Recombinant Human Thioredoxin

Source : Escherichia Coli. Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 11.7 kDa. 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.

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.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

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