abz-Ala-Phe-Arg-Phe-Ser-Gln-EEDnp (SFQ-3915-PI) to be the most potent (kcat = 11.6 s-1, Km = 0.3 µM).5 This substrate may help in studies focused on the biological role of hK6.1. Scarisbrick, et al., Brain, 125, 1283 (2002). 2. Blaber, et al., FASEB J., 18, 920 (2004). 3. Diamandis, et al., Clin. Biochem., 33, 579 (2000).

4. Ni, et al., Br. J. Cancer, 91, 725 (2004). 5. Angelo, et al., J. Biol. Chem., 281, 3116 (2006)

Abz-Ala-Phe-Arg-Phe-Ser-Gln-EDDnp (M.W. 1082.15) C50H63N15O13Substrate for Human Kallikrein 6 (hK6)

SFQ-3915-PI -20 °C

1 mg5 mg

50195

Isopeptidase T Substrate See Code MLG-3176-v on page 206.

KyS-1 See Code SMO-3225-v on page 182.

Legumain SubstrateZ-Ala-Ala-Asn-MCA

Benzyloxycarbonyl-l-alanyl-l-alanyl-l-asparagine-4-methylcoumaryl-7-amide (M.W. 565.57) C28H31N5O8 [149697-16-5] Substrate for Legumain

A MCA-3209-v-20 °C

5 mg vial

65

A.A. Kembhavi, D.J. Buttle, C.G. Knight, and A.J. Barret, Arch. Biochem. Biophys., 303, 208 (1993). J.-M. Chen, et al., J. Biol. Chem., 272, 8090 (1997). B. Manoury, E.W. Hewitt, N. Morrice, P.M. Dando, A.J. Barret, and C. Watts, Nature, 396, 695 (1998). S.J. Choi, et al., J. Biol. Chem., 274, 27747 (1999). P.M. Dando, M. Fortunato, L. Smith, C.G. Knight, J.E. McKendrick, and A.J. Barret, Biochem. J., 339, 743 (1999).

Leu-Gly • ½ H2Ol-Leucylglycine (M.W. 188.22 • 9.01) C8H16N2O3 • ½ H2O [686-50-0]

AA OLG-3024-20 °C

0.1 g1 g

2555

Leu-Gly-Glyl-Leucylglycylglycine (M.W. 245.28) C10H19N3O4 [1187-50-4]

AA OLG-3025-20 °C

0.1 g1 g

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PRODUCT GRADE CODE QTy PRICE

Lysine Hydroxylase SubstrateAla-Arg-Gly-Ile-Lys-Gly-Ile-Arg-Gly-Phe-Ser-Gly • 3AcOH • 5H2O[lysine Hydroxylase Substrate L-1]

AA SAG-4166-20 °C

25 mg 525

(M.W. 1218.4 • 180.16 • 90.08) C53H91N19O14 • 3CH3COOH • 5H2O Substrate for lysine Hydroxylase

K.I. Kivirikko, K. Shudo, S. Sakakibara, and D.J. Prockop, Biochemistry, 11, 122 (1972). (Original)

Met-Metl-methionyl-l-methionine (M.W. 280.41) C10H20N2O3S2 [7349-78-2]

A OMM-3152-20 °C

0.1 g1 g

40170

MALTI SubstrateAc-Leu-Arg-Ser-Arg-MCA

Ac-LRSR-MCA(M.W. 729.84) C33H51N11O8Substrate for MALTI

MCA-3952-PI -20 °C

5 mg 95

P. Niyomrattanakit, S. Yahorava, I. Mutule, F. Muturlis, R. Petrovska, P. Prusis, G. Katzenmeier, and J.E.S. Wikberg, Biochem. J., 397, 203-211 (2006).

Reference Compound for MOCAc-type Fluorescence-Quenching SubstrateMOCAc-Pro-Leu-Gly AA MOC-3164-s

-20 °C

0.1 mgvial

30(7-Methoxycoumarin-4-yl) acetyl-l-prolyl-l-leucyl-glycine (M.W. 501.53) C25H31N3O8 [140430-56-4]Reference Compound for MOCAc-type Fluorescence-Quenching SubstrateC.G. Knight, F. Willenbrock, and G. Murphy, FEBS Lett., 296, 263 (1992).

Neprilysin SubstrateZ-Ala-Ala-Leu-pNA

Benzyloxycarbonyl-l-alanyl-l-alanyl-l-leucine p-nitroanilide (M.W. 527.57) C26H33N5O7 [61043-33-2]

AA SAP-3127-20 °C

0.1 g1 g

50305

Substrate for Subtilisin A and Serine Protease of Bacillus subtilis IFO3027 / NeprilysinV.M. Stepanov, et al., Biochem. Biophys. Res. Commun., 77, 298 (1977). Y. Shimizu, T. Nishino, and S. Murao, Agric. Biol. Chem., 47, 1775 (1983). Y. Takaki, et al., J. Biochem., 128, 897 (2000). N. Iwata, Y. Takaki, S. Fukami, S. Tsubuki, and T.C. Saido, J. Neurosci. Res., 70, 493 (2002).

Neutral Endopeptidase SubstratesZ-Gly-Gly-Leu-pNA

Benzyloxycarbonyl-glycylglycyl-l-leucine-p-nitroanilide(M.W. 499.52) C24H29N5O7 [53046-98-3] Substrate for Neutral Endopeptidase

AA SGL-3111 -20 °C

25 mg100 mg

1 g

60160910

M. Orlowski and S. Wilk, In, Peptides, Structure and Biological Functions, (E. Gross and J. Meienhofer, Eds.), Pierce Chemical Co., 1980, p. 925.

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Abz-Ala-Gly-Leu-Ala-p-Nitro-Benzyl-Amide

(Trifluoroacetate Form) SAG-3905-PI

-20 °C

5 mg 25 mg

45175

2-Aminobenzoyl-l-Alanyl-Glycyl-l-Leucyl-l-Alanyl-para-Nitro-Benzyl-Amide (M.W. 583.65) C28H37N7O7 Substrate for Thermolysin and Neutral Endopeptidase 24.11 (NEP)N. Nishino and J.C. Powers, J. Biol. Chem., 255, 3482 (1980). R.S. Rush, et al., Arch. Biochem. Biophys., 231, 390 (1984).D.I. Mundy and W.J. Strittmatter, Cell, 40, 645 (1985).

Pepsin SubstrateMOCAc-Ala-Pro-Ala-Lys-Phe-Phe-Arg-Leu-Lys(Dnp)-NH2

(Trifluoroacetate Form)

A SMO-3216-v-20 °C

1 mg vial

140

(7-Methoxycoumarin-4-yl)Acetyl-l-alanyl-l-prolyl-l-alanyl-l-lysyl-l-phenylalanyl-l- phenylalanyl-l-arginyl-l-leucyl-[Ne-(2,4-dinitrophenyl)-l-lysine] amide (M.W. 1458.6) C71H95N17O17 Fluorescence-Quenching Substrate for Proteinase A / PepsinH. Kondo, Y. Shibano, T. Amachi, N. Cronin, K. Oda, and B.M. Dunn, J. Biochem., 124, 141 (1998). • This compound is distributed under the license of Suntory Limited.

Peptidoglutaminase SubstrateBoc-Gln-Pro

t-Butyloxycarbonyl-l-glutaminyl-l-proline (M.W. 343.38) C15H25N3O6 [2419-99-0] Substrate for Peptidoglutaminase

AA SQP-3151-20 °C

0.1 g1 g

40170

J.S. Hamada and W.E. Marshall, J. Food Sci., 53, 1132 (1988).

Reference Compound for Peptidyl-MCA SubstrateAMC

7-Amino-4-methyl-coumarin(M.W. 175.18) C10H9NO2 [26093-31-2]

AA MCA-3099-v-20 °C

5 mgvial

50

Reference Compound for Analysis with Peptidyl-MCA Substrates

Peptidyl Prolyl cis-trans Isomerase (PPlase) SubstrateSuc-Ala-Glu-Pro-Phe-pNASuc-AEPF-pNA

(Acetate Form) (M.W. 682.69) C32H38N6O11

SAP-3947-PI -20 °C

1 mg5 mg

2565

Substrate for Peptidyl-prolyl Isomerase (PPIase) Pin1Z.J. Shen, S. Esnault, and J.S. Malter, Nat. Immunol., 6, 1280 (2005). S. Esnault, Z.J. Shen, E.Whitesel and J.S. Malter, J. Immunol., 177, 6999 (2006).

Suc-Ala-Leu-Pro-Phe-pNA See Code SAF-3162-v on page 178.

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Plasmin SubstrateBoc-Glu-Lys-Lys-MCA A MEK-3105-v

-20 °C

5 mg vial

80t-Butyloxycarbonyl-l-glutamyl-l-lysyl-l-lysine 4-methylcouma-ryl-7-amide (M.W. 660.76) C32H48N6O9 [73554-85-5] Substrate for PlasminH. Kato, N. Adachi, Y. Ohno, S. Iwanaga, K. Takada, and S. Sakakibara, J. Biochem., 88, 183 (1980).

Boc-Val-Leu-Lys-MCA See Code MVL-3104-v on page 178.

Prion Proteins See Cellular Prion Protein on page 184.

Prolyl Endopeptidase SubstrateSuc-Gly-Pro-MCA AA MGP-3109-v

-20 °C

5 mg vial

55Succinyl-glycyl-l-proline 4-methylcoumaryl-7-amide (M.W. 429.42) C21H23N3O7 [80049-85-0]Substrate for Propyl Endopeptidase (Post-proline Cleaving Enzyme)T. Kato, T. Nakano, K. Kojima, T. Nagatsu, and S. Sakakibara, J. Neurochem., 35, 527 (1980).

Proteinase 3 SubstrateAbz-Val-Ala-Asp-Nva-Arg-Asp-Arg-Gln-EDDnp [Abz-VADnVRDRQ-EDDnp], nV = Nva

(Trifluoroacetate Form)

SNP-3232-v-20 °C

1 mg vial

110

2-Aminobenzoyl-l-valyl-l-alanyl-l-aspartyl-l-norvalyl-l-arginyl-l-aspartyl-l-arginyl-l-glutamine 2-(2,4-dinitrophenyl)aminoethyl-amide(M.W. 1285.3) C53H80N20O18Fluorescence-Quenching Substrate for Human Neutrophil Proteinase 3

B. Korkmaz, et al., J. Biol. Chem., 282, 1989 (2007).B. Korkmaz, et al., Nat. Protoc., 3, 991 (2008).

Proteinase A SubstratesMOCAc-Ala-Pro-Ala-Lys-Phe-Phe-Arg-Leu-Lys(Dnp)-NH2 See Code SMO-3216-v on page 199.Suc-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-MCA See Code MRP-3110-v on page 185.

Protein Kinase SubstratePyr-Lys-Arg-Pro-Ser-Gln-Arg-Ser-Lys-Tyr-Leu

(M.W. 1373.6) C60H100N20O17 [136132-68-8] Substrate for Protein Kinase C

A SKL-4237-v-20 °C

5 mg vial

290

I. Yasuda, A. Kishimoto, S. Tanaka, M. Tominaga, A. Sakurai, and Y. Nishizuka, Biochem. Biophys. Res. Commun., 166, 1220 (1990).

Arg-Arg-Leu-lle-Glu-Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Gly [RR-SRC]

(M.W. 1519.7) C64H106N22O21 [81156-93-6]Substrate for Tyrosine Protein-Kinase

AA

SRG-4184-v-20 °C

0.5 mg vial

85

J.E. Casnellie, M.L. Harrison, L.J. Pike, K.E. Hellström, and E.G. Krebs, Proc. Natl. Acad. Sci. USA, 79, 282 (1982).

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE H-Arg-Arg-Leu-Ile-Glu-Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Gly-NH2

(Acetate Form) RRLIEDAEYAARG(M.W. 1518.71) C64H107N23O20 [81156-93-6]Substrate for Protein Tyrosine Kinase (PTK)

PTK-3956-PI -20 °C

1 mg5 mg

45155

J.E. Casnellie, M.L. Harrison, L.J. Pike, K.E. Hellstrom, and E.G. Krebs, Proc. Natl. Acad. Sci. USA, 79, 282 (1982).S.E. Ramer, D.G. Winker, A. Carrera, T.M. Robets, and C.T. Walsh, Proc. Natl. Acad. Sci. USA, 88, 6254, (1991).H.S. Earp, K.S. Austin, G.Y. Gillespie, S.C. Buessow, A.A. Davies, and P.J. Parker, J. Biol. Chem., 260, 4351 (1985).

Protein Phosphatase SubstrateH-Arg-Arg-Leu-Ile-Glu-Asp-Ala-Glu-Tyr(H2PO3)-Ala-Ala-Arg-Gly-NH2RRLIEDAE-py-AARG

(Acetate Form) (M.W. 1598.69) C64H108N23O23P

PTP-3955-PI -20 °C

1 mg5 mg

85345

Substrate for Protein Tyrosine Phosphatase (PTP)K.L. Lim, D.S.Y. Lai, M.B. Kalousek, Y. Wang, and C.J. Pallen, Eur. J. Biochem, 245, 693 (1997).V. Bhandari, K. Leong Lim, and C.J. Pallen, J. Biol. Chem., 273, 8691 (1998).J.J. Perez-Villar, et al., Molec. Cell. Biol., 19, 2903 (1999).

Pyro-glutamyl Peptidase SubstratesPyr-Ala

l-Pyroglutamyl-l-alanine (M.W. 200.19) C8H12N2O4 [21282-08-6] Substrate for Pyroglutamyl Peptidase

AA OVA-3079-20 °C

0.1 g1 g

32130

R.F. Doolittle, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds.), Academic Press, New York, 1970, pp. 555-569.

Pyr-MCAl-Pyroglutamic acid 4-methylcoumaryl-7-amide (M.W. 286.28) C15H14N2O4 [66642-36-2] Substrate for Pyroglutamyl PeptidaseK. Fujiwara and D. Tsuru, J. Biochem., 83, 1145 (1978).

AA MPX-3101-v-20 °C

5 mg vial

50

Renin SubstratesAsp-Arg-Val-Tyr-lle-His-Pro-Phe-His-Leu-Val-Ile-His

(M.W. 1645.9) C79H116N22O17 [82048-97-3]Substrate for Renin

A SDH-4133-v-20 °C

0.5 mg vial

55

D.A. Tewksbury, R.A. Dart, and J. Travis, Biochem. Biophys. Res. Commun., 99, 1311 (1981).

Dabcyl-γ-Abu-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Edans

(Trifluoroacetate Form)(M.W. 1798.16) C90H120N22O16S [142988-22-5]FRET Substrate for Renin

SFQ-3731-PI-20 °C

1 mg5 mg

3401360

G.T. Wang, et al., Anal Biochem, 210, 351-9 (1993). N. Nakamura, et al., J Biochem (Tokyo), 109, 741-5 (1991). K. Murakami, et al., Anal Biochem, 110, 232-9 (1981).

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PRODUCT GRADE CODE QTy PRICE

Nma-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys(Dnp)-D-Arg-D-Arg-NH2

(Trifluoroacetate Form)

SFQ-3229-v-20 °C

1 mg vial

175

[2-(Methylamino)benzoyl]-l-isoleucyl-l-histidyl-l-prolyl-l-phenylalanyl-l-histidyl-l-leucyl-l-valyl-l- isoleucyl-l-histidyl-l-threonyl-[Nε-(2,4-dinitrophenyl)-l-lysyl]-d-arginyl-d-arginine amide (M.W. 1952.20) C91H134N30O19 Synthetic Product Fluorescence-Quenching Substrate for Human Renin S. Takahashi, K. Hori, M. Shinbo, K. Hiwatashi, T. Gotoh, and S. Yamada, Biosci. Biotechnol. Biochem.,72, 3232 (2008).

Suc-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-MCA See Code MRP-3110-v on page 185.

β-Secretase SubstratesMOCAc-Ser-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-Arg-Lys(Dnp)-Arg-Arg-NH2 [MOCAc-SEVNLDAEFRK(Dnp)RR-NH2]

(Trifluoroacetate Form)

B SMO-3212-v-20 °C

1 mg vial

185

(7-Methoxycoumarin-4-yl) acetyl-l-seryl-l-glutamyl-l-valyl-l-Asparaginyl-l-leucyl-l-aspartyl-l-alanyl-l-glutamyl-l-phenylalanyl-l-arginyl-[Ne-(2,4-dinitrophenyl)-l-lysyl]-l-arginyl-l-arginine amide (M.W. 2001.1) C86H125N27O29 Fluorescence-Quenching Substrate for b-SecretaseH. Koike, H. Seki, Z. Kouchi, M. Ito, T. Kinouchi, S. Tomioka, H. Sorimachi, T.C. Saido, K. Maruyama, K. Suzuki, and S. Ishiura, J. Biochem., 126, 235 (1999).

H-Arg-Glu(Edans)-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-Lys(Dabcyl)-Arg-OH

(Trifluoroacetate Form) H-RE(Edans)-EVNLDAEFK(Dabcyl)R-OH(M.W. 2005.26) C91H129N25O25S

SFQ-3690-PI-20 °C

1 mg

129

Fluorescence-Quenching Substrate for Memapsin 2 (b-Secretase)J. Ermolieff, J.A. Loy, G. Koelsch, and J. Tang, Biochemistry, 39, 12450 (2000). (substrate termed FS-1 this paper)

γ-Secretase SubstrateNma-Gly-Gly-Val-Val-Ile-Ala-Thr-Val-Lys(Dnp)-d-Arg-d-Arg-d-Arg-NH2

(Trifluoroacetate Form)

B SFQ-3217-v-20 °C

1 mg vial

185

[2-Methylamino)benzoylglycylglycyl-l-valyl-l-valyl-l-isoleucyl-l-alanyl-l-threonyl-l- valyl-[Ne-(2,4-dinitrophenyl)-l-lysyl]-d-arginyl-d-arginyl-d-arginine amide (M.W. 1609.8) C70H116N26O18 Fluorescence-Quenching Substrate for g-SecretaseM.R. Farmery, L.O. Tjernberg, S.E. Pursglove, A. Bergman, B. Winblad, and J. Näslund, J. Biol. Chem., 278, 24277 (2003). (Original)

Serum Peptidase SubstrateDnp-Leu-Gly-Ile-Ala-Gly-Arg-NH2

2,4-dinitrophenyl-l-leucyl-glycyl-l-isoleucyl-l-alanyl-glycyl-l-arginine amide (M.W. 750.80) C31H50N12O10 Substrate for Serum Peptidase

A SDL-3083-v-20 °C

2.5 mg vial

95

Y. Masui, T. Takemoto, S. Sakakibara, H. Hori, and Y. Nagai, Biochem. Med., 17, 215 (1977).

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Site-1 Protease (S1P) SubstrateAc-Val-Phe-Arg-Ser-Leu-Lys-MCA

(Trifluoroacetate Form) Acetyl-l-valyl-l-phenyl-l-arginyl-l-seryl-l-leucyl-l-lysine 4-methylcoumaryl-7-amide(M.W. 948.14) C47H69N11O10Substrate for Site-1 Protease (S1P)

MCA-3679-PI-20 °C

1 mg5 mg

85345

D. Cheng, P.J. Espenshade, C.A. Slaughter, J.C. Jaen, M.S. Brown, and J.L. Goldstein, J. Biol. Chem., 274, 22805 (1999).

Subtilisin A SubstrateZ-Ala-Ala-Leu-pNA See Code SAP-3127 on page 198.

Suc-Ala-Ala-pNASuccinyl-l-alanyl-l-alanine p-nitroanilide (M.W. 380.35) C16H20N4O7

AA SAA-3117-20 °C

0.1 g1 g

40180

Suc-Ala-pNASuccinyl-l-alanine p-nitroanilide (M.W. 309.27) C13H15N3O6

AA SAN-3116-20 °C

0.1 g1 g

30105

Trans-glutaminase SubstrateZ-Gln-Gly

Benzyloxycarbonyl-l-glutaminylglycine (M.W. 337.33) C15H19N3O6 [6610-42-0] Substrate for Transglutaminase

AA SZQ-3190-20 °C

1 g5 g

170515

J.E. Folk and P.W. Cole, J. Biol. Chem., 241, 5518 (1966). H. Ando, M. Adachi, K. Umeda, A. Matsuura, M. Nonaka, R. Uchio, H. Tanaka, and M. Motoki, Agric. Biol. Chem., 53, 2613 (1989).

Tripeptidyl Peptidase II SubstrateAla-Ala-Phe-MCA

(Hydrochloride Form)AA MCA-3201-v

-20 °C

5 mg vial

55

l-alanyl-l-alanyl-l-phenylalanine 4-methylcoumaryl-7-amide (M.W. 464.51) C25H28N4O5 [62037-41-6] Substrate for Tripeptidyl Peptidase II (Component of Giant Protease with Some Proteasome Function)R. Glas, M. Bogyo, J.S. McMaster, M. Gaczynska, and H. L. Ploegh, Nature, 392, 618 (1998). E. Geier, G. Pfeifer, M. Wilm, M. Lucchiari-Hartz, W. Baurmeister, K. Eichmann, and G. Niedermann, Science, 283, 978 (1999).

Trypsin and Trypsin-like Protease SubstratesAc-Arg-OMe • HCl

Acetyl-l-arginine methyl ester • monohydrochloride

B SRM-3078-20 °C

1 g5 g

40105

(M.W. 230.26 • 36.46) C9H18N4O3 • HCI [1784-05-0] Substrate for C1rR.B. Sim, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, ed.), Academic Press, New York, 1981, pp. 26-42.

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Ac-Gly-Lys-OMe • AcOH [AGLME]

Acetyl-glycyl-l-lysine methyl ester

A SGK-3058-20 °C

0.1 g1 g

3099

(M.W. 259.30 • 60.05) C11H21N3O4 • CH3COOH [14752-92-2] Substrate for u-PA (Urokinase) and C1s

P.L. Walton, Biochim. Biophys. Acta., 132, 104 (1967). N. Miwa, Y. Obata, and A. Suzuki, Biochem. Biophys. Res. Commun., 112, 754 (1983). R.B. Sim, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, Ed.), Academic Press, New York, 1981, pp. 26-42.

Boc-Gln-Ala-Arg-MCAt-Butyloxycarbonyl-l-glutaminyl-l-alanyl-l-arginine4-methylcoumaryl-7-amide (M.W. 630.69) C29H42N8O8 [113866-20-9] Substrate for Trypsin

A MQR-3135-v-20 °C

5 mg vial

65

S. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, Eur. J. Biochem., 172, 17 (1988).

Boc-Leu-Gly-Arg-MCA See Code MLG-3102-v on page 196.Boc-Phe-Ser-Arg-MCA See Code MFS-3107-v on page 193.

Bz-Arg-MCA(Hydrochloride form) Benzoyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 435.48) C23H25N5O4 [83701-04-6] Substrate for Trypsin

A MBR-3092-v-20 °C

5 mg vial

45

Y. Kanaoka, T. Takahashi, H. Nakayama, K. Takada, T. Kimura, and S. Sakakibara, Chem. Pharm. Bull., 25, 3126 (1977).

Bz-Arg-NH2 • HCl • H2OBenzoyl-l-arginine amide monohydrochloride monohydrate

AA SRA-3002-20 °C

1 g5 g

3280

(M.W. 277.32 • 36.46 • 18.02) C13H19N5O2 • HCI • H2O [4299-03-0] Substrate for TrypsinK.A. Walsh, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds.), Academic Press, New York, 1970, pp. 41-63.

Bz-Arg-OEt • HCl [BAEE]

Benzoyl-l-arginine ethyl ester monohydro-chloride

A SRE-3001-20 °C

1 g25 g

3055

(M.W. 306.36 • 36.46) C15H22N4O3 • HCI [2645-08-1] Substrate for Trypsin K.A. Walsh, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds.), Academic Press, New York, 1970, pp. 41-63.

Bz-dl-Arg-pNA • HCl [dl-BAPA]

A SRN-3013-20 °C

0.1 g5 g

2545

Benzoyl-dl-arginine p-nitroanilide monohydrochloride (M.W. 398.42 • 36.46) C19H22N6O4 • HCl [911-77-3]Substrate for Trypsin-like ProteaseK.A. Thomas and R.A. Bradshaw, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, Ed.), Academic Press, New York, 1981, pp. 609-620. G.A. Grant, A.Z. Eisen, and R.A. Bradshaw, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, Ed.), Academic Press, New York, 1981, pp. 722-734.

Bz-L-Arg-pNA See Code SRN-3057 on page 182.

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Tos-Arg-OMe • HCI

[TAME] Tosyl-l-arginine methyl ester monohydrochlo-ride

A STR-3003-20 °C

5 g25 g

100 g

3599

272(M.W. 342.41 • 36.46) C14H22N4O4S • HCI [1784-03-8] Substrate for TrypsinK.A. Walsh, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds.), Academic Press, New York, 1970, pp. 41-63.

Tos-Lys-OMe • HCITosyl-l-lysine methyl ester monohydrochloride (M.W. 314.40 • 36.46) C14H22N2O4S • HCI [5266-48-8] Substrate for Trypsin

A STK-3054-20 °C

0.1 g1 g

2545

F. Widmer and J.T. Johansen, Carlsberg Res. Commun., 44, 37 (1979). F. Widmer, K. Breddam, and J.T. Johansen, Proc. 16th European Peptide Symposium (K. Brunfeldt, Ed.), Scriptor, Copenhagen 1981, pp. 46-55.

Ubiquitin Proteasome System Substrates Ac-Arg-Leu-Arg-MCAAc-RLR-MCA

(Trifluoroacetate Form) (M.W. 642.76) C30H46N10O6 [929903-87-7]Fluorogenic Substrate; Substrate for 20S ProteasomeA.F. Kisselev, et al., J. Biol. Chem., 281 (2006).A.F. Kisselev and A.L.Goldberg, Meth. Enzy., 398 (2005).K.J. Rogders and R.T. Dean, Intl. J. Biochem.Cell.Biol., 35 (2003)

MCA-3729-PI -20 °C

1 mg5 mg

100400

Ac-Gly-Pro-Leu-Asp-MCA[Ac-GPLD-MCA]

(Acetate Form)Substrate for Caspase-Like Site of Proteasomes(M.W. 599.65) C29H37N5O9

MCA-3649-PI-20 °C

5 mg 95

A. Kisselev, M. Garcia-Calvo, H.S. Overkleeft, E. Peterson, M.W. Pennington, H.L. Ploegh, N.A. Thornberry, and A.L.Goldberg, J. Biol. Chem., 278, 35869 (2003).

Ac-Nle-Pro-Nle-Asp-MCA(M.W. 655.75) C33H45N5O9

MCA-3650-PI-20 °C

5 mg 95

Substrate for Caspase-Like Site of ProteasomesA. Kisselev, M. Garcia-Calvo, H.S. Overkleeft, E. Peterson, M.W. Pennington, H.L. Ploegh, N.A. Thornberry, and A.L.Goldberg, J. Biol. Chem., 278, 35869 (2003).

Suc-Ala-Glu-MCASuccinyl-l-alanyl-l-glutamic acid a-4-methyl-coumaryl-7-amide (M.W. 475.45) C22H25N3O9 Substrate for Ingensin / Proteasome.

A MAE-3160-v-20 °C

5 mg vial

55

S. Ishiura, T. Tsukahara, T. Tabira, and H. Sugita, FEBS Lett., 257, 388 (1980)

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Z-Leu-Arg-Gly-Gly-MCABenzyloxycarbonyl-l-leucyl-l-arginyl-glycylglycine 4-methylcoumaryl-7-amide (M.W. 692.76) C34H44N8O8 [167688-68-2] Substrate for Isopeptidase T

A MLG-3176-v-20 °C

5 mg vial

95

R.L Stein, Z. Chen, and F. Melandri, Biochemistry, 34, 12616 (1995).

Z-Leu-Leu-Glu-MCABenzyloxycarbonyl-l-leucyl-l-leucyl-l-glutamic acid a-(4-methylcoumaryl-7-amide) (M.W. 664.75) C35H44N4O9 [348086-66-8] Substrate for Proteasome

A MLG-3179-v-20 °C

5 mg vial

75

Z-Leu-Leu-Leu-MCABenzyloxycarbonyl-l-leucyl-l-leucyl-l-leucine 4-methylcoumaryl-7-amide (M.W. 648.79) C36H48N4O7 Substrate for Proteasome

A MLL-3177-v-20 °C

5 mg vial

65

S. Tsubuki, H. Kawasaki, Y. Saito, N. Miyashita, M. Inomata, and S. Kawashima, Biochem. Biophys. Res. Commun., 196, 1195 (1993).

Boc-Leu-Arg-Arg-MCA See Code MLR-3140-v on page 193.Pro-Phe-Arg-MCA See Code MPF-3096-v on page 197.Suc-Leu-Leu-Val-Tyr-MCA See Code MLL-3120-v on page 178.

u-PA (Urokinase) Substrates Also see SGK-3058 Ac-Gly-Lys-OMe • AcOH n page 204.

Glt-Gly-Arg-MCAGlutarylglycyl-l-arginine 4-methylcoumaryl-7-amide (M.W. 502.52) C23H30N6O7 [65147-16-2] Substrate for u-PA (Urokinase)

A MGG-3097-v-20 °C

5 mg vial

55

T. Morita, H. Kato, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, J. Biochem., 82, 1495 (1977). S. Iwanaga, T. Morita, H. Kato, T. Harada, N. Adachi, T. Sugo, I. Maruyama, K. Takada, T. Kimura, and S. Sakakibara, In, KININS-II: Biochemistry, Pathophysiology, and Clinical Aspects, (S. Fujii, H. Moriya, and T. Suzuki, eds.), Plenum Publishing Co., 1979, pp. 147-163.

Pyr-Gly-Arg-MCAl-Pyroglutamyl-glycyl-l-arginine 4-methylcou-maryl-7-amide (M.W. 499.52) C23H29N7O6 Substrate for t-PA and u-PA (Urokinase)

A MPR-3145-v-20 °C

5 mg vial

55

Vascular Processing Enzyme SubstratesAc-Glu-Ser-Glu-Asn-MCA[Ac-ESEN-MCA]

MCA-3227-v -20 °C

5 mg 120

Acetyl-l-glutamyl-l-seryl-l-glutamyl-l-asparagine α-(4-methylcoumaryl-7-amide)(M.W. 676.63) C29H36N6O13 Substrate for Vacuolar Processing Enzyme (VPE)M. Kuroyanagi, M. Nishimura, and I. Hara-Nishimura, Plant Cell Physiol., 43, 143 (2002).N. Hatsugai, M. Kuroyanagi, K. Yamada, T. Meshi, S. Tsuda, M. Kondo, M. Nishimura, and I. Hara-Nishimura, Science, 305, 855 (2004).M. Kuroyanagi, K. Yamada, N. Hatsugai, M. Kondo, M. Nishimura, and I. Hara-Nishimura, J. Biol. Chem., 280, 32914 (2005).

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Z-Arg-OBzl(p-NO2) • HBr

Benzyloxycarbonyl-l-arginine p-nitrobenzyl ester • Monohydrobromide (M.W. 443.45 • 80.91) C21H25N5O6 • HBr [96723-72-7]

A SRB-3157-20 °C

0.1 g1 g

35120

Z-Asp-CH2-DCB See Code ICE-3174-v on page 158.Z-Glu-Lys(bio)-Asp-aomk See Code ICA-3189-v on page 158. Z-Glu-Lys(Biotinyl)-Asp-CH2-DCB See Code ICA-3189-v on page 158.

Z-Gly-LeuBenzyloxycarbonylglycyl-l-leucine (M.W. 322.36) C16H22N2O5 [1421-69-8]

AA SGL-3019-20 °C

0.1 g1 g

25160

Z-Gly-Leu-NH2Benzyloxycarbonylglycyl-l-leucine amide (M.W. 321.37) C16H23N3O4 [7535-72-0]

AA SGL-3037-20 °C

0.1 g1 g

3080

Z-Gly-PheBenzyloxycarbonylglycyl-l-phenylalanine (M.W. 356.37) C19H20N2O5 [1170-76-9]

AA SGF-3020-20 °C

0.1 g1 g

2255

Z-Gly-Phe-NH2Benzyloxycarbonylglycyl-l-phenylalanine amide (M.W. 355.39) C19H21N3O4 [5513-69-9]

AA SGF-3021-20 °C

0.1 g1 g

3080

Z-Gly-ProBenzyloxycarbonylglycyl-l-proline (M.W. 306.31) C15H18N2O5 [1160-54-9]

AA SGP-3055-20 °C

0.1 g1 g

2255

Z-Gly-Pro-LeuBenzyloxycarbonylglycyl-l-prolyl-l-leucine (M.W. 419.47) C21H29N3O6 [2646-63-1]

AA SGL-3039-20 °C

0.1 g1 g

40180

Z-Gly-Pro-Leu-GlyBenzyloxycarbonylglycyl-l-prolyl-l-leucyl-glycine (M.W. 476.52) C23H32N4O7

AA SGG-3040-20 °C

0.1 g1 g

55340

Z-Ile-Glu(OtBu)-Ala-Leu-H (aldehyde) See Code IAT-3169-v on page 171.Z-Leu-Leu-H (aldehyde) See Code IZL-3178-v on page 155.Z-Leu-Leu-Leu-H (aldehyde) See Code IZL-3175-v on page 162.Z-Leu-Leu-Nva-H (aldehyde) See Code IAT-3170-v on page 171.

Z-Phe-TyrBenzyloxycarbonyl-l-phenylalanyl-l-tyrosine (M.W. 462.49) C26H26N2O6

AA SFy-3044-20 °C

0.1 g1 g

3080

Z-Tyr-GluBenzyloxycarbonyl-l-tyrosyl-l-glutamic acid (M.W. 444.43) C22H24N2O8 [988-70-5]

AA SyE-3069-20 °C

0.1 g1 g

30115

Z-Tyr-ONpBenzyloxycarbonyl-l-tyrosine p-nitrophenyl ester (M.W. 436.41) C23H20N2O7 [3556-56-7]

A-B SyN-3016-20 °C

0.1 g1 g

2560

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Design of FRETS-25XaaEach substrate (SFA-3701-v - SFV-3719-v) in the FRETS-25Xaa series contains a highly fluorescent 2-(N-methylamino)benzoyl (Nma) group linked to the side chain of the amino-terminal d-2,3-diamino proprionic acid (D-A2pr) residue, which is efficiently quenched by a 2,4-dinitrophenyl (Dnp) group linked to the e-amino function of Lys. Xaa represents a fixed position of each of the 19 natural amino acids excluding Cys (noted in product name, code SFA-3701-v - SFV-3719-v). A mixture of 5 amino acid residues (P, Y, K, I, and D) is at the Yaa position along with a mixture of 5 amino acid residues (F, A, V, E, and R) at the Zaa position for each fixed Xaa. This provides a peptide mixture of 25 combinations of each Xaa series resulting in a combinatorial library totaling 475 peptide substrates. Both Nma and Dnp groups are linked to the side chain of the individual residues, allowing for the determination of the cleavage site by a specific enzyme, through mass spectrometric analysis and Edman degradation as well.

PrincipleWhen an enzyme of interest cleaves any peptide bond between d-A2pr(Nma) and Lys(Dnp) in the substrate, the fluorescence at λex = 340 nm and λem = 440 nm increases in proportion to the release of the Nma fluorophore from the internal Dnp quencher.

Reagents1) Each substrate stock solutions: each FRETS-25Xaa (Code SFA-3701-v - Code SFV-3719-v) in 1.0 ml of

DMSO (1 mM, total of peptides)2) Reference compounds stock solution: a 1:1 mixture of two solutions of Code STD-3720-v and Code STD-

3721-v, each of which is reconstituted by dissolving peptides in 0.5 ml of DMSO at the concentration of 2 mM (1 mM, each reference compound)

3) Enzyme solution: an enzyme of interest in an appropriate buffer4) Buffer

Procedure for the deduction of the substrate specificity of an enzyme with unidentified cleavage specificityChoose the proper conditions for the measurement, such as substrate concentration and sensitivity setting, depending on the purpose of the experiment and the instrument available. Described here is one of the recommended procedures for determining the enzymatic cleavage site by the combination of the fluorometric analysis and liquid chromatography-mass spectrometry (LC-MS) analysis.

FRETS* - 25Xaa Series* FRETS: Fluorescence Resonance Energy Transfer Substrates

O

NH

NO2

NO2PheAlaValGluArg

ProTyrLysIleAsp

Xaa -Ala-Phe-Pro-Lys-D-Arg-D-ArgD-A2pr-Gly- - -

Zaa Yaa

Nma Dnp

FRETS 25

Fluorescence-Quenching Substrate Library All library products have the general structure:d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Gly-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg where A2pr(Nma) = Nb-[2-(N-Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Ne-(2,4-dinitrophenyl)lysine)All substrates are sold as trifluoroacetate form and contain 1 µmol of stated library.

Please refer to our complete product brochure for additional experimental details and protocol recommendations. Please contact our technical specialists or refer to our web site for additional information.

Frets (Peptide) Library

Page 65: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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RS AND SuBSTRATES

i) Primary screening: selection of the favored Xaa• Substrate solution for primary screening (PS solution): Dilute 20 µl of each of the above substrate stock

solution with 1980 µl of an appropriate buffer (10 µM) • Reference compounds solution for primary screening (PR solution): Dilute 20 µl of the above reference compounds stock solution with 1980 µl of an appropriate buffer (10 µM)

1) Set a fluorescence spectrophotometer at λex = 340 nm and λem = 440 nm2) Mix one of the PS solution and the PR solution in ratios of 10/0, 9/1, 8/2, 5/5 and 0/103) Measure the fluorescence of the prepared solutions to obtain the calibration curve for the cleaved products4) Pipette 200 µl each of all PS solutions into the cells and incubate them in the fluorescence

spectrophotometer for 3 min (temperature equilibration)5) Measure the fluorescence of each solution (initial fluorescence blank)6) Add an appropriate volume of enzyme solution7) Record the increase of the fluorescence intensity8) Terminate the enzymatic reaction by using a proper inhibitor (leupeptin, E-64, pepstatin, EDTA and so on)

or changing the pH of the reaction medium (using TCA, AcOH, NaOH and so on)9) Choose the best Xaa-containing substrate for secondary screening

ii) Secondary screening: identification of the specificity of the enzyme (I)• Substrate solution for secondary screening (SS solution): Dilute 200 µl of the stock solution of the best Xaa-containing substrate chosen by the above primary screening with 1800 µl of an appropriate buffer (100 µM) • Reference compounds solution for secondary screening (SR solution): Dilute 200 µl of the above reference compounds stock solution with 1800 µl of an appropriate buffer (100 µM)

1) Set a fluorescence spectrophotometer at λex = 340 nm and λem = 440 nm2) Mix the SS solution and the SR solution in ratios of 100/0, 95/5, 90/10, 80/20, 50/50 and 0/1003) Measure the fluorescence of the prepared solutions to obtain the calibration curve for the cleaved products4) Pipette 200 µl of the SS solution into the cells and incubate them in the fluorescence spectrophotometer for

3 min (temperature equilibration)5) Measure the fluorescence of each solution (initial fluorescence blank)6) Add an appropriate volume of enzyme solution7) Record the increase of the fluorescence intensity8) Terminate the enzymatic reaction by using a proper inhibitor or changing the pH of the reaction medium upon

completion of the reaction at the points of 0%, 5%, 10% and 20% of the total9) Subject 100 µl aliquots to LC-MS

iii) LC-MS: identification of the specificity of the enzyme (2) • Analytical conditions column: ODS eluant: A) H2O containing 0.05% TFA, B) CH3CN containing 0.05% TFA gradient: 10% to 40% B) in A) over 50 min detection: UV at 220 nm and 400 nm or fluorescence

1) Inject 100 µl aliquots of each terminated solution at different stages of the reaction2) Measure the MW of the cleaved product(s) in the peak(s) with the absorbance at 220 nm but not with 400 nm

[identification of the N-terminal segment(s)]3) Deduce their structure from the attached list of the theoretical MW for the cleaved products *Comment 1: If the N-terminal segment has the identical retention time to the C-terminal segment or one of the starting uncleaved substrates, detection of the products by fluorescence is recommended. *Comment 2: In the accidental case where the two products with the same MW (ex. Zaa-Yaa=Phe-Asp and Val-Tyr, Glu-Asp and Phe-Pro) are generated from one of the substrates, their analyses should be carried out by MS-MS sequencing and/or by Edman degradation.

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TES Usefulness and limitation of FRETS-25Xaa series for screening of substrate

specificities of proteases We have confirmed that FRETS-25Xaa series are effectively used for the assay of numerous proteases such as trypsin, chymotyrpsin, elastase, thrombin, papain, calpain, pepsin and thermolysin. However, they did not work well for the assay of caspase-3 and furin, probably because they have only three changeable sites (Zaa-Yaa-Xaa) in each substrate (deficiency of P4 site). This fact implies that FRETS-25Xaa might not be applicable to the assay of an enzyme with wide range interacting sites with substrate.

1. K. Takada, M. Tsunemi, Y. Nishiuchi, and T. Kimura, A Fluorescence Resonance Energy Transfer Substrate (FRETS) Library for Determining Protease Specificity. [Peptide Revolution: Genomic, Proteomics & Therapeutics] (Proceedings of the 18th American Peptide Symposium) 327 (2003).2. S. Tanskul, K. Oda, H. Oyama, N. Noparatnaraporn, M. Tsunemi, and K. Takada, Substrate specificity of alkaline serine proteinase isolated from photosynthetic bacterium, Rubrivivax gelatinosus KDDS1. Biochem. Biophys. Res. Commun., 309, 547 (2003).

PRODUCT CODE QTy PRICEFRETS (Peptide) Library

Please refer to instructions on page 208-209.

FRETS-25Ala(Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Ala-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFA-3701-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nb-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Arg(Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Arg-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFR-3702-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Asn(Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Asn-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFN-3703-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Asp(Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Asp-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFD-3704-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nb-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Ne-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

Page 67: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE FRETS-25Gln

(Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Gln-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFQ-3705-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nb-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Ne-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Glu (Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Glu-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFE-3706-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nb-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Ne-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Gly (Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Gly-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFG-3707-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nb-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Ne-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25His (Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- His-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFH-3708-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Ile (Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Ile-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFI-3709-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Leu (Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Leu-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFL-3710-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Lys(Trifluoroacetate Form)d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Lys-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFK-3711-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

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208 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT GRADE CODE QTy PRICE

FRETS-25Met (Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Met-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFM-3712-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Phe (Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Phe-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFF-3713-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Pro (Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Pro-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFP-3714-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Ser(Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Ser-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFS-3715-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Thr(Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Thr-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFT-3716-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Trp(Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Trp-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFW-3717-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nβ-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Nε-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25Tyr(Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Tyr-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFy-3718-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nb-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Ne-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

Page 69: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE FRETS-25Val

(Trifluoroacetate Form) d-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]- Val-Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg

SFV-3719-v-20 °C

1 mmolvial

120

A2pr(Nma) : Nb-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (Lys(Dnp): Ne-(2,4-dinitrophenyl)lysine) Fluorescence-Quenching Substrate Library

FRETS-25-STD1d-A2pr(Nma)-Gly

STD-3720-v-20 °C

1 mmolvial

30

A2pr(Nma) : Ne-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid (M.W. 294.31) C13H18N4O4 Standard Compound 1 for Fluorescence-Quenching Substrate Library FRETS-25 Xaa Series

FRETS-25-STD2 (Trifluoroacetate Form) Ala-Phe-Pro-Lys(Dnp)-d-Arg-d-Arg- (Lys(Dnp): Ne-(2,4-dinitrophenyl)lysine) (M.W. 940.02) C41H61N15O11

STD-3721-v-20 °C

1 mmolvial

30

Standard Compound 2 for Fluorescence-Quenching Substrate Library FRETS-25 Xaa Series

Page 70: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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210 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT GRADE CODE QTy PRICE

Polypeptides(Pro-Pro-Gly)5 • H2O

(M.W. 1274.4) C60H87N15O16 Purity: higher than 97% by HPLC

OPG-4005-20 °C

25 mg100 mg

60170

K. Kivirrikko, K. Suga, Y. Kishida, S. Sakakibara, and D.J. Prockop, Biochem. Biophys. Res. Commun., 45, 1591 (1971). (Chem. Synthesis and Biochem.)

(Pro-Pro-Gly)10 • H2O(M.W. 2530.8) C120H172N30O31 Purity: higher than 95% by HPLC

OPG-4006-20 °C

25 mg100 mg

85250

S. Sakakibara, Y. Kishida, Y. Kikuchi, R. Sakai, and K. Kakiuchi, Bull. Chem. Soc. Japan, 41, 1273 (1968). (Chem. Synthesis)

(Pro-Hyp-Gly)5 • H2O(M.W. 1354.4) C60H87N15O21 Purity: higher than 96% by HPLC

OPG-4032-20 °C

25 mg 400

S. Sakakibara, K. Inouye, K. Shudo, Y. Kishida, Y. Kobayashi, and D.J. Prockop, Biochim. Biophys. Acta., 303, 198 (1973). (Chem. Synthesis)

(Pro-Hyp-Gly)10 • H2O(M.W. 2690.8) C120H172N30O41 Purity: higher than 90% by HPLC

OPG-4033-20 °C

25 mg 595

S. Sakakibara, K. Inouye, K. Shudo, Y. Kishida, Y. Kobayashi, and D.J. Prockop, Biochim. Biophys. Acta., 303, 198 (1973). (Chem. Synthesis)

Poly-l-Glutamic Acid Sodium SaltM.W. > 8000 cut off by dialysis, NCA polymer-ized product

OEE-3063-20 °C

0.1 g1 g

47233

Poly-l-lysine HydrobromideM.W. > 8000 cut off by dialysis, NCA polymer-ized product

OKK-3056-20 °C

0.1 g1 g

47233

Poly-l-lysine HydrochlorideM.W. > 8000 cut off by dialysis, NCA polymer-ized product [26124-78-7]

OKK-3075-20 °C

0.1 g1 g

47233

OligopeptidesDipeptidesb-Ala-His [Carnosine]

b-alanyl-l-Histidine (M.W. 226.23) C9H14N4O3 [305-84-0]

AA OAH-3085-20 °C

1 g5 g

3580

Glu-Glul-glutamyl-l-Glutamic Acid (M.W. 276.24) C10H16N2O7 [3929-61-1]

A OEE-3080-20 °C

0.1 g1 g

40200

Gly-GlyGlycyl-glycine (M.W. 132.12) C4H8N2O3 [556-50-3]

AA OGG-3028-20 °C

5 g25 g

100 g

253570

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RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Gly-Leu

Glycyl-l-leucine (M.W. 188.23) C8H16N2O3 [869-19-2]

AA OGL-3022-20 °C

0.1 g1 g5 g

2540

105

Gly-PheGlycyl-l-phenylalanine (M.W. 222.24) C11H14N2O3 [3321-03-7]

AA OGF-3053-20 °C

0.1 g1 g

2240

Gly-Phe-NH2 • AcOHGlycyl-l-phenylalanine amide (M.W. 221.26 • 60.05) C11H15N3O2 • CH3COOH [13467-26-0]

AA OGF-3023-20 °C

0.1 g1 g

3080

Gly-ProGlycyl-l-proline (M.W. 172.18) C7H12N2O3 [704-15-4]

AA OGP-3052-20 °C

0.1 g1 g

3060

His-Leul-histidyl-l-leucine (M.W. 268.31) C12H20N4O3 [7763-65-7]

AA OHL-3065-20 °C

0.1 g1 g

30105

Leu-Gly • ½ H2Ol-leucyl-glycine (M.W. 188.22 • 9.01] C8H16N2O3 • ½ H2O [686-50-0]

AA OLG-3024-20 °C

0.1 g1 g

2555

cyclo (Leu-Gly) [Morphine Tolerance Peptide]

Cyclo (l-leucyl-l-glycine)

PMI-4070-20 °C

25 mg100 mg

50130

R. Walter, R.F. Ritzmann, H.N. Bhargava, and L.B. Flexner, Proc. Natl. Acad. Sci. USA, 76, 518 (1979). (Original)I

Met-Metl-methionyl-l-Methionine (M.W. 280.41) C10H20N2O3S2 [7349-78-2]

A OMM-3152-20 °C

0.1 g1 g

40170

Pyr-Alal-Pyroglutamyl-l-alanine (M.W. 200.19) C8H12N2O4 [21282-08-6] Substrate for Pyroglutamyl Peptidase

AA OVA-3079-20 °C

0.1 g1 g

32130

R.F. Doolittle, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, Eds.), Academic Press, New York, 1970, pp. 555-569.

TripeptidesGlu(Cys-Gly) [Glutathione,GSH]

g-l-glutamyl-l-Cysteinyl-glycine (M.W. 307.32) C10H17N3O6S [70-18-8]

B OEG-3050-20 °C

1 g5 g

25 g

223570

Gly-Gly-GlyGlycyl-glycyl-glycine (M.W. 189.17) C6H11N3O4 [556-33-2]

AA OGG-3061-20 °C

1 g5 g

25 g

3080

315

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212 Order Hotline 1-800-777-4779 502-266-8787

PRODUCT GRADE CODE QTy PRICE

Gly-Gly-HisGlycyl-glycyl-l-Histidine (M.W. 269.26) C10H15N5O4 [93404-95-06] Cu-Binding Peptide

A OGH-3076-20 °C

0.1 g1 g

50350

S. Lau, T.P.A Kruch, and B. Sarkar, J. Biol. Chem., 249, 5878 (1974).

Gly-His-Lys • AcOH • H2O [Liver-Cell Growth Factor]

l-glycyl-l-histidyl-l-lysine • AcOH • H2O

PLC-4022-20 °C

25 mg100 mg

90190

L. Pickart, L. Thayer, and M.M. Thaler, Biochem. Biophys. Res. Commun., 54, 562 (1973). (Original)

Ile-Pro-Ile • H2O [Diprotin A]

l-isoleucyl-l-Propyl-l-Isoleucine • H2O

IDP-4132-20 °C

25 mg100 mg

75170

(M.W. 341.45 . 18.02 ) C17H31N3O4 • H2O [90614-48-5] Inhibitor for Dipeptidyl Aminopeptidase IVH. Umezawa, T. Aoyagi, K. Ogawa, H. Naganawa, M. Hamada, and T. Takeuchi, J. Antibiotics, 37, 422 (1984). (Original; IC50 & Chem. Structure) • This compound is distributed through the Peptide Institute, Inc. under the license of Microbial Chemistry Research Foundation.

Leu-Gly-Glyl-leucyl-glycyl-glycine (M.W. 245.28) C10H19N3O4

AA OLG-3025-20 °C

0.1 g1 g

30110

Pro-Leu-Gly-NH2 • ½H2O [MSH-Release Inhibiting Factor; MIF]

l-prolyl-l-leucyl-glycine amide • ½H2O

PMI-4024-20 °C

25 mg100 mg

3060

(M.W. 284.35 . 9.01) C13H24N4O3 . ½H2O [2002-44-0]

A. Vivas and M.E. Celis, J. Endocrinol., 78, 1 (1978). (Pharmacol.)

Pyr-His-Pro-NH2 • H2O TRH (Thyrotropin Releasing Hormone)

l-Pyroglutamyl-l-histidyl-l-proline amide (M.W. 362.39 • 18.02) C16H22N6O4 • 4H2O

AA PTR-4011-20 °C

25 g100 g

55150

R. Burgus, T.F. Dunn, D. Desiderio, and R. Guillemin, C.R. Acad. Sci. Paris, 269, 1870 (1969) (Original; Ovine) J. Bøler, F. Enzman, K. Folkers, C.Y. Bowers, and A.V. Schally, Biochem. Biophys. Res. Commun., 37, 705 (1969). (Original; Porcine)

Thr-Val-Leu [Schizophrenia Related Peptide]

l-threonyl-l-valyl-l-Leuine (M.W. 331.41) C15H29N3O5

C.E. Frohman, Chem. Eng. News, 55, 35 (1977). (Original)

PSC-4061-20 °C

25 mg100 mg

99205

TetrapeptidesArg-Gly-Asp-Ser • ½AcOH • 2H2O [Fibronectin Active Fragment (RGDS)]

l-arginyl-l-glycyl-l-aspartyl-l-Serine

PFA-4171-20 °C

25 mg100 mg

285910

(M.W. 433.42 • 30.03 • 36.03 ) C15H27N7O8 • ½CH3COOH • 2H2OM.D. Piershbacher and E. Ruoslahti, Nature, 309, 30 (1984). (Original) D.M. Haverstick, J.F. Cowan, K.M. Yamada, and S.A. Santoro, Blood, 66, 946 (1985). (Pharmacol.)

Page 73: Assay Methods Using Peptidyl-MCA Substrates (1) · The initial rate of increase in the AMC concentration can be monitored 1) fluorometrically at λex = 380 nm and λem = 460 nm (Fig.

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ENZYME INHIBITO

RS AND SuBSTRATESPRODUCT GRADE CODE QTy PRICE Gly-Gly-Tyr-Arg • AcOH • 2H2O

Glycyl-glycyl-l-tyrosyl-l-arginineOGG-3119

-20 °C

0.1 g1 g

70350

(M.W. 451.48 • 60.05 • 36.03) C19H29N7O6 • CH3COOH • 2H2O Affinity Ligand for PapainM.O. Funk, Y. Nakagawa, J. Skochdopole, and E.T. Kaiser, Int. J. Peptide Protein Res., 13, 296, (1979).

Phe-Met-Arg-Phe-NH2 • 1½ AcOH • 2H2O [FMRF-amide]

l-Phenyl-l-methionyl-l-arginyl-l-phenylalanine amide 1½AcOH • 2H2O

PFM-4142 -20 °C

25 mg100 mg

275790

(M.W. 598.76 • 90.08 • 36.03 ) C29H42N8O4S • 1½CH3COOH • 2H2O D.A. Price and M.J. Greenberg, Science, 197, 670 (1977). (Original)

Thr-Lys-Pro-Arg • 2AcOH • 4H2O [Tuftsin]

l-threonyl-l-lysyl-l-prolyl-l-arginine

PTF-4020-20 °C

25 mg100 mg

145340

(M.W. 500.59 • 120.10 • 72.06 ) C21H40N8O6 • 2CH3COOH • 4H2O [72103-53-8] Phagocytosis-Stimulating PeptideK. Nishioka, A. Constantpoulos , P.S. Satoh, and V.A. Najjar, Biochem. Biophys. Res. Commun., 47, 172 (1972). (Original) K. Nishioka, P.S. Satoh, A. Constantpoulos, and V.A. Najjar, Biochim. Biophys. Acta, 310, 230 (1973). (Chem. Synthesis & Pharmacol.)

Trp-Met-Asp-Phe-NH2 • HCl • H2O [CCK-Tetrapeptide (30-33)]

PCK-4083-20 °C

25 mg100 mg

120360

l-Trptophyl-l-methionyl-l-aspartyl-l-phenylalanine amide (M.W. 596.70 • 3646 • 18.02 ) C29H36N6O6S • HCI • H2O [5609-49-4]J.F. Rehfeld, L.I. Larsson, N.R. Goltermann, T.W. Schwarz, J.J. Holst, S.L. Jensen, and J.S. Morley, Nature, 284, 33 (1980). (Neural Pharmacol.)