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.

Glutathione-Agarose has been used:

• to purify glutathione S-transferase (GST)-fused protein for generating polyclonal antibody M4P
• to incubate supernatant fractions for the purification of full-length p53 (aa 1-393) and its DNA-binding domain (aa 94-288)
• in affinity purification of the fusion protein

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.

One g powder swells to ≥10 ml of gel

Lyophilized powder stabilized with lactose