|Other Names||Glutathione S-transferase A2, GST HA subunit 2, GST class-alpha member 2, GST-gamma, GSTA2-2, GTH2, GSTA2, GST2|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.|
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Provided below are standard protocols that you may find useful for product applications.
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.
Tars, K., et al. J. Mol. Biol. 397(1):332-340(2010)Moyer, A.M., et al. Cancer Epidemiol. Biomarkers Prev. 19(3):811-821(2010)Gemignani, F., et al. Mutat. Res. 671 (1-2), 76-83 (2009) Rohrdanz, E., et al. Arch. Biochem. Biophys. 298(2):747-752(1992)Bogaards, J.J., et al. Biochem. J. 286 (PT 2), 383-388 (1992) Klone, A., et al. Biochem. J. 285 (PT 3), 925-928 (1992)
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