Reduced Glutathione

Glutathione (γ-L-Glutamyl-L-Cysteinylglycine, GSH) is a non-canonical tripeptide synthesised endogenously by every nucleated cell. It is the principal small-molecule cellular antioxidant, present at millimolar concentrations in most tissues, and serves as a reductant for glutathione peroxidase (the enzymatic detoxifier of hydrogen peroxide and lipid peroxides) and as a substrate for glutathione S-transferase (phase-II xenobiotic conjugation).

CAS 70-18-8, molecular formula C₁₀H₁₇N₃O₆S, molecular weight 307.32 g/mol. Wikidata QID Q116907, PubChem CID 124886, ChEMBL ID CHEMBL1543.

Glutathione's free thiol (the cysteine sulfhydryl group) is the redox-active centre. Cycling between reduced (GSH) and oxidised disulfide-bonded (GSSG) forms allows it to neutralise reactive oxygen and nitrogen species while being regenerated by glutathione reductase using NADPH. The cellular GSH/GSSG ratio is a sensitive indicator of oxidative state and is a regulated parameter in many cellular processes.

Investigated as both a research reagent (for redox studies, protein-thiol modification work) and as a research-grade reference compound for the substantial clinical literature on glutathione precursor supplementation (N-acetylcysteine) and direct glutathione administration in oxidative-stress- associated disease models.

Supplied as a research-grade reference standard for laboratory use only. Not a licensed medicinal product in the United Kingdom and not approved by the MHRA for human or veterinary administration. Sale is restricted to researchers, institutions and laboratory professionals; the compound must be retained within research premises. End-user compliance with the Human Medicines Regulations 2012, the Misuse of Drugs Act 1971 (where applicable) and local institutional biosafety policy is the responsibility of the buyer.