Thioredoxin 1 (C61S/C72S mutant, human, recombinant)

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. In the human recombinant enzyme, the initiating methionine is removed, and thus the positions of the amino acids are counted without the N-terminal methionine. Cysteine-to-serine substitutions at Cys61 (C61S) and Cys72 (C72S) in Trx1 (Trx1C61S/C72S) prevent oxidation-induced inhibition of protein disulfide reductase activity in Trx1. Cayman's Thioredoxin 1 (C61S/C72S mutant, human, recombinant) protein can be used for enzyme activity assays.Synonyms: Trx1, TrxA, Txn1. Purity: >85% estimated by SDS-PAGE. Source: Active recombinant human thioredoxin 1 (C61S/C72S mutant) expressed in E. coli. Amino Acids: Full length. MW: 11.7 kDa. Formulation: (Request formulation change), Lyophilized in 50 mM Tris-HCl, pH 7.5, with 1 mM EDTA. UniProt Accession #: P10599.