10482_2013_13_MOESM2_ESM
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Figure S1. Overexpression and purification of recombinant His-ChrS protein. a, 15% SDS-PAGE of crude extracts of E. coli XL10-Gold(pTrcHis-ChrS) uninduced (lanes labeled NI) or induced with 0.5 mM IPTG (lanes I). Protein molecular mass markers are shown to the left in kilodaltons. The position of the His-ChrS protein is also indicated. b, detection of His- ChrS by Western blotting. A duplicate of the gel in (A) was blotted, incubated with the HisProbe-HRP reagent, and detected with Super Signal West Pico, as described under Methods. c, 15% SDS-PAGE of the purification of His-ChrS by Ni-NTA affinity-chromatography. The protein was purified from the soluble fraction of IPTG-induced E. coli XL10-Gold(pTrcHis- ChrS) cells as described in Methods. CE, crude extract; P, purified protein c b a
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a. b. c. - PowerPoint PPT Presentation
Transcript of 10482_2013_13_MOESM2_ESM
Figure S1. Overexpression and purification of recombinant His-ChrS protein.
a, 15% SDS-PAGE of crude extracts of E. coli XL10-Gold(pTrcHis-ChrS)
uninduced (lanes labeled NI) or induced with 0.5 mM IPTG (lanes I). Protein
molecular mass markers are shown to the left in kilodaltons. The position of the
His-ChrS protein is also indicated. b, detection of His-ChrS by Western blotting. A
duplicate of the gel in (A) was blotted, incubated with the HisProbe-HRP reagent,
and detected with Super Signal West Pico, as described under Methods. c, 15%
SDS-PAGE of the purification of His-ChrS by Ni-NTA affinity-chromatography. The
protein was purified from the soluble fraction of IPTG-induced E. coli XL10-
Gold(pTrcHis-ChrS) cells as described in Methods. CE, crude extract; P, purified
protein
cba
