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Recombinant His-ChrS Protein Overexpression and Purification

This study presents the overexpression and purification of recombinant His-ChrS protein in E. coli XL10-Gold using Ni-NTA affinity chromatography. The process involves SDS-PAGE analysis of crude extracts and the purification steps. Western blotting was performed for protein detection.

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Recombinant His-ChrS Protein Overexpression and Purification

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  1. a b c 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

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