Thioredoxin Reductase 1 (rat, recombinant, aa 3-499)

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 (rat, recombinant, aa 3-499) protein can be used for enzyme activity assay and Western blot (WB) applications.Synonyms: NADPH-dependent Thioredoxin Reductase, TrxR1, Txnrd1. Purity: >45% estimated by SDS-PAGE. Source: Active recombinant rat TrxR1 expressed in E. coli. Amino Acids: 3-499. MW: 54.5 kDa. Formulation: (Request formulation change), 50 mM Tris, pH 7.4, with 800 mM sodium chloride and 10% glycerol. Applications: Enzyme activity assay and Western blot (WB). Specific Activity: batch specific. UniProt Accession #: O89049.