Thioredoxin Reductase 1 (rat, 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.{14257,52830,57136} 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.{52831,14257} TrxR1 is ubiquitously expressed, localizes to the cytoplasm, and is regulated by the antioxidant transcription factor Nrf2.{52830,52832} 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-?B and p53, and has roles in apoptosis and cell signaling.{52833,57136} Genome-wide deletion of Txnrd1 is embryonic lethal in mice.{52834} Increased serum TrxR1 activity is associated with reduced progression-free survival in patients with non-small cell lung cancer (NSCLC).{52835} Cayman’s Thioredoxin Reductase 1 (rat, recombinant; aa 3-499) protein can be used for enzyme activity assay and Western blot (WB) applications.