Thioredoxin E.Coli Recombinant Shipping: Synonyms Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856. Introduction 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. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. 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. This could be especially useful in refolding proteins expressed in E. coli. To this end, thioredoxin has been shown to act as a protein disulfide isomerase.Its Molecular Weight is 11.9kDa. and the pI is 4.67. Description Recombinant Thioredoxin was purified from E. coli harboring its gene. Source Escherichia Coli. Physical Appearance Sterile Lyophilized Powder. Formulation Each mg of protein contains 20mM phosphate buffer pH 7.4. Solubility It is recommended to reconstitute the lyophilized TRX in sterile 18MΩ-cm H2O. Stability TRX although stable at 4°C for 3 weeks, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence >