Glutathione-Agarose: sc-2009

Glutathione-Agarose is a bioconjugated form of agarose, a natural polymer extracted from seaweed, that is extensively utilized in biochemical and molecular biology research, particularly for the affinity purification of glutathione S-transferases (GST) and GST-fusion proteins. This affinity medium consists of glutathione, a tripeptide composed of glutamate, cysteine, and glycine, covalently coupled to agarose beads through stable thioether bonds. The primary mechanism of action for Glutathione-Agarose revolves around its high affinity for GST, a family of enzymes involved in detoxification processes. GST-fusion proteins, which are genetically engineered proteins tagged with GST, can be selectively bound to and eluted from glutathione-agarose columns. This facilitates the purification of these proteins from complex biological mixtures, allowing researchers to study protein interactions, functions, and structures in a purified form. Moreover, this method is advantageous for isolating proteins expressed in recombinant DNA technology applications, where high purity is crucial. The specificity and efficiency of glutathione-agarose in binding GST-tagged proteins make it an invaluable tool in proteomics research, enabling the detailed analysis of protein pathways and interactions without the encumbrance of clinical or therapeutic considerations.

Glutathione-Agarose References:

1. Expression of two glutathione S-transferase genes in the yeast Issatchenkia orientalis is induced by o-dinitrobenzene during cell growth arrest.  |  Tamaki, H., et al. 1999. J Bacteriol. 181: 2958-62. PMID: 10217793
2. Determination of some kinetic and characteristic properties of glutathione S-transferase from bovine erythrocytes.  |  Gυvercin, S., et al. 2008. Protein Pept Lett. 15: 6-12. PMID: 18221006
3. Purification and partial characterization of glutathione S-transferase from insecticide-resistant field populations of Liposcelis paeta Pearman (Psocoptera: Liposcelididae).  |  Wu, S., et al. 2009. Arch Insect Biochem Physiol. 70: 136-50. PMID: 19140127
4. Purification and study of a bacterial glutathione S-transferase.  |  Arca, P., et al. 1990. FEBS Lett. 263: 77-9. PMID: 2185038
5. The effect of some antineoplastic agents on glutathione S-transferase from human erythrocytes.  |  Erat, M. and Şakiroğlu, H. 2013. J Enzyme Inhib Med Chem. 28: 711-6. PMID: 22512726
6. An alternative easy method for antibody purification and analysis of protein-protein interaction using GST fusion proteins immobilized onto glutathione-agarose.  |  Zalazar, L., et al. 2014. Anal Bioanal Chem. 406: 911-4. PMID: 24337186
7. Glutathione S-transferases in Fasciola hepatica.  |  Howell, MJ., et al. 1988. J Parasitol. 74: 715-8. PMID: 3294369
8. Expression, Purification, and Biophysical Characterization of Klebsiella Pneumoniae Nicotinate Nucleotide Adenylyltransferase.  |  Daya, T., et al. 2022. Protein J. 41: 141-156. PMID: 35083643
9. Isolation and biochemical characterisation of a glutathione S-transferase from Echinococcus granulosus protoscoleces.  |  Fernández, C. and Hormaeche, CE. 1994. Int J Parasitol. 24: 1063-6. PMID: 7883440
10. Anti-oncogene product p53 binds DNA helicase.  |  Sakurai, T., et al. 1994. Exp Cell Res. 215: 57-62. PMID: 7957681
11. Biochemical properties of cloned glutathione S-transferases from Schistosoma mansoni and Schistosoma japonicum.  |  Walker, J., et al. 1993. Mol Biochem Parasitol. 61: 255-64. PMID: 8264729
12. Glutathione S-transferases from the white-rot fungus, Phanerochaete chrysosporium.  |  Dowd, CA., et al. 1997. Biochem J. 324 (Pt 1): 243-8. PMID: 9164863
13. Glutathione-binding proteins of Setaria digitata: antibody responses in human infected with Wuchereria bancrofti.  |  Bal, M. and Das, MK. 1996. Parasite Immunol. 18: 473-7. PMID: 9226683
14. Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli.  |  Tudyka, T. and Skerra, A. 1997. Protein Sci. 6: 2180-7. PMID: 9336840