Glutathione (GSH): an antioxidant tripeptide with documented purity

Glutathione is made of three amino acids: glutamate is attached to cysteine through an atypical γ-carboxyl bond, and glycine is attached to cysteine through an ordinary α-bond. That γ-bond is what makes the molecule resistant to cleavage by most intracellular peptidases; the free thiol (-SH) group of cysteine is responsible for its reducing activity. Molecular formula: C₁₀H₁₇N₃O₆S, molar mass 307.32 g/mol, CAS 70-18-8. Inside the cell, glutathione works as a pair with its oxidised form GSSG: it is the main intracellular thiol redox buffer and a cofactor of the enzyme glutathione peroxidase, and glutathione S-transferases use it to conjugate electrophilic compounds. This describes the biochemistry of the molecule, not a promised effect. The full breakdown of the mechanism with primary-source citations is in the monograph at /en/wiki/glutathione.

Longeva sends samples for analysis to independent third-party laboratories itself (Janoshik, Testides, Uzorak, North American Diagnostics) rather than relying on the raw-material supplier's figures alone. These are third-party labs in the plain sense: none of them holds ISO 17025 accreditation, and we do not claim otherwise. Longeva peptide batches come with a certificate of analysis; published reports are collected in the open archive at /en/coa, searchable by product name or batch number. If there is no report for your particular glutathione batch yet, check back later: the archive fills up as new analyses come in.