Thioredoxin Reductase 1 (human, recombinant)

Thioredoxin reductase 1 (TrxR1) is an oxidoreductase encoded by the TXNRD1 gene in humans and a member of the antioxidant thioredoxin system, which is involved in the maintenance of cellular thiol redox homeostasis. 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 TrxR1. TrxR1 is ubiquitously expressed, localizes to the cytoplasm, and is regulated by the antioxidant transcription factor Nrf2. TrxR1 catalyzes the NADPH-dependent reduction of oxidized thioredoxin (Trx), restoring the disulfide reductase function of Trx, which regulates redox-sensitive transcription factors, such as NF-kappaB and p53, and has roles in apoptosis and cell signaling. Genome-wide deletion of Txnrd1 is embryonic lethal in mice. Increased serum TrxR1 activity is associated with reduced progression-free survival in patients with non-small cell lung cancer (NSCLC). Cayman's Thioredoxin Reductase 1 (human, recombinant) protein can be used for enzyme activity assay.Synonyms: NADPH-dependent Thioredoxin Reductase, TrxR1, Txnrd1. Purity: >95% estimated by SDS-PAGE. Source: Active recombinant human TrxR1 expressed in E. coli. Amino Acids: 499 residues. Formulation: (Request formulation change), TE buffer with 50% glycerol. Applications: WB.