Glutathione 1500mg

Glutathione (GSH) is a tripeptide unlike any other peptide we stock. The three residues — glutamate, cysteine, glycine — would form an unremarkable short peptide if linked by standard α-peptide bonds. What makes Glutathione distinctive is the γ-glutamyl bond between glutamate and cysteine: the glutamate's side-chain γ-carboxyl forms the peptide bond rather than its α-carboxyl. This unusual linkage makes Glutathione resistant to virtually all standard peptidases (which cleave α-bonds) and is the structural basis for its role as the dominant non-protein thiol in cellular redox chemistry. This guide explains what Glutathione is, the published research context, and how its quality is independently verified.

Glutathione has the structure γ-L-Glutamyl-L-cysteinyl-glycine — three amino acids with the non-standard γ-bond at the glutamate. The active redox group is the free thiol (-SH) on the cysteine side chain, which can exist as the reduced form (GSH, sulfhydryl) or the oxidized form (GSSG, a disulfide-linked dimer). The molecular weight of reduced GSH is approximately 307.32 g/mol with the empirical formula C10H17N3O6S. It is supplied as a lyophilized white powder for laboratory reconstitution.

Glutathione is sold strictly for laboratory and research use. It is not approved by the FDA or any other regulatory body for human or veterinary use, and nothing in this guide constitutes guidance for human administration.

Published research on Glutathione spans virtually every aspect of cellular biology that involves redox state. GSH is the dominant intracellular reducing agent — present at millimolar concentrations in most cell types, which is exceptionally high for a metabolite — and serves as the cofactor for glutathione-S-transferase enzymes in phase-II detoxification chemistry, for glutathione peroxidases in peroxide reduction, and for many smaller redox-relay reactions. The GSH:GSSG ratio is a primary cellular indicator of redox state, with healthy cytosol typically maintaining ratios in the range of 100:1 to 1000:1 in favor of the reduced form. Research literature on Glutathione touches oxidative stress, hepatology, immunology, and aging biology — researchers should evaluate primary sources directly within their specific subfield.

Glutathione quality verification is distinctive: in addition to total purity, the GSH:GSSG ratio is itself a quality indicator, since GSH spontaneously oxidizes to GSSG when exposed to air and moisture. Every batch of MHS Longevity Glutathione is submitted to an independent third-party laboratory before release:

Lyophilized Glutathione should be stored at -20°C or below for extended stability. The free thiol on the cysteine residue makes GSH inherently sensitive to oxidation — the molecule will slowly equilibrate toward GSSG even in the dry state under suboptimal storage. Once reconstituted, the solution oxidizes faster, particularly in oxygenated buffers; single-use aliquoting in deoxygenated buffer where the protocol allows preserves the reduced form across a study timeline. Protection from light, moisture, and oxidizing contaminants applies throughout. Standard aseptic technique applies during reconstitution.