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.1,2,3 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.1,2,4 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 73.2,5 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.1,2 In mammals, Trx1 regulates redox-sensitive transcription factors including NF-κB, p53, and the glucocorticoid receptor, as well as inhibits apoptosis through redox-sensitive binding and regulation of apoptosis signal-regulating kinase 1 (ASK1).2,4 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.5 Cayman’s Thioredoxin 1 (E. coli) Polyclonal Antiserum can be used for immuno-inhibition of Trx1 activity.WARNING This product is not for human or veterinary use.
