L-Glutathione 1500mg

L-Glutathione (gamma-L-glutamyl-L-cysteinyl-glycine), commonly abbreviated GSH, is a tripeptide distinguished by an unusual gamma peptide bond formed between the side-chain carboxyl of glutamate and the amine of cysteine, with glycine attached to cysteine by a conventional peptide bond. It is present in virtually all mammalian cells and is the most abundant low-molecular-weight thiol in the body. Because of its central role in maintaining cellular redox balance, glutathione is one of the most widely used reference compounds in oxidative-stress and detoxification research.

In the research-supply context, reduced glutathione is a standard tool for studying antioxidant defence, thiol chemistry, and phase-II detoxification. It is supplied here as a research-grade reagent for laboratory benchwork and is not a therapeutic product.

Glutathione's activity centres on the reactive thiol (–SH) group of its cysteine residue. This thiol donates electrons to neutralise reactive oxygen species such as free radicals and peroxides, and in doing so glutathione is oxidised to glutathione disulfide (GSSG), in which two glutathione molecules are joined by a disulfide bond. The cellular ratio of reduced (GSH) to oxidised (GSSG) glutathione is a widely used index of oxidative stress.

Beyond direct radical scavenging, glutathione serves as a cofactor for glutathione peroxidase and glutathione S-transferase enzymes, participates in the regeneration of other antioxidants such as vitamins C and E, and conjugates xenobiotics and electrophiles during phase-II detoxification. It also reduces disulfide bonds in cytoplasmic proteins, supporting protein-folding and redox-signalling research.

Documented areas of glutathione research include: antioxidant defence and reactive-oxygen-species neutralisation; the GSH/GSSG redox ratio as a stress marker; phase-II detoxification and xenobiotic conjugation; enzymatic cofactor roles; and regeneration of other cellular antioxidants. These describe the published research landscape and are provided for scientific context only. They are not claims of efficacy. Ronin Peptides supplies L-Glutathione exclusively as a research-grade reagent and provides no dosing protocols or therapeutic recommendations.

Reduced glutathione is sensitive to oxidation. Store unopened lyophilized vials dry, cold, and protected from air and light; long-term storage should be at or below −20 °C. Because the reduced thiol oxidises readily once in solution, reconstitute close to the time of use, keep solutions cold at 2–8 °C, minimise air exposure, and avoid repeated freeze–thaw cycles.

Glutathione is the reference intracellular antioxidant and is often studied alongside other redox-active compounds. Unlike enzymatic antioxidants, it is a small tripeptide that acts stoichiometrically through its cysteine thiol. It is frequently studied in combination with, or as a benchmark against, precursors such as N-acetylcysteine and cofactors that support its regeneration. Within a research catalogue it is distinct from the signalling peptides, being a metabolic-antioxidant reagent rather than a receptor-targeted compound.

A 1500 mg vial of L-Glutathione reconstituted with 10 mL of bacteriostatic water yields a final concentration of 150 mg/mL. Other diluent volumes scale linearly: 15 mL gives 100 mg/mL, 5 mL gives 300 mg/mL. Because the reduced thiol oxidises on exposure to air, prepare working solutions immediately before use.

1. Bring both vials to room temperature before opening.
2. Sanitise both rubber stoppers with an alcohol swab.
3. Pull the chosen diluent volume into a sterile transfer syringe.
4. Direct the water against the inner wall of the vial as it is injected.
5. Invert slowly until dissolved; do not vortex or shake vigorously.
6. Refrigerate at 2–8 °C and minimise air exposure.

1. Meister A, Anderson ME. Glutathione. Annual review of biochemistry. 1983. PMID 6137189.
2. Lu SC. Glutathione synthesis. Biochimica et biophysica acta. 2013. PMID 22995213.
3. Forman HJ, Zhang H, Rinna A. Glutathione: overview of its protective roles, measurement, and biosynthesis. Molecular aspects of medicine. 2009. PMID 18796312.