{"id":71470,"date":"2026-05-20T11:55:00","date_gmt":"2026-05-20T11:55:00","guid":{"rendered":"https:\/\/medsbase.com\/?post_type=product&p=71470"},"modified":"2026-05-21T07:14:08","modified_gmt":"2026-05-21T07:14:08","slug":"l-glutathione-reduced-gsh","status":"publish","type":"product","link":"https:\/\/medsbase.com\/nl\/l-glutathione-reduced-gsh\/","title":{"rendered":"L-Glutathione (Reduced \/ GSH) Injectable \u2014 Research Grade"},"content":{"rendered":"

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Quick Answer \u2014 What is Glutathione (GSH)?<\/h3>\n

L-Glutathione (reduced; GSH)<\/strong> is the tripeptide \u03b3-glutamyl-cysteinyl-glycine (\u03b3-Glu-Cys-Gly), CAS 70-18-8, molecular formula C10<\/sub>H17<\/sub>N3<\/sub>O6<\/sub>S, MW 307.32 g\/mol. GSH is the most abundant non-protein cellular thiol (millimolar intracellular concentrations) and the canonical reference compound for cellular antioxidant defence research. The unique \u03b3-peptide bond<\/strong> between glutamate’s \u03b3-carboxyl and cysteine’s amino group (rather than the standard \u03b1-peptide bond) makes GSH resistant to common peptidases \u2014 only \u03b3-glutamyltransferase (\u03b3-GT) can cleave it. Cells use GSH as the primary electron donor for glutathione peroxidase-mediated hydrogen-peroxide reduction, as the conjugating co-substrate for glutathione-S-transferase-mediated xenobiotic detoxification, and as the redox-status buffer that controls protein thiol-disulfide equilibrium. Supplied here as lyophilized USP-grade powder for laboratory research use only.<\/p>\n<\/div>\n

Wat u krijgt bij MedsBase:<\/strong> Lyophilized \u226599% HPLC-verified L-Glutathione (reduced form) \u00b7 COA available on request \u00b7 Discreet temperature-stable packaging \u00b7 Worldwide research-supply courier \u00b7 1,400+ verified klantbeoordelingen<\/a><\/div>\n

\ud83d\udce6 Elke bestelling is gedekt door onze Reshipment Assurance Policy<\/strong><\/a> \u2014 als uw pakket niet binnen 20 werkdagen arriveert, sturen wij het opnieuw.<\/p>\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n
Specificatie<\/th>\nDetail<\/th>\n<\/tr>\n<\/thead>\n
Compound Class<\/strong><\/td>\n\u03b3-Glutamyl tripeptide; primary cellular non-protein thiol antioxidant; small-molecule research peptide (\u03b3-linked, peptidase-resistant)<\/td>\n<\/tr>\n
Chemical Name<\/strong><\/td>\nL-Glutathione, reduced (\u03b3-L-Glutamyl-L-cysteinyl-glycine; synonyms: GSH, glutathione free acid, reduced glutathione)<\/td>\n<\/tr>\n
CAS-nummer<\/strong><\/td>\n70-18-8 (reduced GSH form); related: 27025-41-8 (oxidised GSSG dimer form, not supplied here)<\/td>\n<\/tr>\n
Molecuulformule<\/strong><\/td>\nC10<\/sub>H17<\/sub>N3<\/sub>O6<\/sub>S<\/td>\n<\/tr>\n
Moleculair gewicht<\/strong><\/td>\n307.32 g\/mol (free acid)<\/td>\n<\/tr>\n
Sequentie<\/strong><\/td>\n\u03b3-L-Glutamyl-L-cysteinyl-glycine (\u03b3-Glu-Cys-Gly). Note the \u03b3-peptide bond<\/strong> between glutamate’s \u03b3-COOH side chain and cysteine’s \u03b1-amino group, rather than the standard \u03b1-peptide bond. This non-standard linkage is what makes GSH resistant to common \u03b1-peptidases \u2014 only \u03b3-glutamyltransferase (\u03b3-GT) cleaves it, which is the rate-limiting step in extracellular GSH degradation and recycling.<\/td>\n<\/tr>\n
Werkingsmechanisme<\/strong><\/td>\nThree primary cellular roles<\/strong>. (1) Electron donor for glutathione peroxidase<\/em> (GPx family) \u2014 2 GSH + H2<\/sub>O2<\/sub> \u2192 GSSG + 2 H2<\/sub>O, the canonical cellular hydrogen-peroxide-reduction reaction; GSSG is then reduced back to 2 GSH by NADPH-dependent glutathione reductase. (2) Co-substrate for glutathione-S-transferase<\/em> (GST family) \u2014 conjugates GSH to electrophilic xenobiotic and endogenous substrates, generating excretable mercapturic acid conjugates (the central liver-detoxification pathway). (3) Redox-status buffer<\/em> \u2014 GSH:GSSG ratio (typically ~100:1 in healthy cells) controls protein thiol-disulfide equilibrium via thioredoxin- and glutaredoxin-mediated exchange, regulating thousands of redox-sensitive protein activities.<\/td>\n<\/tr>\n
Form<\/strong><\/td>\nLyophilized white-to-off-white crystalline powder; single-use research vials. Highly hygroscopic<\/strong> \u2014 reseal vials promptly after each withdrawal to avoid moisture uptake.<\/td>\n<\/tr>\n
Zuiverheid<\/strong><\/td>\n\u226599% (HPLC verified, COA on request); titration confirms \u226598% reduced GSH form (\u22642% oxidised GSSG content). USP-grade reference.<\/td>\n<\/tr>\n
Oplosbaarheid<\/strong><\/td>\nWater 20 mg\/mL; PBS (pH 7.2) 10 mg\/mL \u2014 readily soluble at the supplied vial concentrations. The thiol (-SH) group makes GSH air-oxidation-sensitive \u2014 prepare working solutions fresh from the lyophilized vial and use within 24 hours where possible. DMSO is a suitable co-solvent for cell-culture stock preparation (up to 100 mg\/mL) and provides additional protection against air-oxidation.<\/td>\n<\/tr>\n
Opslag<\/strong><\/td>\nLyophilized: 2\u20138 \u00b0C in original sealed packaging for short-term working stock; \u221220 \u00b0C for long-term storage of unopened vials (stable \u226536 months at \u221220 \u00b0C; \u226518 months at 2\u20138 \u00b0C). Reconstituted aqueous solutions: 2\u20138 \u00b0C, use within ~7 days (air-oxidation to GSSG is the limiting factor). Protect from light. Avoid repeated freeze-thaw of reconstituted solutions<\/strong> \u2014 cumulative cycles accelerate GSH \u2192 GSSG oxidation.<\/td>\n<\/tr>\n
Onderzoeksgebruik<\/strong><\/td>\nFor laboratory research use only. Not for human or veterinary diagnostic or therapeutic use. Glutathione is not on the WADA Prohibited List. It is approved as a clinical injectable in some jurisdictions (Italy \/ Japan \/ Korea \/ Philippines as Tationil and similar brand names) for hepatology and oxidative-stress conditions; the research-grade material supplied here is intended for laboratory use only and is distinct from those clinical preparations.<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n

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What Is L-Glutathione (Reduced \/ GSH)?<\/h2>\n

L-Glutathione (reduced form, GSH)<\/strong> is the most abundant non-protein cellular thiol in eukaryotic biology \u2014 present at millimolar intracellular concentrations (1\u201310 mM in most cell types; up to 10 mM in hepatocytes) and serving as the master molecular buffer for cellular redox status. Structurally it is a tripeptide of glutamate, cysteine, and glycine (\u03b3-Glu-Cys-Gly), CAS 70-18-8, molecular formula C10<\/sub>H17<\/sub>N3<\/sub>O6<\/sub>S, molecular weight 307.32 g\/mol.<\/p>\n

The defining structural feature of glutathione is its \u03b3-peptide bond<\/strong>. Standard peptides are linked through \u03b1-peptide bonds between the \u03b1-carboxyl of one amino acid and the \u03b1-amino of the next. In glutathione, the bond between glutamate and cysteine is unconventional: it is formed between the \u03b3-carboxyl<\/em> of glutamate’s side chain and the \u03b1-amino of cysteine. This non-standard linkage is the molecular basis for glutathione’s resistance to common cellular peptidases \u2014 only \u03b3-glutamyltransferase (\u03b3-GT, GGT, EC 2.3.2.2) recognises and cleaves the \u03b3-bond. As a result, glutathione is uniquely stable in the cellular cytosol where it would otherwise be rapidly degraded by \u03b1-peptidase activity, and \u03b3-GT-mediated extracellular degradation is the rate-limiting step of glutathione recycling.<\/p>\n

Glutathione is synthesised in two ATP-dependent steps by the cytosolic enzymes glutamate-cysteine ligase (GCL)<\/strong> \u2014 which forms the \u03b3-glutamyl-cysteine bond \u2014 and glutathione synthetase (GSS)<\/strong> \u2014 which adds the C-terminal glycine. GCL is the rate-limiting enzyme and is feedback-inhibited by glutathione itself, providing autoregulation of cellular glutathione levels. Cysteine availability is the other major rate-limiting input \u2014 which is why N-acetylcysteine (NAC), a cysteine prodrug, is the canonical clinical intervention for boosting cellular glutathione synthesis in oxidative-stress and detoxification contexts (the basis of NAC’s approval for paracetamol overdose and other clinical indications).<\/p>\n

Glutathione exists in cells in two interconverting forms: the reduced form (GSH)<\/strong> with a free thiol (-SH) group, and the oxidised form (GSSG)<\/strong> where two GSH molecules are linked by a disulfide bridge. The GSH:GSSG ratio (typically ~100:1 in healthy cells, dropping to 10:1 or lower under oxidative stress) is the canonical cellular redox biomarker. GSSG is reduced back to 2 GSH by glutathione reductase (GR, GSR)<\/strong>, an NADPH-dependent flavoenzyme \u2014 connecting the GSH redox system to NADPH availability and ultimately to the pentose phosphate pathway. This is why pentose-phosphate-pathway disruption (G6PD deficiency, glucose-6-phosphate availability) impairs GSH-system function and triggers oxidative cell damage.<\/p>\n

The research-grade material supplied here is the reduced GSH form, supplied as lyophilized powder for reconstitution and research-protocol use alongside the peptide catalogue.<\/p>\n

Mechanism of Action \u2014 Three Primary Cellular Roles<\/h2>\n

GSH’s biological mechanism is the sum of three primary cellular roles that are all well-characterised in published biochemistry:<\/p>\n