Glutathione 1500 mg is supplied by Healthy Peps as a high-purity reduced tripeptide for antioxidant and enzymology research, shipped from Canada with batch documentation.
Healthy Peps Research Team · Research Editorial Team
Last reviewed November 2026. For in vitro laboratory research only.
Physicochemical Reference Data
| Compound | L-Glutathione, reduced form (γ-glutamyl-cysteinyl-glycine) |
| CAS Number | 70-18-8 |
| Molecular Formula | C10H17N3O6S |
| Molecular Weight | 307.32 g/mol |
| Appearance | White to off-white crystalline powder |
| Solubility (lab) | Water and aqueous buffers |
| Vial Format | 1500 mg |
| Storage | −20 °C, desiccated, protected from light |
Mechanism & Research Context
Glutathione is the most abundant non-protein thiol in mammalian cells and the substrate for antioxidant enzyme systems including glutathione peroxidase and glutathione S-transferase. The reduced form (GSH) and its oxidised disulfide (GSSG) form a redox couple, and the GSH:GSSG ratio is one of the most widely used markers of oxidative status in cell biology.
In the literature, glutathione is studied for its role in cellular defence against reactive oxygen species, in phase II detoxification reactions, and in modulating the efficacy and toxicity of chemotherapeutic agents. Its clinical history includes use as an adjunctive agent in chemotherapy research, where published work examines whether it reduces the neurotoxicity associated with platinum-based compounds.
For laboratory use, it is a standard reagent in oxidative-stress assays, GSH/GSSG ratio measurements, glutathione-S-transferase and peroxidase activity assays, and protein-protection studies. The reduced form is the correct reagent for these assays, which is why the oxidation state is stated explicitly on this listing.
The 1500 mg quantity suits laboratories preparing their own assay buffers at defined concentrations rather than working from small analytical aliquots.
How It Compares to Related Peptides
Glutathione is a small tripeptide reagent rather than a receptor-ligand peptide: it is water-soluble at high concentration, is used as an assay substrate and antioxidant standard, and its oxidation state is analytically critical. It is not interchangeable with any other item on this catalogue.
Reconstitution, Stability & Handling
Prepare working solutions in water or the buffer specified by your assay. Reduced glutathione oxidises in solution, particularly with aeration or at alkaline pH, so solutions should be prepared fresh and kept cold. The bulk powder should be kept desiccated at −20 °C away from light and allowed to reach room temperature before opening.
Selected Reading & Research Notes
- Glutathione redox biology literature. Establishes the GSH/GSSG couple as the primary thiol redox buffer in mammalian cells and a standard oxidative-stress marker.
- Adjunctive glutathione chemotherapy research. Examines glutathione in the context of platinum-compound toxicity and antioxidant status in treated patients.
Frequently Asked Questions
Where can I buy glutathione in Canada?
Healthy Peps ships glutathione Canada-wide from within Canada with batch documentation and an available COA.
Is this the reduced or oxidised form?
This is the reduced form (GSH), CAS 70-18-8 — the correct reagent for glutathione peroxidase, transferase and GSH/GSSG ratio assays.
How stable are glutathione solutions?
Reduced glutathione oxidises over time in aqueous solution, so working solutions are prepared fresh and kept cold, and the powder is stored desiccated at −20 °C.
Is glutathione for human consumption?
No. It is supplied as a laboratory research reagent and is not intended for human or veterinary use.
Why 1500 mg?
The larger quantity supports laboratories that prepare their own assay buffers at defined molar concentrations across many plates.
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