Glutathione (GSH)

Glutathione (GSH) is a low molecular weight thiol-containing tripeptide composed of L-glutamate, L-cysteine, and glycine, linked by an unusual peptide bond between the amino group of cysteine and the carboxyl group of the glutamate side chain, and a normal peptide bond between cysteine and glycine. This unique structure, particularly the sulfhydryl group of cysteine, is central to its biological activity. Historically, GSH was discovered in 1888 by J. de Rey-Pailhade and later isolated and characterized by F.G. Hopkins in 1921. Its significance in cellular defense mechanisms has been a subject of extensive research since the mid-20th century. Research has elucidated its involvement in detoxification processes, regulation of gene expression, cell proliferation, and immune function. Biochemically, GSH exists in both reduced (GSH) and oxidized (GSSG) forms, with the GSH/GSSG ratio serving as a crucial indicator of cellular oxidative stress. GSH participates in various enzymatic reactions, including those catalyzed by glutathione peroxidases and glutathione S-transferases, which are vital for neutralizing reactive oxygen species and detoxifying xenobiotics. Its direct antioxidant activity involves the donation of an electron from its thiol group to free radicals, thereby reducing them to less reactive species. Research applications include studies on oxidative stress mechanisms, enzyme kinetics, and cellular signaling pathways. This product is intended solely for in vitro laboratory research and not for human or animal consumption.