Antioxidant & redox research
Glutathione
Glutathione (GSH) is a naturally occurring tripeptide of glutamate, cysteine and glycine, and the most abundant low-molecular-weight thiol in mammalian cells. Its defining chemical feature is an unusual gamma peptide bond at the glutamate residue. VaultLabs supplies reduced glutathione as a lyophilised reference material for in vitro laboratory research only.
Research use only. For in vitro research use only. Not for human or animal consumption. Not for human consumption, medical use, or personal application.
Reviewed by VaultLabs Research Editorial Desk · Last updated 2026-08-03
Key facts
- Sequence is γ-L-glutamyl-L-cysteinylglycine; the glutamate is linked through its side-chain carboxyl, not the alpha carboxyl.
- CAS registry number 70-18-8; molecular formula C10H17N3O6S; molecular weight 307.32 g/mol.
- That gamma linkage is what makes glutathione resistant to standard peptidases and gives it an unusually long intracellular lifetime.
- The free thiol on the cysteine residue oxidises readily to the disulfide dimer GSSG — the single most important handling consideration.
- The cellular GSH:GSSG ratio is a standard laboratory measure of oxidative state.
- Chemical name
- L-Glutathione (reduced form)
- Common synonyms
- GSH, γ-L-glutamyl-L-cysteinylglycine
- Sequence
- γ-Glu-Cys-Gly
- CAS number
- 70-18-8
- Molecular formula
- C10H17N3O6S
- Molecular weight
- 307.32 g/mol
- Appearance
- White to off-white lyophilised powder
- Catalog strength
- 1500 mg vial
What glutathione is
Glutathione is a tripeptide, but not a conventional one. In an ordinary peptide, residues are joined through alpha carboxyl groups. In glutathione, the glutamate connects to cysteine through its side-chain carboxyl — a gamma linkage. That single structural quirk has a large functional consequence: standard peptidases do not recognise the bond, so glutathione persists intracellularly far longer than a conventional tripeptide would.
The second defining feature is the free thiol on the cysteine residue. This is the chemically reactive centre that lets glutathione act as the cell's principal redox buffer, and it is also the reason the reduced form is difficult to keep reduced. Two GSH molecules oxidise to the disulfide dimer GSSG, and that conversion happens readily in air and in solution.
The catalog presentation is 1500 mg, a bulk fill more typical of a reagent than of a peptide reference standard, reflecting how the material is generally used in assay preparation.
Where the research literature sits
Glutathione has one of the largest literatures of any molecule in this catalog. The core areas are redox homeostasis, detoxification chemistry through glutathione S-transferase conjugation, and the use of the GSH:GSSG ratio as a quantitative index of cellular oxidative state.
It is also a workhorse laboratory reagent rather than only a research subject: glutathione-based affinity purification, antioxidant assay standards and enzyme substrate preparation all consume characterised material. For most purchasers this reagent role, not a biological hypothesis, is the reason for the order.
Consumer marketing around glutathione — particularly for skin lightening and intravenous infusion — is extensive and largely unsupported by the kind of evidence regulators require. VaultLabs supplies laboratory material and makes no claims of that sort.
Analytical characterisation and handling
Release is by HPLC against a stated purity specification with a lot-linked certificate. The most meaningful related substance for reduced glutathione is the oxidised dimer GSSG, and its level is a direct indicator of how well the material has been manufactured, packaged and shipped.
Handling follows from that chemistry. Keep vials sealed and protected from air and moisture, equilibrate to room temperature before opening so the powder does not take up water, and minimise the time the material spends exposed. Weighing single-use aliquots on first opening is usually better practice than repeatedly opening a 1500 mg vial.
In solution, oxidation accelerates at neutral to alkaline pH and in the presence of trace metal ions. Prepare working solutions fresh, consider chelating trace metals where the assay permits, and do not assume that a stored stock still reflects the certified reduced-form content.
Regulatory position and supply
Glutathione supplied by VaultLabs is a laboratory reagent and reference material. It is not a supplement, not an injectable preparation, and not intended for human or veterinary use. Orders are accepted on a research-use basis only.
The catalog presentation is a 1500 mg lyophilised vial with lot-linked certificate retrieval through batch verification.
Research interest areas
Redox balance assays
Glutathione peroxidase coupled reactions
Oxidative stress models
Cell viability under ROS challenge
Storage information
2–8 °C (lyophilized, sealed)
2–8 °C sealed; protect from oxidation and moisture.
Stability notes
Reduced glutathione oxidizes to GSSG — store lyophilized sealed, reconstitute fresh when possible, or use stabilized formulations per SOP.
Selected literature
Named papers behind the statements on this page. Each entry resolves on PubMed and through its DOI, so you can read the source rather than take our summary of it. Inclusion describes the research record and is not a claim about this material’s suitability for any use.
Glutathione: overview of its protective roles, measurement, and biosynthesis
Forman HJ, et al. · Molecular Aspects of Medicine · 2009
Standard reference for GSH biosynthesis and, importantly here, the pitfalls in measuring it.
Glutathione peroxidases
Brigelius-Flohé R, et al. · Biochimica et Biophysica Acta · 2013
Enzymology of the GSH/GSSG couple that underlies most redox assay designs.
Databases and verification
Registry and database entries for independent identity checks. These are standing searches rather than fixed records, so they stay current as new work is indexed.