L-Glutathione (zredukowany/GSH) do iniekcji — klasa badawcza

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What Is L-Glutathione (Reduced / GSH)?

L-Glutathione (reduced form, GSH) is the most abundant non-protein cellular thiol in eukaryotic biology — present at millimolar intracellular concentrations (1–10 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 (γ-Glu-Cys-Gly), CAS 70-18-8, molecular formula C₁₀H₁₇N₃O₆S, molecular weight 307.32 g/mol.

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

Glutathione is synthesised in two ATP-dependent steps by the cytosolic enzymes glutamate-cysteine ligase (GCL) — which forms the γ-glutamyl-cysteine bond — and glutathione synthetase (GSS) — 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 — 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).

Glutathione exists in cells in two interconverting forms: the reduced form (GSH) with a free thiol (-SH) group, and the oxidised form (GSSG) 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), an NADPH-dependent flavoenzyme — 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.

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.

Mechanism of Action — Three Primary Cellular Roles

GSH’s biological mechanism is the sum of three primary cellular roles that are all well-characterised in published biochemistry:

• Glutathione peroxidase (GPx) substrate — hydrogen peroxide and lipid peroxide reduction — The most-cited role of GSH. The GPx family (GPx1–8, with the selenium-dependent GPx1 the most abundant) catalyses the reaction 2 GSH + ROOH → GSSG + ROH + H₂O, reducing hydrogen peroxide and lipid hydroperoxides to water and alcohols respectively. This is the cell’s primary defence against reactive oxygen species generated by mitochondrial respiration, NADPH-oxidase activity, and other oxidative processes. GPx4 is the specific isoform that catalyses lipid-hydroperoxide reduction and is the molecular target whose loss-of-function triggers ferroptosis — the iron-dependent regulated cell death pathway that has become a major focus of recent cancer-research and neurodegenerative-disease research.
• Glutathione-S-transferase (GST) co-substrate — xenobiotic and endobiotic conjugation — The GST family (cytosolic, microsomal, and mitochondrial members; ~20 human GST isoforms) catalyses the conjugation of GSH to electrophilic substrates via the GSH thiol group, generating GSH-S-conjugate adducts that are subsequently processed by γ-GT and dipeptidases to mercapturic acids and excreted. This is the central Phase II detoxification pathway in liver and other tissues, processing a vast range of xenobiotics (drug metabolites, environmental chemicals, products of Phase I cytochrome-P450 metabolism), endogenous electrophiles (4-hydroxynonenal, acrolein from lipid peroxidation), and reactive intermediates (NAPQI from paracetamol, the basis of NAC therapy in paracetamol overdose).
• Redox-status buffer — protein thiol-disulfide equilibrium regulation — The cellular GSH:GSSG ratio sets the thermodynamic equilibrium for protein-thiol redox state via thioredoxin- and glutaredoxin-mediated exchange. Thousands of cellular proteins have redox-sensitive cysteine residues whose thiol-disulfide state is regulated by this equilibrium — including key transcription factors (NF-κB, AP-1, Nrf2, p53), signalling kinases (PTPs, PTEN), apoptosis machinery (caspases), and metabolic enzymes (glyceraldehyde-3-phosphate dehydrogenase, others). GSH-mediated redox buffering is therefore not just an antioxidant defence but a signalling regulatory mechanism — a fact that has emerged in published research over the past two decades and is one of the most-cited rationales for the use of GSH in research protocols beyond simple antioxidant supplementation.
• Cysteine reservoir and inter-organ amino acid trafficking — GSH serves as a tissue-stable, transport-permissible reservoir of cysteine — the rate-limiting amino acid for new protein synthesis and for further GSH synthesis. Cysteine in free form is metabolically unstable (auto-oxidises to cystine, can generate H₂S, etc.), so the body maintains its cysteine pool largely as GSH and traffics cysteine between organs (especially liver → kidney, liver → other tissues) as GSH that is then processed back to cysteine by γ-GT at the target tissue.
• Direct radical scavenging — Beyond enzymatic roles, GSH directly reacts with hydroxyl radical, peroxyl radical, and reactive nitrogen species through the thiol group. Quantitatively this contributes less to total antioxidant defence than the enzymatic GPx-mediated mechanism, but is important in compartments and conditions where enzymatic systems are saturated or absent (extracellular GSH in lung lining fluid, gut lumen GSH, etc.).

The pharmacokinetic profile of injectable GSH is well-characterised: IV administration produces rapid systemic distribution with peak plasma concentrations within minutes, but plasma half-life is short (~10–15 minutes) due to rapid γ-GT-mediated breakdown to cysteinylglycine and subsequent re-synthesis or further breakdown at target tissues. The brief plasma residence is one of the reasons why daily or twice-daily IV dosing protocols are common in published GSH research. Cell-membrane permeability of intact GSH is low — cells primarily import the constituent amino acids and re-synthesise GSH intracellularly. This is why oral GSH is poorly bioavailable and why injectable preparations (or alternatively NAC as a cysteine prodrug) are required for effective tissue delivery in published research.

Opublikowane zastosowania badawcze

GSH is used in laboratory research contexts that investigate:

• Cellular antioxidant defence — the canonical reference compound — by far the most-cited cellular antioxidant in the published literature; standard reference compound for any new antioxidant intervention research; the molecular gold standard for cellular redox-status analysis
• Hydrogen peroxide and lipid peroxide reduction research — direct GPx substrate; used in published research on GPx isoform pharmacology, peroxide-handling pathway dissection, and the integration of GSH with thioredoxin and peroxiredoxin redox systems
• Ferroptosis research — GPx4-mediated lipid-hydroperoxide reduction is the gatekeeper of ferroptosis; GSH and its synthesis-pathway interventions (BSO, erastin, RSL3) are the canonical tools for ferroptosis induction / suppression research in cancer, neurodegeneration, and ischaemia-reperfusion contexts
• Phase II detoxification and xenobiotic-conjugation research — GST substrate for the central liver-detoxification pathway; used in research on drug-metabolite handling, environmental-chemical exposure, paracetamol-induced hepatotoxicity (NAPQI scavenging), and the broader pharmacology of mercapturic-acid conjugation
• Protein-thiol redox signalling research — the GSH:GSSG ratio controls thiol-disulfide equilibrium of thousands of cellular proteins; used in research on redox-sensitive transcription factors (Nrf2, NF-κB, AP-1), kinase regulation (PTPs, PTEN), and the broader cellular “redoxome”
• Mitochondrial dysfunction and ageing research — mitochondrial GSH levels decline with age and in many disease models; published research uses exogenous GSH and GSH-pathway interventions to probe mitochondrial-redox contributions to ageing, neurodegeneration, and metabolic disease
• Hepatology and liver-injury research — GSH is most abundant in hepatocytes (5–10 mM concentration); used in published research on alcoholic liver disease, NAFLD/MASH, viral hepatitis models, and paracetamol-overdose / drug-induced liver injury
• Hematology and erythrocyte research — erythrocyte GSH is the major defence against oxidative haemolysis; used in research on G6PD deficiency, sickle-cell disease, oxidative haemolysis pharmacology
• Cancer redox and chemoprotection research — many chemotherapeutic drugs generate ROS as part of their mechanism, and tumour cells often have elevated GSH levels; published research uses GSH and GSH-pathway interventions to dissect chemotherapy redox biology

For broader context on cellular cofactor and redox / antioxidant research compounds in this catalogue, see B12 (Cyanocobalamin) (small-molecule research-companion cofactor — methylation cycle), L-Karnityna (mitochondrial fatty-acid shuttle — companion small-molecule), NAD⁺ (direct dinucleotide-pool supplementation — redox electron-transport), 5-Amino-1MQ (NAD-axis sparing via NNMT inhibition), and SS-31 (Elamipretide) (cardiolipin-binding mitochondrial-targeted antioxidant peptide). Browse the full katalog peptydów i związków badawczych, lub zobacz przygotowane zestawy związków do badań nad długowiecznością hub.

Dostępne mocowania i stężenia

MedsBase stocks Glutathione in three lyophilized vial sizes calibrated to typical research-protocol dose ranges. Each strength is available in 10-vial or 20-vial pack formats:

All three strengths are the same chemical entity (lyophilized L-glutathione reduced form, ≥99% HPLC purity, USP-grade titration-confirmed reduced-form content). The 1500 mg vial provides the lowest per-mg cost for clinical-translational research protocols. Researchers should determine specific dose ranges from peer-reviewed literature appropriate to the protocol.

How It Compares — Glutathione vs NAD⁺

Glutathione and NAD⁺ are the two most-studied small-molecule cellular redox / coenzyme compounds in this catalogue, and they sit on connected but mechanistically distinct branches of cellular redox biology. GSH is the master cellular antioxidant defence small molecule — present at millimolar concentrations and reducing peroxides via the GPx-substrate mechanism. NAD⁺ is the master cellular electron-transport coenzyme — reducible to NADH for electron transport in glycolysis / TCA cycle / β-oxidation, and substrate for sirtuins and PARPs. The two systems are interconnected: NADPH (made from NAD via the pentose phosphate pathway) is the reducing equivalent that regenerates GSH from GSSG via glutathione reductase. Research that probes cellular redox biology often manipulates both pools and compares the consequences.

For research focused on cellular antioxidant defence, ferroptosis, Phase II detoxification, or redox signalling, Glutathione is the canonical reference compound. For research focused on sirtuin biology, longevity-axis biochemistry, or NAD-dependent redox regulation, NAD⁺ is the more targeted tool. The two compounds are commonly co-administered in research that probes the integrated cellular-redox-system response to oxidative stress, ageing, or mitochondrial dysfunction.

Przechowywanie i rekonstytucja

Przed rekonstytucją: store lyophilized vials refrigerated at 2–8 °C in original sealed packaging. For long-term storage, freeze unopened vials at −20 °C (stable ≥36 months at −20 °C; ≥18 months at 2–8 °C). Lyophilized GSH is highly hygroscopic — reseal vials promptly after each withdrawal to avoid moisture uptake (which accelerates GSH → GSSG oxidation). Protect from light.

Procedura rekonstytucji: inject sterile water, bacteriostatic water, or PBS (pH 7.2) down the side wall of the vial (not directly onto the lyophilized cake). For a 600 mg vial, 6.0 mL of diluent yields a 100 mg/mL working stock; 3.0 mL yields 200 mg/mL. For a 900 mg vial, 9.0 mL yields 100 mg/mL; 4.5 mL yields 200 mg/mL. For a 1500 mg vial, 7.5 mL yields a 200 mg/mL stock; 15 mL yields 100 mg/mL. GSH dissolves rapidly with gentle swirling at room temperature.

Critical for reconstituted GSH: the thiol (-SH) group is air-oxidation-sensitive — reconstituted solutions progressively oxidise to the GSSG form, even refrigerated. Prepare working solutions fresh from lyophilized vials where possible, or use within 7 days of reconstitution refrigerated. For long-term storage of reconstituted material, add chelators (1 mM EDTA) to slow metal-catalysed oxidation, store under inert atmosphere (argon or nitrogen-purged), or use DMSO co-solvent (which provides additional protection). Do not freeze-thaw repeatedly. Discard if marked colour change (yellow / brown) or precipitation appears.

Najczęściej zadawane pytania

What is the difference between reduced (GSH) and oxidised (GSSG) glutathione?

GSH is the reduced form with a free thiol (-SH) group on its cysteine residue — the biologically active form that serves as the cellular antioxidant. GSSG is the oxidised dimer form where two GSH molecules are linked through their cysteine sulfurs by a disulfide bridge — the spent form that needs to be re-reduced to 2 GSH by glutathione reductase. The cellular GSH:GSSG ratio (typically ~100:1 in healthy cells, dropping to 10:1 or lower under oxidative stress) is the canonical biomarker of cellular redox status. We supply the reduced GSH form; researchers requiring GSSG specifically should consult dedicated suppliers.

Why does GSH have a γ-peptide bond instead of a normal α-peptide bond?

The non-standard γ-peptide bond between glutamate’s γ-COOH and cysteine’s α-NH₂ is what gives glutathione its cellular peptidase-resistance. Standard cellular α-peptidases (aminopeptidases, carboxypeptidases) only recognise α-peptide bonds and cannot cleave the γ-bond. Only γ-glutamyltransferase (γ-GT, GGT) recognises and cleaves the γ-bond — and γ-GT is the rate-limiting enzyme of GSH degradation, expressed mainly on the apical surface of epithelial cells (kidney, biliary tract, etc.). This non-standard linkage is therefore essential for glutathione’s stable intracellular accumulation at millimolar concentrations.

Why is GSH oral bioavailability low?

Intact GSH is poorly absorbed across the intestinal epithelium because: (1) the γ-peptide bond prevents recognition by the standard PEPT1 / PEPT2 di-/tri-peptide transporters that absorb other tripeptides; (2) γ-GT activity at the brush border degrades much of the orally-administered GSH to its constituent amino acids before absorption; (3) the cysteine that is liberated is then largely consumed by enterocyte first-pass GSH re-synthesis. The net oral bioavailability of intact GSH is therefore very low, which is why injectable preparations or N-acetylcysteine (NAC, a cysteine prodrug) are preferred for systemic GSH-boosting research interventions.

Jakie opublikowane zakresy dawek były stosowane w badaniach?

Injectable IV GSH research-protocol dosing typically uses 600–1200 mg per dose, daily or 2–3×/week, for 4–12 weeks in human-subject research (mirroring the Italian Tationil approved-product dose range of 600–2400 mg/d). Rodent in-vivo work uses 50–150 mg/kg IV / IP, mirroring the dose range that produces reliable systemic GSH elevation despite the short plasma half-life. In-vitro cell-culture protocols typically use 0.5–10 mM in growth medium (cells take up cysteine from GSH and re-synthesise intracellular GSH). Researchers should consult primary literature appropriate to the specific application.

Why is GSH plasma half-life so short?

Plasma γ-GT activity rapidly cleaves the γ-peptide bond of circulating GSH to cysteinylglycine, which is then further cleaved by dipeptidases to cysteine + glycine. The combined γ-GT + dipeptidase cascade gives intact circulating GSH a plasma half-life of only ~10–15 minutes. This is why repeated daily dosing is used in clinical-research protocols rather than single high-dose bolus regimens, and why N-acetylcysteine (NAC) — which is taken up intact and used for intracellular GSH synthesis — is sometimes preferred as a longer-acting cysteine-source alternative for cellular GSH boosting research.

Can GSH be combined with B12, NAC, or other redox / cofactor compounds in research protocols?

Yes — GSH is mechanistically connected to many other cellular-redox and cofactor compounds. Common research-protocol combinations include: GSH + NAC (parallel cysteine-source strategies — GSH as the intact tripeptide, NAC as the cysteine prodrug — to compare extracellular vs intracellular GSH-supplementation routes); GSH + B12 (oxidative-stress-related neurology and methylation-cycle research); GSH + NAD⁺ (integrated redox-pool dissection); GSH + SS-31 (mitochondrial-targeted redox research). Reconstitute each separately just before use and add separately rather than co-storing reconstituted solutions.

How does this research-grade GSH compare with clinical preparations like Tationil?

Tationil (and similar branded clinical preparations available in Italy / Japan / Korea / Philippines) is reduced-form L-glutathione approved as a clinical injectable for hepatology and oxidative-stress indications. The research-grade GSH supplied here is the same reduced-form L-glutathione at ≥99% HPLC purity, supplied without a clinical-use label and intended for laboratory research only. Researchers seeking clinical-use GSH should obtain it through a clinical supply chain; researchers seeking research-grade material for in-vitro and in-vivo laboratory protocols can use the material supplied here.

Is GSH on the WADA Prohibited List?

No. Glutathione is not on the WADA Prohibited List. It is a naturally-occurring cellular antioxidant tripeptide present at millimolar concentrations in every nucleated cell — therefore not subject to athletic-performance regulatory restrictions.

Other Small-Molecule Research Companion Compounds

• B12 (Cyanocobalamin) — Cobalamin coenzyme — methylation-cycle research companion
• L-Karnityna — Mitochondrial fatty-acid shuttle — closest small-molecule research-companion analogue
• NAD⁺ — Oxidised dinucleotide coenzyme — direct NAD-pool / electron-transport research
• 5-Amino-1MQ — NNMT inhibitor — NAD-axis precursor sparing, methylation-pool buffering
• SS-31 (Elamipretide) — Cardiolipin-binding mitochondrial-targeted antioxidant peptide
• BAC Water (Woda bakteriostatyczna) — Wymagany do rekonstytucji każdej liofilizowanej fiolki — sterylny rozcieńczalnik z 0,9% benzylowym alkoholem jako środkiem konserwującym

Więcej opcji w Peptydach

Ranking według liczby ostatnich zamówień MedsBase — co wybierają inni klienci w tej kategorii.

BPC-157

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Retatrutide

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BAC Water (Woda bakteriostatyczna)

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NAD⁺

US$210.00 – US$1,975.00Fourchette de prix : US$210.00 à US$1,975.00