THIOREDOXIN

The Uses of THIOREDOXIN

Thioredoxin from Escherichia coli has been used in thioredoxin reductase assay, peroxidase-coupled thioredoxin system assay and peroxiredoxin assay.

Background

Thioredoxin is a small dithiol protein and specific reductant for major allergenic proteins present in foods from animal and plant products. It is a 12-kD oxidoreductase enzyme encoded by TXN and TXN2 genes that contains a dithiol-disulfide active site. It plays an essential role as an antioxidant in neutralizing food allergens and redox signalling. Allergens containing disulfide bonds are inactivated when reduced by thioredoxin.

General Description

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.

Biochem/physiol Actions

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.

Metabolism

Not Available