Description
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
Applications
Western Blot
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Product Overview
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.
Molecular Weight
23,149 Da
Purity
Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Stability
Lyophilized DsbA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DsbA should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Buffer
The protein was lyophilized after from a sterile solution containing 50mM sodium phosphate buffer and 100mM sodium chloride.
Synonyms
DsbA; Thiol:disulfide interchange protein dsbA; Disulfide Oxidoreductase
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