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| Product Data | |
| Description | Recombinant protein of human glutathione S-transferase alpha 2 (GSTA2) |
| Species | Human |
| Expression Host | HEK293T |
| Expression cDNA Clone or AA Sequence | Recombinant protein was produced with TrueORF clone, RC202479. Click on the TrueORF clone link to view cDNA and protein sequences. |
| Tag | C-Myc/DDK |
| Predicted MW | 25.5 kDa |
| Concentration | >50 ug/mL as determined by microplate BCA method |
| Purity | > 80% as determined by SDS-PAGE and Coomassie blue staining |
| Buffer | 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol |
| Reference Data | |
| Locus ID | 2939 |
| Refseq Size | 1320 |
| Cytogenetics | 6p12.2 |
| Refseq ORF | 666 |
| Synonyms | GST2; GSTA2-2; GTA2; GTH2 |
| Summary | 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] |
| Protein Pathways | Drug metabolism - cytochrome P450, Glutathione metabolism, Metabolism of xenobiotics by cytochrome P450 |
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