Anti-GSTA1/GSTA2/GSTA3/GSTA4/GSTA5 Antibody Fluoro488 Conjugated

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding these enzymes are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of some drugs. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase belonging to the alpha class. The alpha class genes, located in a cluster mapped to chromosome 6, are the most abundantly expressed glutathione S-transferases in liver (hepatocytes) and kidney (proximal tubules) . In addition to metabolizing bilirubin and certain anti-cancer drugs in the liver, the alpha class of these enzymes exhibit glutathione peroxidase activity, thereby protecting the cells from reactive oxygen species and the products of peroxidation.

Glutathione S-transferase A1; GST HA subunit 1; GST class-alpha member 1; GST-epsilon; GSTA1-1; GTH1; Glutathione S-transferase A1, N-terminally processed; GSTA1

1. Atkinson, HJ; Babbitt, PC (Nov 24, 2009) . Glutathione transferases are structural and functional outliers in the thioredoxin fold.. Biochemistry 48 (46) : 11108–16. 2. Boyer TD (March 1989) . The glutathione S-transferases: an update. Hepatology 9 (3) : 486–96.