Longevity Research

Glutathione - 1500MG

CAS # 70-18-8

A 3-amino acid tripeptide (γ-Glu-Cys-Gly) that serves as the body's primary endogenous antioxidant, neutralizing reactive oxygen species and supporting cellular detoxification pathways in research models. Premium Research Peptide.

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Purity≥99% HPLC
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CAS70-18-8
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About Glutathione - 1500MG

Glutathione (reduced form, GSH) is a gamma-linked tripeptide of glutamate, cysteine, and glycine and the most abundant low-molecular-weight thiol antioxidant in mammalian cells. With the molecular formula C10H17N3O6S and a molecular weight of 307.32 g/mol (CAS 70-18-8), it is present at millimolar concentrations in healthy tissue and participates in an unusually broad range of biochemical processes. The unusual gamma-glutamyl bond between glutamate and cysteine distinguishes it structurally from standard peptides.

Research on glutathione spans redox homeostasis, reactive-oxygen-species neutralization, xenobiotic and drug detoxification via conjugation, protein disulfide regulation, and immune-cell function. It serves as the central substrate of the glutathione peroxidase and glutathione S-transferase enzyme families and cycles between reduced (GSH) and oxidized (GSSG) states to maintain cellular redox balance. This reduced L-glutathione is supplied for laboratory research use only.

Research use only — not for human or animal consumption. Per-batch documentation is provided with the material.

Handling and Storage Tips:

Keep peptides cold and away from light once received.

For short-term use (days to weeks), refrigeration at 4°C (39°F) is acceptable.

Lyophilized peptides are typically stable at room temperature for several weeks, making it suitable for moderate-term storage.

For long-term storage (months to years), it’s best to freeze peptides at -80°C (-112°F). Freezing optimally preserves peptide stability for extended periods.

FDA Disclosure & Intended Use:

FDA Disclosure: The statements on this website and the products sold herein have not been evaluated by the U.S. Food and Drug Administration (FDA). These products are not intended to diagnose, treat, cure, or prevent any disease. Products sold are for Research Use Only and are not for human or animal use.

Intended Purpose: Products sold on this site are intended solely for basic laboratory research, pharmaceutical research, or the development of new tests. They are not intended for diagnostic, therapeutic, or clinical use.

Specifications

Identification
  • MaterialGlutathione - 1500MG
  • Also searched asGSH, L-Glutathione
  • Research AreaLongevity Research
  • Presentation
  • CAS Number70-18-8
  • Molecular FormulaC10H17N3O6S
  • Molecular Weight307.32 g/mol
  • TypeEndogenous tripeptide (thiol antioxidant)
  • Receptor / TargetNon-receptor; cofactor/substrate for glutathione peroxidases, glutathione S-transferases, and glutaredoxin redox systems
  • PubChem CID124886 →
Amino Acid Sequence

gamma-L-Glutamyl-L-cysteinylglycine (gamma-Glu-Cys-Gly)

Analytical Data
  • Purity (HPLC)≥99%
  • Identity (MS)Confirmed to specification
  • TestingAccredited (ISO 17025) third-party laboratory
  • DocumentationPer-batch COA →
Key Characteristics
Molecular FormulaC10H17N3O6S
Molecular Weight307.32 g/mol
CAS Number70-18-8
PubChem CID124886
Sequencegamma-L-Glutamyl-L-cysteinylglycine (gamma-Glu-Cys-Gly)
Receptor / TargetSubstrate/cofactor for glutathione peroxidases, S-transferases, and glutaredoxin systems (non-receptor)
FormLyophilized powder, reduced L-glutathione (1500mg vial)
SolubilityFreely soluble in water (~65 g/100 mL at 25°C); insoluble in most organic solvents
StorageStore cold and protected from light; -20°C for long-term storage; minimize air exposure to limit oxidation
StabilityReduced form is oxidation-sensitive in solution; prepare fresh and keep cold to preserve the reduced (GSH) state
Research Context
Redox homeostasisCentral reagent in studying cellular oxidation-reduction balance via the GSH/GSSG couple.
Oxidative stress & ROSUsed to study neutralization of reactive oxygen species and lipid/protein oxidative damage.
Detoxification biochemistryStudied as the conjugating substrate of glutathione S-transferases in xenobiotic and drug metabolism.
Neurodegeneration modelsExamined in models of oxidative-stress-associated neuronal injury and aging.
Immune cell functionInvestigated for roles in lymphocyte redox regulation and immune signaling.
Protein thiol regulationExplored in protein S-glutathionylation and disulfide-bond redox signaling research.
Research Findings

Glutathione is among the most extensively studied endogenous small molecules in biochemistry. Research literature documents its function as the principal intracellular thiol buffer, its role as substrate for glutathione peroxidase in hydrogen-peroxide detoxification, its conjugation reactions with electrophiles via glutathione S-transferases, and its participation in protein S-glutathionylation as a post-translational redox modification.

The reduced form (GSH) is readily oxidized to the disulfide GSSG, and maintaining a high GSH/GSSG ratio is a widely used experimental index of cellular redox status. Material is provided as a research reagent only.

History

Glutathione was first isolated in 1888 and structurally characterized in the 1920s and 1930s, with Frederick Gowland Hopkins among the early investigators who identified it as a widespread cellular constituent. Its gamma-glutamyl tripeptide structure and central role in cellular redox biology have since made it one of the most-studied endogenous antioxidants in biochemistry.

References
  1. Meister A, Anderson ME. Glutathione. Annu Rev Biochem. 1983;52:711-760.
  2. Lu SC. Glutathione synthesis. Biochim Biophys Acta. 2013;1830(5):3143-3153.
  3. Forman HJ, Zhang H, Rinna A. Glutathione: overview of its protective roles, measurement, and biosynthesis. Mol Aspects Med. 2009;30(1-2):1-12.
  4. PubChem Compound Summary for CID 124886, Glutathione. National Center for Biotechnology Information.

View compound profile on NIH PubChem →

Cited literature refers to laboratory and preclinical research. This material is supplied strictly for research use only and is not intended to diagnose, treat, cure, or prevent any disease.

Why researchers choose Helio Peptides
99%+ PurityHPLC-verified every batch
Accredited TestingIndependent ISO 17025 laboratory
Per-Batch COADocumentation tied to your lot
Made in the USADiscreet, protected shipping
Frequently Asked
Are these research materials third-party tested?

Yes — every batch is analysed by an accredited (ISO 17025) independent laboratory using HPLC and mass spectrometry, with a per-batch Certificate of Analysis.

What purity are the materials?

Materials are verified to 99%+ HPLC purity. Any batch that does not meet the threshold is not released.

Do you provide a Certificate of Analysis (COA)?

Yes. Per-batch COA documentation is provided and is traceable by lot number.

Where do you ship from?

Materials are shipped from the USA in discreet, protective packaging.

Are these products for human use?

No. All materials are sold strictly for laboratory research use only — not for human or animal consumption, diagnosis, treatment, or prevention of any disease.

RESEARCH USE ONLY · NOT FOR HUMAN OR VETERINARY USE · 21+