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Glutathione (Reduced, GSH)

≥99% Purity
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COA Included

Categories: Anti-aging Peptides, Immune Peptides

Glutathione (GSH) is the most abundant intracellular antioxidant in mammalian cells. A tripeptide master regulator of cellular redox homeostasis, detoxification, and immune cell function in biological research.


Glutathione (L-Glutathione, reduced form, abbreviated GSH) is a ubiquitous tripeptide composed of glutamate, cysteine, and glycine, joined by a unique gamma-peptide bond between the glutamate gamma-carboxyl group and the cysteine alpha-amino group. This gamma-linkage protects the molecule from normal peptidase degradation, contributing to its extraordinary intracellular stability. GSH is synthesized in the cytoplasm of virtually all mammalian cells in a two-step enzymatic process catalyzed by glutamate-cysteine ligase (GCL, the rate-limiting step) and glutathione synthetase (GS), reaching intracellular concentrations of 1-10 mM — making it the single most abundant non-protein thiol compound in biology.

GSH functions as the central hub of the cellular antioxidant defense network through multiple mechanisms. It directly scavenges reactive oxygen species (ROS) and reactive nitrogen species (RNS) through its cysteine thiol group, becoming oxidized to glutathione disulfide (GSSG) in the process. Glutathione reductase then regenerates GSH from GSSG using NADPH, maintaining the high GSH/GSSG ratio (typically >100:1) that defines a healthy cellular redox environment. Beyond direct scavenging, GSH serves as the essential cofactor for glutathione peroxidases (GPx family, selenium-dependent ROS detoxification), glutathione S-transferases (GSTs, phase II xenobiotic detoxification), and glutaredoxins (thiol-disulfide exchange reactions critical for protein function). The GSH/GSSG ratio is the most widely used biomarker of cellular oxidative stress in research settings.

Research applications for glutathione span oxidative stress biology, toxicology (xenobiotic conjugation studies), immunology (lymphocyte proliferation and NK cell function require adequate GSH), mitochondrial biology (mitochondrial GSH pool maintenance is critical for electron transport chain function), neuroscience (neuronal vulnerability to oxidative damage), and aging research (progressive GSH depletion is a hallmark of biological aging across tissues). Published data demonstrate that intracellular GSH levels decline with age in virtually all tissues studied, and this decline correlates with increased oxidative damage markers and mitochondrial dysfunction.

Supplied as a lyophilized powder (reduced form, active thiol) with ≥99% purity. This product is oxygen and moisture sensitive — store at -20°C desiccated under inert atmosphere. Reconstitute immediately before use with deoxygenated sterile water. For cellular biology and oxidative stress research only.

⚠ Supplied strictly for research and experimental purposes only.