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Glutathione: Research Overview

What is glutathione? Glutathione is an endogenous tripeptide of glutamate, cysteine, and glycine, joined through an unusual γ-glutamyl linkage. It is the cell's principal low-molecular-weight thiol antioxidant, studied in redox biology, oxidative-stress models, and detoxification enzymology. It is sold strictly for laboratory research use.
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Technical profile

CompoundGlutathione (GSH; reduced glutathione)
ClassEndogenous tripeptide (γ-L-glutamyl-L-cysteinyl-glycine)
StructureGlu-Cys-Gly, with the glutamate joined to cysteine through a γ-glutamyl (side-chain) linkage rather than a standard α-peptide bond; the cysteine thiol is the reactive group
Molecular formulaC10H17N3O6S
Molecular weight307.33 g/mol
CAS number70-18-8
PubChem CID124886
Form suppliedLyophilized powder, sealed vial
StorageLyophilized: 2–8 °C, protected from light. — the thiol oxidizes in solution
VerificationHPLC purity ≥99%, identity confirmation — documented on the batch COA

What does the research literature cover?

Glutathione is one of the most extensively characterized molecules in cell biology, with a literature spanning decades. Published research covers:

Important context: although glutathione is an endogenous molecule found in virtually all cells, the material described here is supplied for laboratory research — assay work, redox experiments, and enzymology — only. Summaries here describe what researchers have studied; they are not claims about effects in humans.

Why purity matters for glutathione research

Redox research results are only as reliable as the material in the vial. Oxidized (GSSG) content, truncated sequences, or other impurities shift measured GSH/GSSG ratios and confound assay baselines. Every VP Peptides glutathione batch ships with a Certificate of Analysis documenting ≥99% HPLC purity and identity confirmation from independent third-party testing.

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Frequently asked questions

Is glutathione a peptide?

Yes — glutathione is a tripeptide, one of the shortest peptides with major biological roles. Its three residues (glutamate, cysteine, glycine) are joined with a distinctive γ-glutamyl linkage, which makes it resistant to most standard peptidases.

What is the GSH/GSSG ratio?

GSH is the reduced (thiol) form of glutathione and GSSG is the oxidized (disulfide) form. The ratio of the two is a standard experimental readout of cellular redox state: laboratories measure it in cell and tissue samples as a marker of oxidative stress.

Is this glutathione approved for human use?

The glutathione supplied by VP Peptides is a research chemical for in-vitro and laboratory investigation only. It is not manufactured, labeled, or tested for use as a drug, supplement, food ingredient, or cosmetic, and no claims are made about effects in humans.

How should glutathione be stored in the lab?

Lyophilized vials should be kept at 2–8 °C and protected from light. Handle per your laboratory protocol, since the free thiol gradually oxidizes to GSSG in solution.

Redox buffering and the bioavailability question

In cell biology, glutathione is often described as the cell's principal redox buffer. Present at millimolar concentrations, its cysteine thiol cycles between the reduced (GSH) and oxidized (GSSG) forms, and the balance between the two is used experimentally as an index of intracellular redox tone. Review literature situates glutathione at the center of thiol-based antioxidant defense, of detoxification through the glutathione S-transferases, and of the regeneration of other antioxidant systems (Wu et al., 2004). This is why redox studies so often report the GSH/GSSG ratio rather than any single absolute value.

A recurring theme in the literature — and an important caution for interpreting supplementation studies — is that glutathione taken orally is extensively broken down in the gastrointestinal tract, so delivering the intact tripeptide into cells is not straightforward. Human trials of oral glutathione have reported mixed results: one placebo-controlled study of daily oral glutathione found no significant change across a panel of systemic oxidative-stress biomarkers (Allen and Bradley, 2011), while a later randomized trial reported that longer-term oral dosing raised measured body stores of glutathione (Richie et al., 2015). Read together, the two illustrate why this clinical evidence base is characterized as inconsistent rather than settled, and why formulation and study design weigh heavily on outcomes.

These summaries describe published research only. The glutathione supplied here is a laboratory reagent for redox and enzymology experiments; nothing above is a health claim, and no statement about effect, safety, or efficacy in humans is intended.

Selected research references

Related research compounds

Research use only. All products described on this page are furnished for laboratory research purposes only and are not for human or veterinary use, not for use in food or cosmetics, and not for any diagnostic or therapeutic application. Nothing on this page is medical advice or a claim of safety or efficacy in humans. Research summaries reference publicly available preclinical literature; specific citations are listed in the references above.