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For research use only. Not for human or veterinary use.Glutathione. For research use only. Not for human or veterinary use.

Glutathione research peptide

$86.00

For research use only. Not for human or veterinary use.

  • ≥98% by HPLC (lot-specific)
  • Canada fulfilment

Size

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Third-party lab verified

HPLC + MS

Independently tested for identity and purity

Batch
GLU-081226
Tested
August 12, 2026
Purity
99.7%

Tested by Testides

Glutathione

$86.00

Product description

Glutathione research peptide is supplied to qualified Canadian institutions as a characterized laboratory material for in vitro redox, enzymology, and analytical work. The compound is the reduced tripeptide γ-glutamyl-cysteinyl-glycine (GSH), the principal low-molecular-weight thiol in most eukaryotic cells.

In vitro, glutathione participates in thiol–disulfide exchange and is the electron donor for glutathione peroxidases and glutathione S-transferases. The unusual γ-peptide bond between glutamate and cysteine resists cleavage by ordinary aminopeptidases, which is why the tripeptide persists as a discrete reagent in cell-free and cell-culture systems. Laboratories typically use it as a defined reducing equivalent, a calibration standard, or a control ligand when mapping GSH-dependent enzymes and the GSH/GSSG couple.

The material is offered lyophilized in the reduced form. Identity data (CAS 70-18-8, formula C10H17N3O6S, molecular weight 307.3 g/mol, PubChem CID 124886) are listed on the specification table. Solutions air-oxidize to GSSG; prepare fresh under the receiving laboratory's chemical-hygiene plan and store the closed lyophilized vial at −20 °C, protected from light.

Lots are sourced from a GMP-aligned peptide manufacturing partner and released against the stated HPLC purity for that lot (≥98% by HPLC, lot-specific). Identity, chromatographic purity, and related analytical results are documented on the lot certificate of analysis (COA). Retain the COA with the inventory record.

This listing is a research-use-only peptide offered to qualified Canadian institutions for in vitro and laboratory use. Purchasing access is limited to verified Canadian research institutions; individual consumer accounts are not accepted. It is not for human or veterinary use, is not intended for diagnostic procedures, and has not been evaluated or authorized by Health Canada as a drug, diagnostic, or medical product.

Material specifications

Fields a receiving desk can paste into an order record.

SKU
NL-GLUT-1500
Pack
1500 mg lyophilized vial
Purity
≥98% by HPLC (lot-specific)
CAS
70-18-8
Molecular formula
C10H17N3O6S
Molecular weight
307.3 g/mol
Sequence
γ-Glu-Cys-Gly
PubChem CID
124886
For research use only. Not for human or veterinary use.Bacteriostatic Water. For research use only. Not for human or veterinary use.USP GradeCOA

Bacteriostatic Water

For research use only. Not for human or veterinary use.

Laboratory Reagents

$24.00

For research use only. Not for human or veterinary use.NAD+. For research use only. Not for human or veterinary use.99.8%COA

NAD+

For research use only. Not for human or veterinary use.

Laboratory Reagents

$128.00

Common questions

The glutamate residue is joined to cysteine through its side-chain γ-carboxyl rather than the α-carboxyl used in normal peptide bonds. Standard aminopeptidases cannot cleave that geometry, so glutathione resists general proteolysis; γ-glutamyl transpeptidase is the dedicated enzyme that breaks it.
It is the ratio of reduced glutathione to its oxidised disulphide form. Two GSH molecules are oxidised to one GSSG, which glutathione reductase reduces back using NADPH. The ratio, rather than total glutathione, is the informative measure of redox state, and it differs between subcellular compartments.
The literature disagrees. A 1992 human study found no rise in circulating glutathione after a large single oral load, consistent with γ-glutamyl transpeptidase degradation during first pass. A 2015 randomised trial using months of supplementation reported increased body stores. The question remains genuinely contested.
Most human glutathione peroxidase isoforms are selenoproteins, carrying selenocysteine in the catalytic site. Because that residue performs the peroxide-reducing chemistry, selenium availability is a direct input into glutathione peroxidase activity rather than an incidental nutritional detail.
Peroxidases use glutathione as an electron donor to reduce peroxides, generating GSSG that can be recycled. S-transferases conjugate glutathione onto electrophiles as the committed step of phase II metabolism, consuming it irreversibly and requiring new synthesis to replace it.
The free cysteine thiol air-oxidises readily, converting GSH to GSSG in aqueous solution. This is also why glutathione redox measurements are so sensitive to sample handling: oxidation occurring after collection cannot be distinguished from oxidation that occurred in the cell.