Rabbit anti-Human GSTA2 Polyclonal Antibody | anti-GSTA2 antibody
GSTA2, NT (GSTA2, GST2, Glutathione S-transferase A2, GST HA subunit 2, GST class-alpha member 2, GST-gamma, GSTA2-2, GTH2) (AP)
ELISA: 1:1,000
WB: 1:100-500
Applications are based on unconjugated antibody.
Western Blot (WB)
(Western blot analysis of GSTA2 Antibody (N-term) in MDA-MB231 cell line lysates (35ug/lane). GSTA2 (arrow) was detected using the purified Pab.)
Immunohistochemistry (IHC)
(Formalin-fixed and paraffin-embedded human hepatocarcinoma reacted with GSTA2 Antibody (N-term), which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated.)
NCBI and Uniprot Product Information
NCBI Description
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-tranferase 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. 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. [provided by RefSeq, Jul 2008]
Uniprot Description
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.