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. 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. Trx1 contains two active site cysteine residues at positions 32 and 35, with additional cysteines at positions 62, 69, and 73. 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. It 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). Exogenous administration of extracellular recombinant human Trx1 has anti-inflammatory effects in a variety of animal models. Trx1 levels are increased in a variety of human primary tumors, and increased tumor levels of Trx1 are associated with decreased survival in patients with colorectal cancer. Cayman''s Thioredoxin 1 (human) Polyclonal Antibody can be used for ELISA, immunohistochemistry (IHC), and Western blot (WB) applications.
