Glutathione
1500mg
Glutathione is a tripeptide composed of glutamate, cysteine and glycine, synthesised intracellularly in mammals and present in millimolar concentrations in most tissues. Research has investigated its role as a major antioxidant, electrophile scavenger and substrate for glutathione peroxidase and glutathione S-transferase enzymes in oxidative stress and detoxification pathways. Lyophilised powder, third-party tested.
Published research on Glutathione is indexed on PubMed. See our full UK buyer's guide for Glutathione.
Intended Use: Strictly for in-vitro laboratory research. Not for use in humans or animals. Not to be used in foods, drugs, or medical diagnostics. This product has not been evaluated by the MHRA or FDA. Buyer assumes full responsibility for safe handling and regulatory compliance.
99.95%
Purity
LAB
Certified
SAME
Day Ship
Quantity
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Mitochondrial Research Stack
Cellular bioenergetics pairing. NAD+ and Glutathione.
Buy Glutathione as part of this curated 2-vial research stack instead of separately. Same components, lower total price.
Research Use Only
This product is intended strictly for research and laboratory use only. Not for human consumption, medical use, or diagnostic purposes.
Certificate of Analysis
Third-party tested
Lyophilised Stability
24 months
Sealed at -20°C, light-protected
Reconstituted Stability
Up to 3 months
Stored at 2-8°C after mixing
Cold-Chain Shipping
Always
Dry-cold pack, Royal Mail Tracked 24
Important Notice
All compounds are sold individually and do not include research supplies. Products are provided in lyophilised (powder) form and require proper reconstitution before use in research settings.
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Glutathione Price (UK)
Glutathione 1500mg is £34.99 per vial, supplied from stock in the UK with a third-party HPLC certificate published on this page. UK delivery is £4.50 by Royal Mail Tracked 24, or free once your basket reaches £45 (£10.01 away at this price). Orders placed before 2pm on a working day are dispatched the same day.
| Vial | Price | Cost per mg | Availability |
|---|---|---|---|
| Glutathione 1500mgThis page | £34.99 | £0.023 | In stock |
Prices are in GBP and shown per vial as supplied, lyophilised, for in-vitro laboratory research only. Cost per mg is given so researchers can compare vial sizes on a like-for-like basis. Stock and pricing on this table are read live from our inventory, so they match the basket. See our FAQ for delivery and payment options, and quality & testing for how each batch is verified.
Product Specifications
Research Overview
Glutathione is the tripeptide gamma-L-glutamyl-L-cysteinyl-glycine, molecular formula C₁₀H₁₇N₃O₆S, molecular weight 307.32 g/mol, CAS 70-18-8. Its defining structural feature is the gamma-glutamyl linkage: the glutamate residue is joined through its side-chain carboxyl rather than the usual alpha-peptide bond, which makes the molecule resistant to most intracellular peptidases and means it is cleaved almost exclusively by gamma-glutamyl transpeptidase at the outer cell surface (Zhang, Forman and Choi, Methods in Enzymology, 2005). Biosynthesis runs through two ATP-dependent steps, glutamate-cysteine ligase (EC 6.3.2.2) followed by glutathione synthetase. The first step is rate-limiting and subject to feedback inhibition by glutathione itself, holding intracellular concentrations in the low millimolar range, typically 1 to 8 mM (Griffith, Free Radical Biology and Medicine, 1999; Lu, Biochimica et Biophysica Acta, 2013). Research interest centres almost entirely on the cysteine thiol. As a soft nucleophile it conjugates electrophiles in glutathione S-transferase-catalysed phase-II reactions; as a two-electron reductant it supplies reducing equivalents to the glutathione peroxidase family, cycling to the disulfide GSSG and back through glutathione reductase and NADPH. Schafer and Buettner (Free Radical Biology and Medicine, 2001) formalised the GSSG/2GSH couple as a quantitative index of the cellular redox environment, a framework still used to describe redox state across proliferation, differentiation and apoptosis in cultured cells. Interest broadened sharply after Yang and colleagues (Cell, 2014) used targeted metabolomic profiling across twelve ferroptosis-inducing small molecules and found that glutathione depletion converges on inactivation of the selenoenzyme glutathione peroxidase 4, placing glutathione availability directly upstream of iron-dependent lipid peroxidation. Laboratories sourcing glutathione in the UK generally use it as a defined reductant and as a substrate for GST and GPx assays in oxidative stress, xenobiotic conjugation and ferroptosis models. Supplied as lyophilised L-glutathione powder for in-vitro research use only.
Product Specifications
Laboratory Handling
- Store lyophilised vials at -20°C, protected from light and moisture. Reconstituted solution should be kept at 2-8°C and used within 4 weeks.
- Reconstitute with bacteriostatic water, adding the solvent slowly down the inner glass wall rather than directly onto the powder, then swirl gently until fully dissolved. Do not shake or vortex.
- The free thiol oxidises to the disulfide GSSG on air exposure, and the oxidation rate rises with pH as thiolate character increases. Minimise headspace and stopper-open time, keep solutions cold, and prepare single-use aliquots rather than repeatedly accessing one vial.
- Handle under aseptic laboratory conditions with alcohol-swabbed stoppers and sterile syringes. Avoid repeated freeze-thaw cycles, which accelerate loss of reduced glutathione relative to GSSG.
Frequently Asked Questions
What is Glutathione?
Glutathione (GSH) is the endogenous tripeptide gamma-L-glutamyl-L-cysteinyl-glycine, molecular formula C₁₀H₁₇N₃O₆S, molecular weight 307.32 g/mol, CAS 70-18-8. The glutamate residue is linked through its side-chain carboxyl, giving a gamma-glutamyl bond rather than a standard alpha-peptide bond, which is why the molecule resists most intracellular peptidases and is cleaved chiefly by gamma-glutamyl transpeptidase at the cell surface. It is synthesised in the cytosol by glutamate-cysteine ligase (EC 6.3.2.2) and glutathione synthetase, with the first, rate-limiting step feedback-inhibited by glutathione itself and intracellular concentrations typically 1 to 8 mM (Griffith, Free Radical Biology and Medicine, 1999). Supplied as lyophilised L-glutathione powder for in-vitro research use only.
Glutathione vs N-Acetylcysteine (NAC)
Glutathione and N-acetylcysteine sit at different points on the same pathway. Glutathione is the finished tripeptide and the direct cosubstrate for glutathione S-transferases and the glutathione peroxidases; N-acetylcysteine is an acetylated cysteine derivative that acts upstream, deacetylated intracellularly to supply the cysteine that limits glutamate-cysteine ligase flux. The practical distinction in experimental design is compartmental. Intact glutathione is poorly membrane-permeant and extracellular glutathione is degraded by gamma-glutamyl transpeptidase before its amino acids are reimported (Zhang, Forman and Choi, Methods in Enzymology, 2005), whereas cysteine-delivery agents bypass that step. Researchers also distinguish reduced glutathione (GSH) from the disulfide GSSG, since it is the GSSG/2GSH ratio, not total glutathione, that Schafer and Buettner (Free Radical Biology and Medicine, 2001) established as the quantitative index of the cellular redox environment. Both compounds are research chemicals only and neither is supplied for human use.
Glutathione Research Applications
Glutathione is used as a defined reductant and enzyme substrate across oxidative stress, xenobiotic metabolism and redox signalling research. Typical applications include glutathione S-transferase phase-II conjugation assays, glutathione peroxidase and glutathione reductase coupled assays, GSH/GSSG ratio determination as a redox readout in cultured cells, protein S-glutathionylation studies, and ferroptosis models where glutathione availability governs glutathione peroxidase 4 activity and therefore phospholipid hydroperoxide handling (Yang et al., Cell, 2014). It is also used in glutamate-cysteine ligase regulation and Nrf2/ARE pathway work, where glutathione acts as the feedback inhibitor of its own synthesis (Lu, Biochimica et Biophysica Acta, 2013).
Reconstitution Guide
Allow the vial to reach room temperature, then sterilise the rubber stopper of both the glutathione vial and the bacteriostatic water vial with an alcohol swab. Draw the bacteriostatic water into a sterile syringe and inject it slowly down the inner glass wall of the vial, never directly onto the lyophilised powder. Swirl gently in a slow circular motion until fully dissolved. Never shake or vortex. The solution should be clear and colourless. Because the cysteine thiol oxidises to the disulfide GSSG on air exposure, keep stopper-open time and headspace to a minimum and avoid alkaline solvents, which increase thiolate character and accelerate oxidation. Label the vial with the reconstitution date and refrigerate immediately.
See our full peptide reconstitution guide and reconstitution calculator for step-by-step protocol.
Storage Instructions
Lyophilised vials should be stored at -20°C, protected from light and moisture, and remain stable for up to 24 months. Once reconstituted with bacteriostatic water, store at 2-8°C and use within approximately 4 weeks. For longer storage, prepare single-use aliquots at -20°C. Repeated freeze-thaw cycles and repeated stopper punctures both shift the reduced to oxidised balance, so aliquoting matters more for glutathione than for a non-thiol compound. Handle under sterile laboratory conditions throughout.
Frequently Asked Questions
Research References
Related Research Compounds
Research Guides
Glutathione
1500mg · £34.99