Thioredoxin 1 (mouse, recombinant, His-tagged)

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-kappaB, p53, and the glucocorticoid receptor, as well as inhibits apoptosis through redox-sensitive binding and regulation of apoptosis signal-regulating kinase 1 (ASK1). 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 (mouse, recombinant, His-tagged) protein can be used for enzyme activity assay and Western blot applications.Synonyms: Trx1, TrxA, Txn1. Purity: >75%. Source: Active recombinant mouse His-tagged thioredoxin 1 expressed in E. coli. Amino Acids: 2-105. MW: 13.8 kDa. Formulation: (Request formulation change), 50 mM Tris-HCl, pH 7.8, with 150 mM sodium chloride, 10% glycerol, 1 mM EDTA, and 0.1 mM DTT. UniProt Accession #: P10639.