Thioredoxin from Escherichia coli has been used in thioredoxin reductase assay, peroxidase-coupled thioredoxin system assay and peroxiredoxin assay.
Recombinant, human thioredoxin expressed in E. coli. A ubiquitous protein with two redox-active half-cysteine residues that function as a general disulfide reductant. Works efficiently on model compounds (e.g. Ellman′s reagent, Cat. No. 322123) and protein disulfides. Plays an essential role in cellular protection against oxidative stress and cell death. Inhibits apoptosis in Jurkat T-cells and human PBL blasts. Occurs as a single polypeptide chain.
Thioredoxin from Escherichia coli catalyzes REDOX reactions and has a role in various biological processes. It modulates the structure and activity of many proteins. The enzyme thioredoxin reductase catalyzes the reduction of thioredoxin. Thioredoxin also has a role in oxidative stress response.
