GLUTATHIONE

Glutathione

Glutathione (GSH) is the tripeptide γ-L-glutamyl-L-cysteinylglycine, the most abundant low-molecular-weight thiol in animal cells. Its glutamate is joined to cysteine through the side-chain (γ) carboxyl group instead of a standard peptide bond, which shields it from most peptidases. The cysteine thiol does the chemical work, which makes glutathione central to cellular redox research.

Product Specifications

• Product: Glutathione
• Amount: See available options above
• Form: Lyophilized powder
• Purity: Third-party tested by an ISO 17025 U.S. laboratory. See the batch Certificate of Analysis (COA) on this page.
• Storage: Keep sealed and refrigerated at 2–8°C (36–46°F), protected from light.
• Ships from: United States, 2-day UPS

Chemical Profile

• Compound class: Tripeptide (γ-Glu-Cys-Gly)
• Sequence: γ-Glu-Cys-Gly (γ-glutamyl linkage), reduced form
• Molecular formula: C₁₀H₁₇N₃O₆S
• Molecular weight: 307.33 g/mol
• CAS number: 70-18-8

What researchers study

Glutathione is a standard reagent in biochemistry and cell biology. Research areas include:

• Biosynthesis: the two ATP-dependent steps catalyzed by glutamate-cysteine ligase (the rate-limiting enzyme) and glutathione synthetase, and how cysteine supply controls the pool.
• Redox balance: the ratio of reduced GSH to oxidized glutathione disulfide (GSSG) as a readout of oxidative stress, with glutathione reductase regenerating GSH using NADPH.
• Peroxide detoxification: glutathione peroxidases, which use GSH to reduce hydrogen peroxide and lipid hydroperoxides.
• Conjugation: glutathione S-transferases that attach GSH to electrophilic compounds, a key step in xenobiotic metabolism studied in liver models.
• Protein regulation: S-glutathionylation of cysteine residues as a reversible switch on enzyme activity.
• Culture systems: GSH as a supplement in cell, oocyte and embryo culture media, and as a substrate in enzyme assays.

Regulatory status

Glutathione occurs naturally in the body and in foods. The lyophilized material sold here is a research reagent, not an FDA-approved drug product, dietary supplement or cosmetic, and it is not for human use.

Quality & Documentation

Every batch of Glutathione is made in small runs for Rogue Compounds and tested by an independent U.S. laboratory for identity (mass spectrometry) and purity (HPLC). Each vial is labeled with its batch number and a QR code that opens the testing lab’s own report for that batch. The same batch Certificate of Analysis is posted on this page and in our COA Library, so you can check one against the other.

Research overview

For a longer look at Glutathione, covering where it came from, what cell and animal studies have measured, and what the evidence does not show, read our Glutathione research overview. It is written as background reading, and every study it cites is linked to PubMed.

Selected literature

• Lu SC. Glutathione synthesis. Biochim Biophys Acta. 2013;1830(5):3143-3153. PMID 22995213
• Sies H. Glutathione and its role in cellular functions. Free Radic Biol Med. 1999;27(9-10):916-921. PMID 10569624
• Hayes JD, Flanagan JU, Jowsey IR. Glutathione transferases. Annu Rev Pharmacol Toxicol. 2005;45:51-88. PMID 15822171
• Wu G, et al. Glutathione metabolism and its implications for health. J Nutr. 2004;134(3):489-492. PMID 14988435

Research Use Only

This product is sold strictly as a research chemical for in-vitro laboratory and analytical use by qualified professionals. It is not a drug, dietary supplement, food, or cosmetic, and it is not intended to diagnose, treat, cure, or prevent any disease. Not for human or veterinary use. Rogue Compounds does not provide dosing, preparation, or usage instructions. The literature on this page is listed for scientific background only and does not describe this product or any use of it.