Description
Glutathione (GSH) is the tripeptide γ-glutamyl-cysteinyl-glycine, the most abundant small thiol in animal cells and the reference molecule for redox biology. Labs use it in enzyme assays, redox buffers and oxidative-stress models. Pure Peptides Canada supplies reduced glutathione as a lyophilized research reagent in 600 mg and 1500 mg vials, with an independent Janoshik HPLC and mass-spectrometry report, CAD pricing and tracked shipping from inside Canada.
Glutathione at a glance
- What it is: reduced glutathione, a tripeptide with an unusual gamma bond between glutamate and cysteine and a free thiol that does the chemical work.
- Where it is used: glutathione peroxidase and S-transferase assays, GSH/GSSG redox buffers for protein refolding, oxidative-stress cell models and cell culture.
- Key handling fact: GSH oxidizes to the disulfide GSSG in air and in solution, which is why it ships dry.
- Supplied as: sealed lyophilized powder, 600 mg or 1500 mg, single vial or box of 10.
- Delivery: ships from inside Canada by tracked Xpresspost in 3–7 days ($25 CAD), or free in 4–12 days on orders over $299.
Glutathione (reduced)
GSH · γ-L-glutamyl-L-cysteinyl-glycine · tripeptide thiol
- γ-Glu
- Cys
- Gly
Blue: glutamate joined through its side-chain (gamma) carboxyl, not the usual peptide bond. The cysteine thiol carries the redox activity.
- Molecular formula
- C10H17N3O6S
- Molecular weight
- 307.32 g/mol
- CAS number
- 70-18-8
- Oxidized form
- Glutathione disulfide (GSSG), 612.6 g/mol
- Form
- Lyophilized powder, sealed vial
- Sizes
- 600 mg · 1500 mg (single or box of 10)
- SKU
- PP-GSHGLUTATHIONE
Where the evidence stands
- Cell studies
- Animal models
- Human studies
- Approved in Canada
Glutathione biology is well established. This vial is a laboratory reagent and is not authorized for human use in Canada.
What is glutathione?
Glutathione was first noticed in 1888 and named by Frederick Gowland Hopkins in 1921, with its tripeptide structure settled by 1929. Cells build it in two steps: glutamate-cysteine ligase joins glutamate to cysteine through the glutamate side chain, and glutathione synthetase adds glycine. That gamma linkage protects it from ordinary peptidases, which helps explain why cells can maintain it at millimolar concentrations.
The cysteine thiol is the active part. Glutathione donates electrons to neutralize peroxides through glutathione peroxidases, conjugates electrophiles through glutathione S-transferases, and keeps protein thiols reduced. The ratio of reduced to oxidized glutathione, GSH to GSSG, is one of the most widely used markers of cellular redox state. In the lab, mixtures of GSH and GSSG are a standard redox buffer for refolding proteins with disulfide bonds.
What glutathione research looks at
- Enzyme assays: substrate for glutathione peroxidase, S-transferase and reductase activity measurements.
- Redox biology: GSH/GSSG ratios and thiol status in oxidative-stress models.
- Protein chemistry: GSH/GSSG redox buffers for oxidative folding and disulfide shuffling.
- Cell culture: antioxidant supplementation and depletion studies.
- Metabolic research: alongside NAD+ and mitochondrial peptides such as MOTS-c.
Handling note: reduced glutathione oxidizes in solution, faster at higher pH and in the presence of metal ions. Prepare working solutions close to use and protect stocks from air. Regulatory status: this product is sold strictly as a laboratory reagent, not as a drug, supplement, cosmetic or infusion product.
Why researchers order glutathione from Pure Peptides Canada
Choose 600 or 1500 mg above. Orders over $299 ship free across Canada.
See lab resultsChecking a glutathione identity report
Use these numbers to check the mass-spectrometry result for a glutathione peptide batch. They are calculated for reduced glutathione (GSH), the tripeptide γ-L-glutamyl-L-cysteinyl-glycine (C10H17N3O6S):
- Monoisotopic mass: 307.08 Da (average molecular weight about 307.3 g/mol), giving [M+H]+ at m/z 308.09.
- Oxidation check: oxidized glutathione (GSSG), two GSH joined by a disulfide (C20H32N6O12S2, monoisotopic 612.15 Da), appears at [M+H]+ m/z 613.16 and [M+2H]2+ m/z 307.08. A peak at m/z 307.08 whose isotope peaks sit 0.5 apart is GSSG’s doubly charged ion, not reduced GSH.
- Linkage: the γ-glutamyl bond has the same mass as an ordinary α-linked Glu-Cys-Gly, so an intact-mass result confirms composition, not linkage. HPLC retention against a reference standard addresses that.
If doubly charged ions are new to you, start with our guide to peptide mass spectra. The Janoshik glutathione report is on our Lab Testing page.
Glutathione FAQ
Where can I buy glutathione in Canada?
Pure Peptides Canada stocks reduced glutathione (GSH) as a lyophilized research reagent in 600 mg and 1500 mg vials and ships it from inside Canada by tracked Xpresspost in 3–7 days ($25 CAD), or free in 4–12 days on orders over $299.
Is this reduced or oxidized glutathione?
Reduced glutathione, GSH. The oxidized form is the disulfide GSSG, which forms when two GSH molecules lose electrons, for example on exposure to air in solution.
Why is glutathione’s structure unusual?
Its glutamate is linked through the side-chain (gamma) carboxyl group rather than the normal alpha position. That gamma bond makes glutathione resistant to most peptidases.
Is this glutathione third-party tested?
Yes. An HPLC purity and mass-spectrometry identity report from Janoshik Analytical, an independent lab, is listed on our Lab Testing page. Our COA guide explains how to read it.
Can this glutathione be used in people or animals?
No. This product is for in-vitro laboratory research only. It is not a drug, supplement, cosmetic or infusion product, and we do not provide dosing or administration information.
For laboratory research use only. Not a drug, supplement, food or cosmetic, not for human or veterinary use, and not intended to diagnose, treat, cure or prevent any disease.
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