Thioredoxin 1 (E. coli) Polyclonal Antiserum

Thioredoxin 1 (Trx1) is a thiol-disulfide oxidoreductase and part of the antioxidant thioredoxin system that is involved in the maintenance of cellular thiol redox homeostasis.{57135,57136,57138} It is ubiquitously expressed, localizes primarily to the cytoplasm with some nuclear localization, and is upregulated in and released from cells under conditions of oxidative stress.{57135,57136,57137} E. coli Trx1 contains two active site cysteine residues at positions 32 and 35, and human Trx1 contains additional cysteines at positions 62, 69, and 73.{57136,20429} During the catalytic cycle, the active site cysteines are oxidized to a disulfide upon reduction of oxidized protein disulfide substrates and are subsequently restored to their reduced state by thioredoxin reductase (TrxR) and NADPH.{57135,57136} In mammals, Trx1 regulates redox-sensitive transcription factors including NF-?B, p53, and the glucocorticoid receptor, as well as inhibits apoptosis through redox-sensitive binding and regulation of apoptosis signal-regulating kinase 1 (ASK1).{57136,57137} E. coli Trx is a substrate for mammalian thioredoxin reductase but is more stable than mammalian Trx, with oxidation not affecting its activity or inducing its aggregation.{20429} Cayman’s Thioredoxin 1 (E. coli) Polyclonal Antiserum can be used for immuno-inhibition of Trx1 activity.