L-Glutathione

L-Glutathione (GSH, γ-glutamylcysteinylglycine) is the most abundant non-protein thiol antioxidant in mammalian cells, present at millimolar concentrations in virtually all cell types. It is a tripeptide synthesized from L-glutamate, L-cysteine, and glycine through sequential enzymatic reactions catalyzed by γ-glutamylcysteine synthetase (GCS, rate-limiting step) and glutathione synthetase.

GSH functions as both a direct antioxidant (donating electrons to neutralize reactive oxygen and nitrogen species) and as the required substrate for glutathione peroxidase (GPx) enzymes in the detoxification of hydrogen peroxide and lipid hydroperoxides. It also participates in phase II xenobiotic detoxification through glutathione S-transferase (GST) conjugation reactions in the liver. In research applications, GSH is studied in cellular redox biology, skin pigmentation (inhibition of DOPA to melanin conversion), immune cell function, and mitochondrial health.

• Cellular redox homeostasis and glutathione cycle research
• Glutathione peroxidase (GPx) and ROS neutralization studies
• Hepatic phase II xenobiotic detoxification (GST conjugation) research
• Melanin synthesis inhibition and skin pigmentation research
• Immune cell (lymphocyte, NK cell) function and redox regulation
• Mitochondrial antioxidant defense and electron transport chain protection

Dose levels referenced by the MVLabs peptide calculator, shown for research reference only:

Master antioxidant studied for detox/immune pathways; often given as a slow injection.

Research reference only — not dosing guidance for human use. Use the calculator for other vials or volumes.

Supplied as a lyophilized powder. Store at 2–8 °C on receipt; protect from heat, light and moisture, and avoid excessive agitation. If reconstitution is required for laboratory work, use sterile technique — bacteriostatic water, or 0.6% acetic acid for low-solubility peptides. Protocols vary by research application.