E. coli DsbC (aa 20 - 208), recombinant protein from E. coli
Escherichia coli dsbC (YP_003045913, 20 a.a. - 208 a.a.) partial recombinant protein expressed inEscherichia coli .
In 20 mM Tris, pH 7.5 (2 mM EDTA)
2-8°C short term, -20°C long term
DsbC rearranges incorrect disulfide bonds during oxidative protein folding.
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.