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Glutathione S-Transferase (GST), an antioxidant enzyme, is involved in the primary cellular defense mechanism against reactive oxygen species. Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The activity of GSTs is dependent upon a steady supply of GSH from the synthetic enzymes gamma-glutamylcysteine synthetase and glutathione synthetase, as well as the action of specific transporters to remove conjugates of GSH from the cell. The primary role of GSTs is to detoxify xenobiotics by catalyzing the nucleophilic attack by GSH on electrophilic carbon, sulfur, or nitrogen atoms of said nonpolar xenobiotic substrates, thereby preventing their interaction with crucial cellular proteins and nucleic acids.
Recombinant Schistosoma Japonicum GST expressed the target gene encoding Met1-Lys218.
Accession: P08515
Apparent Molecular Weight: 28 KDa, under reducing conditions
Endotoxin < 1 EU/µg
Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
| Form | Lyophilized powder |
| Solubility (25°C) | Reconstitute the lyophilized powder in distilled water to a concentration not less than 100 μg/mL. |
| Storage | Stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days and at -20°C for 3 months. |
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Products are for research use only. Not for human use. We do not sell to patients.
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