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 GST family consists of three superfamilies:the cytosolic, mitochondrial, and microsomal—also known as MAPEG—proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new GST functions.
In the genetic engineering, GST is commonly used to construct high efficiency expression vectors, and thenco-expression with a number of difficult expression proteins as a molecular chaperone, finally achieving a soluble expression.
White powder, lyophilized or colorless liquid
Enzyme Commission Number
About 26kDa (SDS-PAGE detection)
>90% (SDS-PAGE test)
4°C, store at -20°C for long-term preservation.
Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 220.127.116.11; 50812-37-8