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.
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.
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