Overview
Glutathione (GSH) is a naturally occurring tripeptide composed of glutamate, cysteine, and glycine, joined by an unusual γ-peptide bond between the glutamate side-chain carboxyl and cysteine. It is the most abundant low-molecular-weight thiol in most cells and functions as the principal intracellular redox buffer. In its reduced form the molecule presents a free cysteine sulfhydryl (–SH) group that mediates its chemistry; two molecules oxidize to the disulfide dimer GSSG. It is supplied here as a research-grade reagent rather than as a peptide drug.
Mechanism as studied
The research literature characterizes glutathione as a cofactor for the glutathione peroxidase (GPx) enzymes, which reduce hydrogen peroxide and lipid hydroperoxides, and as the conjugation substrate for glutathione S-transferases (GSTs) in phase-II detoxification reactions. The reduced/oxidized couple (GSH/GSSG) is described as a central determinant of cellular redox potential, with glutathione reductase regenerating GSH from GSSG using NADPH. In vitro, the thiol group directly scavenges reactive oxygen and electrophilic species and participates in protein S-glutathionylation. These reactions are documented at the biochemical and cellular level.
Research context
Contexts in which this compound appears in the in-vitro and preclinical research literature:
- Cell-culture redox assays quantifying the GSH/GSSG ratio as an oxidative-stress readout.
- Enzymology of glutathione peroxidase and glutathione reductase coupled to NADPH.
- Phase-II conjugation studies with glutathione S-transferases and electrophilic substrates.
- Protein S-glutathionylation and thiol-redox signaling in cultured cells.
- Preclinical models of oxidative stress examining intracellular thiol pools.
Handling & storage
Handled as a research reagent, glutathione is supplied as a powder that is readily soluble in water or an appropriate aqueous buffer; dissolve to the working concentration required by the assay. Because reduced glutathione oxidizes to GSSG on standing in solution, prepare working solutions fresh and keep them chilled and protected from air. Aliquot stock to avoid repeated handling.
Store the sealed powder at −20 °C, protected from light and moisture, where it is stable long-term. Aqueous solutions are prone to air-oxidation and should be prepared fresh, kept cold, and not subjected to repeated freeze–thaw.
Certificates of analysis
A certificate of analysis for the current lot is in preparation and will be published in the certificate library. Lot documentation is available on request for this compound.
Order Glutathione
Lot-traceable, certificate-backed, and shipped cold-chain from the US.
For research use only
This guide is reference material for qualified researchers. The compound is an analytical-grade reference material supplied strictly for in-vitro laboratory research and development — not a drug, supplement, or medical device, and not for human or animal consumption or any therapeutic, clinical, or diagnostic use. No medical claims are made or implied.
