Thioredoxin Reductase 2 (human, recombinant)

Thioredoxin reductase 2 (TrxR2) is an oxidoreductase encoded by the TXNRD2 gene in humans and a member of the antioxidant thioredoxin system. It exists as a homodimer and contains a dimer interface domain, FAD- and NADPH-binding domains, an N-terminal redox catalytic site, and a C-terminal selenocysteine residue, which is essential for the catalytic activity of TrxR2. TrxR2 is ubiquitously expressed and localizes primarily to the mitochondria. It catalyzes the NADPH-dependent reduction of oxidized thioredoxin 2 (Trx2), restoring the disulfide reductase function of Trx2, which reduces peroxiredoxin-3 (Prx3) dimers. TrxR2 has roles in the maintenance of mitochondrial integrity and redox homeostasis in the aging heart and in the regulation of chondrocyte viability, proliferation, and differentiation. Genome-wide deletion of Txnrd2 is embryonic lethal in mice. TXNRD2 expression and TrxR2 protein levels are increased in bone biopsies from patients with osteosarcoma that later progress to metastatic disease. SNPs in TXNRD2 are associated with serum markers of selenium status in patients with advanced- or high-stage, but not localized low-grade, prostate cancer. Cayman's Thioredoxin Reductase 2 (human, recombinant) protein can be used for enzyme activity assays.Synonyms: NADPH-dependent Thioredoxin Reductase 2, TrxR2, Txnrd2. Purity: >95% estimated by SDS-PAGE. Source: Active recombinant human TrxR2 expressed in E. coli. Amino Acids: 488 residues. Formulation: (Request formulation change), TE buffer with 50% glycerol.