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Research Peptide
Glutathione is a tripeptide antioxidant composed of glutamine, cysteine, and glycine.
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99%+ purity
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3AA
TRIPEPTIDE
Glu-Cys-Gly (γ-glutamylcysteinylglycine)
100K+
PUBLICATIONS
Most studied antioxidant molecule
307Da
MOL. WEIGHT
Master cellular antioxidant
GSH/GSSG
REDOX PAIR
Central to redox homeostasis
750mg
HIGH DOSE
Maximum research concentration
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Research
This listing supplies reduced glutathione (GSH) as a lyophilized reference material for in-vitro and preclinical laboratory work, presented at a 750 mg fill weight per vial. Glutathione is a tripeptide (C10H17N3O6S, CAS 70-18-8) built from three amino-acid residues — glutamine/glutamate, cysteine, and glycine — but it is not a conventional linear peptide. Its defining structural feature is an unusual gamma-glutamyl bond: the first residue is linked through the side-chain carboxyl rather than the alpha-carboxyl, a connectivity that makes the molecule resistant to standard aminopeptidases and gives it distinct chemistry from ordinary tripeptides. Laboratories therefore treat it as a thiol-bearing redox reagent rather than as a simple sequence peptide.
The functional center of the molecule is the free sulfhydryl (–SH) group contributed by the cysteine residue. This thiol is what makes glutathione a widely cited model redox reagent in bench research: it can be reversibly oxidized to the disulfide dimer GSSG, and the GSH/GSSG couple is used across many assay systems as a defined redox reference. Everything below concerns the research substance itself — its documented study history and its analytical fingerprint — and is not a statement about outcomes in humans or animals.
Glutathione is one of the most extensively characterized small molecules in cell biology, and the published work surrounding it is overwhelmingly in-vitro and preclinical. In cell-culture and biochemical systems it is frequently employed as a defined thiol source and as a component of the glutathione redox couple used to poise assay conditions. Reported experimental lines of inquiry include its role in enzyme-catalyzed conjugation reactions (glutathione-S-transferase assays), its interaction with the glutathione peroxidase and glutathione reductase enzyme systems, and its use as a standard in analytical methods that quantify intracellular thiol status. These are descriptions of laboratory systems only and are not evidence of any effect in humans or animals.
These references describe experimental laboratory work only. They are not medical claims, are not evidence of safety or efficacy in humans or animals, and should not be interpreted as guidance for any use outside a controlled research environment. This research is preliminary and ongoing, and nothing here is medical advice.
Each research lot is supplied as an off-white to white crystalline lyophilized solid and characterized before release, with results recorded on a lot-specific Certificate of Analysis (COA). Because glutathione is defined by its reactive thiol, analytical release emphasizes both purity of the target molecule and the redox state of that thiol — a sample partially oxidized to GSSG is chemically distinct even when the peptide backbone is intact.
The COA tied to the specific lot number received is the definitive analytical record for that material. Because purity and residual oxidized content can vary slightly between manufacturing batches, researchers should cite the lot COA rather than generic specifications when documenting experimental inputs, and retain it alongside experimental records to support reproducibility and traceability.
The reactivity that makes glutathione useful also makes it sensitive: the free thiol oxidizes on exposure to air, moisture, elevated temperature, and trace transition-metal ions. Standard laboratory practice is to allow sealed vials to equilibrate to room temperature before opening to limit condensation on the hygroscopic solid, and to prepare working solutions fresh in oxygen-poor, appropriately buffered research-grade solvent. Freshly prepared solutions are preferred because aqueous glutathione oxidizes over time; aliquoting and minimizing headspace air help preserve the reduced form. Specific temperature and stability windows for the solid and reconstituted solutions appear in the storage table on this page.
It is reduced glutathione (GSH), a tripeptide with molecular formula C10H17N3O6S (CAS 70-18-8) assembled from glutamine/glutamate, cysteine, and glycine residues. Its distinguishing structural feature is a gamma-glutamyl linkage on the first residue and a free cysteine thiol (–SH) group, which together set it apart from ordinary linear tripeptides and make it a defined thiol/redox reference material for bench research.
It ships as a lyophilized off-white to white crystalline solid in a sealed vial at a 750 mg fill weight, intended for reconstitution with a research-grade solvent under aseptic technique when preparing in-vitro experiments. The solid form supports shelf stability, and the thiol reagent is best used in freshly prepared solutions.
Purity is measured by HPLC and reported as a percentage of total peak area (specified ≥99%), with the method resolving reduced glutathione from the oxidized GSSG dimer and related impurities. Identity is confirmed separately by mass spectrometry against the theoretical mass for C10H17N3O6S. The lot-specific Certificate of Analysis documents these values plus appearance and is the authoritative record for the exact material received.
Its cysteine-derived free thiol can be reversibly oxidized to the disulfide GSSG, so the GSH/GSSG couple provides a well-defined redox pair used across many in-vitro assay systems to poise and reference redox conditions. This is a description of laboratory redox chemistry and characterization work only; it is not a claim about any effect in humans or animals.
Published work is predominantly in-vitro and biochemical, spanning glutathione-S-transferase conjugation chemistry, glutathione peroxidase and reductase enzyme assays, redox-buffer preparation using defined GSH/GSSG ratios, and its use as an analytical reference standard for thiol quantification. This research is preliminary and ongoing and describes laboratory systems only; it does not establish any human or animal outcome.
This product is sold strictly for in-vitro research and laboratory use only. It is not intended for human or animal consumption, diagnostic purposes, or therapeutic application.
By purchasing this product, you confirm that you are a qualified researcher operating within an appropriate laboratory environment and will use this compound in accordance with all applicable local, state, and federal regulations.
Amino Science Labs assumes no liability for misuse of this product outside of its intended research application.
Allow the sealed vial to reach room temperature before opening to limit condensation on the hygroscopic solid, then prepare working solutions fresh in appropriately buffered, low-oxygen research-grade solvent, since the free thiol oxidizes on exposure to air, moisture, heat, and trace metals. Aliquoting and minimizing air headspace help preserve the reduced form. Follow the temperature and stability windows in the storage table on this page.
No. This material is supplied strictly for in-vitro and laboratory research use by qualified researchers. It is not a drug, supplement, cosmetic, or food, is not intended for human or animal consumption or any diagnostic or therapeutic purpose, and nothing on this page constitutes medical advice.
