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Glutathione is a tripeptide cysteine-glycine-glutamic acid which exists in cells in the reduced form (this product) or oxidised form. Reduced glutathione (GSH) is an antioxidant protecting cell components from endogenous and exogeneous reactive oxygen and nitrogen species. Reduced glutathione has also been intensely used in the affinity purification of proteins with glutathione S-transferase (GST) tag. In the protein purification process, glutathione is used for the elution of GST-fused recombinant proteins from a glutathione-immobilised resins. In the elution buffers, reduced glutathione is typically used in the 10 – 40 mM concentration range.

Glutathione is a tripeptide comprised of three amino acids (cysteine, glutamic acid, and glycine) present in most mammalian tissue. Glutathione acts as an antioxidant, a free radical scavenger and a detoxifying agent. Glutathione is also important as a cofactor for the enzyme glutathione peroxidase, in the uptake of amino acids, and in the synthesis of leukotrienes. As a substrate for glutathione S-transferase, this agent reacts with a number of harmful chemical species, such as halides, epoxides and free radicals, to form harmless inactive products. In erythrocytes, these reactions prevent oxidative damage through the reduction of methemoglobin and peroxides. Glutathione is also involved in the formation and maintenance of disulfide bonds in proteins and in the transport of amino acids across cell membranes