Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.

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

Recombinant Thioredoxin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (2-109 a.a.) and having a molecular mass of 12.9kDa. TRX contains an amino acid His Tag N-terminus and is purified by proprietary chromatographic techniques.

Escherichia Coli.

Sterile Filtered colorless solution.

The TRX His Tag protein solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

Greater than 85.0% as determined by SDS-PAGE.

MHHHHHHMGS DKIIHLTDDS FDTDVLKADG AILVDFWAEW CGPCKMIAPI LDEIADEYQG KLTVAKLNID QNPGTAPKYG IRGIPTLLLF KNGEVAATKV GALSKGQLKE FLDANLAGS.

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