Recombinant Human Thioredoxin

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 Human Recombinant produced in, E. coli, is a single, non-glycosylated, polypeptide chain containing 105 amino acids.

Thyrodoxin human although stable at 4C for 1 week, should be stored desiccated below -18C. Please prevent freeze thaw cycles.

E. coli

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

Specific activity is 7-10 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin. Please refer to our activity assay protocol.