COA Certified · Every Batch TestedSame-Day Shipping on Orders by 2PM ESTUSA Sourced · USA ShippedFree Shipping on Orders Over $300≥99% Purity — HPLC + Mass SpecEndotoxin Tested · Sterility VerifiedCOA Certified · Every Batch TestedSame-Day Shipping on Orders by 2PM ESTUSA Sourced · USA ShippedFree Shipping on Orders Over $300≥99% Purity — HPLC + Mass SpecEndotoxin Tested · Sterility Verified
For Laboratory & Research Use Only — Not for Human or Veterinary Use
All ProductsGLP-1 & MetabolicResearch PeptidesPeptide BlendsNasal SpraysDissolving StripsBioregulatorsResearch BundlesLab Supplies Search
Research Compound Reference

L-Glutathione

L-Glutathione is the reduced thiol form of the endogenous cellular antioxidant commonly abbreviated GSH, supplied as a lyophilized white powder. It is provided in a sealed vial for laboratory research use only.

Molecular profile of L-Glutathione
Also known asGlutathione (reduced); GSH; γ-L-glutamyl-L-cysteinylglycine
CAS Number70-18-8
Molecular FormulaC10H17N3O6S
Molecular Weight307.32
Amino Acid Count3
SequenceLinear tripeptide gamma-L-glutamyl-L-cysteinyl-glycine featuring an atypical gamma-peptide bond between Glu and Cys; the free cysteinyl thiol is the redox-active moiety (full sequence per COA).
Purity≥99% by HPLC · COA available
Physical FormLyophilized powder

What is L-Glutathione?

On record for this item: CAS 70-18-8, formula C10H17N3O6S, molecular weight 307.32, sequence gamma-Glu-Cys-Gly, three residues joined through an unusual gamma-glutamyl bond at the first position. What can be said is that glutathione is a small, highly water soluble thiol bearing peptide, that the free sulfhydryl group is its reactive centre, and that it exists in two interconverting forms, one with a free thiol and one in which two molecules are joined by a disulfide bond. This item is the reduced form.

Glutathione is one of the most studied small molecules in cell biology. The ratio of reduced to oxidised forms is a standard readout of cellular redox state, and the molecule serves as cofactor for the glutathione peroxidase and glutathione S-transferase families in detoxification chemistry described across eukaryotic model systems. Cell culture work uses it as a reductant and as a measured endpoint.

What is not settled is how well exogenous glutathione crosses cell membranes intact, since transport appears limited in many cell types and breakdown to amino acids followed by intracellular resynthesis is an alternative explanation.

Reconstitution & handling

The reduced form dissolves readily in sterile or bacteriostatic water, added slowly down the vial wall with gentle swirling. The solution is acidic, and buffering it toward neutral accelerates air oxidation of the thiol, so solutions are prepared immediately before use. Concentration is simple arithmetic, so 2 mL added to a 200 mg vial yields 100 mg per millilitre.

Storage & stability

The sealed powder is stored at -20 °C, protected from light and moisture, and warmed to room temperature before opening because it is hygroscopic. The dominant stability concern is oxidation of the free thiol to the disulfide form, which proceeds on contact with air and is catalysed by trace metal ions, so metal spatulas and metal ion buffers are avoided. Solutions are refrigerated at 2 to 8 °C for the shortest practical period and aliquoted for single use.

How it's tested

Lots are analysed by reversed phase HPLC at 214 and 220 nm, with the assay specified to resolve the reduced form from the oxidised disulfide form, since the ratio is what matters for a reductant. Free thiol content is determined by a dedicated thiol assay rather than inferred from chromatographic purity, identity is confirmed by mass spectrometry, and a lot-matched certificate is available.

Frequently asked questions

What are the molecular values for this item?

CAS 70-18-8, formula C10H17N3O6S, molecular weight 307.32, and the sequence gamma-Glu-Cys-Gly. The gamma linkage is what distinguishes it from an ordinary tripeptide and why it resists most peptidases.

What is the difference between the reduced and oxidised forms?

The reduced form carries a free thiol group. The oxidised form is two molecules joined through a disulfide bond. This item is supplied as the reduced form.

Why must solutions be prepared fresh?

The free thiol oxidises to the disulfide on contact with air, and the reaction speeds up at neutral pH and in the presence of trace metals. Fresh preparation keeps the reduced fraction high.

Shop lot-tested L-Glutathione

Third-party tested to ≥99% purity, with analytical documentation available.

View product →Reconstitution calculator
Related compounds
AOD-9604ARA-290BPC-157Dihexa

This reference describes the compound's chemistry and analytical properties for laboratory research use only. It is not medical advice; the product is not a drug, supplement, or cosmetic and is not for human or veterinary consumption.