γ-Glu-Cys-Gly

Glutathione (GSH) is a ubiquitous molecule found in many cells and tissues. The three amino acids present in GSH are glycine, cysteine, and glutamic acid.

L-Glutathione (GSH) reduced has been used in the elution buffer to elute GST (glutathione S-transferase)-fused proteins using glutathione-agarose beads. It has been used to prepare a standard curve for GSH analyses.

May be used at 5-10 mM to elute glutathione S-transferase (GST) from glutathione agarose.

Glutathione (GSH) forms conjugates with various metabolites and xenobiotics. It acts as an important co-factor for various enzymes. GSH is involved in many metabolic and signaling pathways. Glutathione functions as a thiol buffer for cellular proteins like thioredoxins and metallothioneins. GSH is also involved in the regeneration of antioxidants like tocopherols and ascorbate.

Endogenous antioxidant that plays a major role in reducing reactive oxygen species formed during cellular metabolism and the respiratory burst. Glutathione-S-transferase catalyzes the formation of glutathione thioethers with xenobiotics, leukotrienes, and other molecules that have an electrophilic center. Glutathione also forms disulfide bonds with cysteine residues in proteins. Via these mechanisms, it can have the paradoxical effect of reducing the efficacy of anti-cancer agents.

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