Description
Description: Disulfide Oxidoreductase produced in E Coli is a periplasmic protein isolated from E Coli, containing 208 amino acids having a molecular mass of 23,149 Dalton. The DsbA is purified by proprietary chromatographic techniques.
Introduction: DsbA appears to be necessary for correct formulation of disulfide bonds in exported proteins in vivo. DsbA is useful as a standard in immunoblotting. This protein catalyses the reduction and exchange of disulfide bonds and the oxidation of free sulfhydryl groups in vitro. It is the strongest oxidant of the thioredoxin superfamily. This thio/disulfide oxidoreductase is required for efficient disulfide bond formation in the periplasm of E. coli