DsbA, Thiol:disulfide interchange protein dsbA.

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.

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.

Escherichia Coli.

Sterile Filtered White lyophilized (freeze-dried) powder.

The protein was lyophilized after from a sterile solution containing 50mM sodium phosphate buffer and 100mM sodium chloride.

It is recommended to reconstitute the lyophilized DsbA in sterile 18MΩ-cm H2O not less than 100 μg/ml, which can then be further diluted to other aqueous solutions.

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.

Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

The sequence of the first five N-terminal amino acids
was determined and was found to be Met-Ly-Lys-Ala-Trp.

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