Summary:
glutathione S-transferase alpha 3
Cat：P07705
| 【Derived From】： E.coli |
| 【Endotoxin】： Not measured |
| 【Amino Acid】： 1-223aa |
| 【Purity】： ≥85% by SDS-PAGE. |
| 【Name】： GSTA3 |
| 【Full Name】： glutathione S-transferase alpha 3 |
| 【Uniprot】： Q16772 |
| 【Gene ID】： 2940 |
| 【Mol Mass】： 25kDa |
| 【Application】： Immunology research |
| 【Purification】： NI-NTA affinity purification |
| 【Bioactive】： No activity experimental data, to be verified. |
| 【Tag】： With a 6×His tag at the N/C-terminus. |
| 【Concentration】： 1mg/ml by SDS-PAGE. |
Store:
| 【Reconstitution】： Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 10μg/ml. Dissolve the lyophilized protein in distilled water.) |
| 【Storage】： Reconstituted protein solution can be stored at 4-7℃ for 2-7 days， stored at < -20℃ for 1 year. |
| 【Formulation】： Powder: Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0. |
Background:
Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. 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 genes that are located in a cluster mapped to chromosome 6. Genes of the alpha class are highly related and encode enzymes with glutathione peroxidase activity. However, during evolution, this alpha class gene diverged accumulating mutations in the active site that resulted in differences in substrate specificity and catalytic activity. The enzyme encoded by this gene catalyzes the double bond isomerization of precursors for progesterone and testosterone during the biosynthesis of steroid hormones. An additional transcript varian
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