Thioredoxin (E. coli), (recombinant) (His-tag)

Thioredoxin (Trx) is a redox protein of approximately 12 kDa. Its primary domain is conserved across a number of Trx family members and contains a conserved catalytic site Cys-Gly-Pro-Cys. It is ubiquitous and found in many organisms from bacteria to mammals. Trx has been shown to function in cell proliferation, redox signaling and inhibition of apoptosis.
Trx is reduced by the NADPH-dependent flavoenzyme thioredoxin reductase, and in turn reduces other proteins such as protein disulfide isomerase (PDI) by cysteine thiol-disulfide exchange. Trx has been reported to selectively activate the DNA binding of a number of transcription factors such as p53, NFkB, AP1 and glucocorticoid receptor, resulting in alteration of gene transcription. The reduced Trx can supply reducing equivalents for ribonucleotide reductase, the essential enzyme for DNA synthesis, and thioredoxin peroxidase. As a cofactor for the peroxiredoxins, Trx plays a direct role in reducing oxidative species such as H₂O₂.