Reconstitution information: Add 0.2 mL of distilled water will yield a concentration of 500 µg/mL.
Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide-isomerase (PDI) and a number of transcription factors such as p53, NF-kB and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: ADF; ATL-derived factor; Thioredoxin; Trx; Txn; Txn1
Gene Aliases: ADF; AW550880; Trx1; Txn; Txn1
Molecular Function: oxidoreductase