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|Application ||WB, IHC-P, E|
|Other Accession||P08263, Q16772, Q7RTV2|
|Calculated MW||25664 Da|
|Antigen Region||1-30 aa|
|Other Names||Glutathione S-transferase A2, GST HA subunit 2, GST class-alpha member 2, GST-gamma, GSTA2-2, GTH2, GSTA2, GST2|
|Target/Specificity||This GSTA2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human GSTA2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||GSTA2 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.|
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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