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Glutathione S-transferase (GST) is a protein with a molecular weight of 26 KDa that naturally occurs in eukaryotic cells. It belongs to the family of Phase II detoxification enzymes. Glutathione-Agarose consists of glutathione attached through its sulfur to epoxy-activated 4% cross-linked beaded agarose, resulting in a 12-atom (10-carbon) spacer. It is provided as a lyophilized powder stabilized with lactose.
Affinity chromatography using glutathione-agarose permits rapid, mild, non-denaturing and highly selective purification of proteins containing glutathione binding sequences, such as Glutathione S-Transferase (GST), glutathione peroxidase and glyoxalase I.
Biochem/physiol Actions
Glutathione S-transferases (GSTs), a superfamily of multifunctional detoxification isoenzymes, have a significant role in cellular signaling. GSTs are emerging as promising therapeutic targets due to the overexpression of specific isozymes in various tumors and their potential involvement in the development of other diseases such as neurodegenerative diseases, multiple sclerosis, and asthma.
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