Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. Disulphide bond isomerase (DsbC), a member of the thioredoxin superfamily, acts as a disulfide isomerase and converts aberrant disulfide bonds to correct ones. It also acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein.
SDS-PAGE - Disulfide-bond isomerase protein (ab51284)
ab51284 run on a 15% SDS-PAGE gel with molecular weight markers.
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