Recombinant Yeast Thioredoxin

Thioredoxin-2, TRX2, TRX-2, TXN-2, TXN2.

Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.

Thioredoxin-2 Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 12.6kDa.

Escherichia Coli.

Sterile Lyophilized Powder.

Each mg of TRX2 protein contains 20mM phosphate buffer pH 7.4.

It is recommended to reconstitute the lyophilized TXN2 in sterile 18MΩ-cm H2O.

TXN2 although stable at 4°C for 3 weeks, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles.

Greater than 95.0% as determined by SDS-PAGE.

TXN2 activity is assayed by measuring the change in absorbance at 650 nm at 25°C 
The specific activity was found to be 3 units/mg.

SDS

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