Description_x000D_ General description_x000D_ Thioredoxin reductase (TrxR) is encoded by TRXB gene. TrxR is one of the member of flavoprotein family of pyridine nucleotide-disulphide oxidoreductases, which also includes lipoamide dehydrogenase, glutathione reductase and mercuric ion reductase. Escherichia coli TrxR is a 70-kDa homodimeric flavoprotein, each monomer of this protein contains a FAD prosthetic group, an NADPH domain and an active site with redox-active disulphide. The catalytic site (-Cys-Ala-Thr-Cys-) in Escherichia coli TrxB is localized on the NADPH domain, whereas in humans TrxB catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) is part of the FAD domain._x000D_ Biochem/physiol Actions_x000D_ Thioredoxin reductase (TRXB) catalyzes the reduction of oxidized thioredoxin using nicotinamide adenine dinucleotide phosphate (NADPH). In thioredoxin pathway, this reduced thioredoxin reduce disulfide bonds in proteins localized in the cytoplasm and is implicated in the recycling of an essential enzyme ribonucleotide reductase. TrxR is essentially involved in protection against oxidation stress, cell growth and transformation, and the recycling of ascorbate from its oxidized form._x000D_ Physical form_x000D_ 1 mg/mL solution in 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol and 1mM DTT._x000D_ Preparation Note_x000D_ Centrifuge the vial prior to opening._x000D_ Other Notes_x000D_ MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA GTGCMAALDA ERYLDGLADA K.