Glutathione 1500mg

Buy high-purity glutathione (1500mg) in Australia. Third-party lab tested at >99% purity. Australian-domestic shipping, AUD pricing, supplied for laboratory research use only.

About glutathione

Glutathione (GSH) is an endogenous tripeptide composed of glutamate, cysteine and glycine, present in virtually every mammalian cell. It is the principal low-molecular-weight thiol antioxidant in eukaryotic cells and is central to redox homeostasis, phase II detoxification and the regulation of intracellular cysteine pools.

In published research, glutathione is most often studied in the context of oxidative stress, hepatic detoxification pathways, immune cell function and mitochondrial redox status.

Optic Labs supplies glutathione as a lyophilised powder in 1500mg research vials, third-party HPLC tested to >99% purity. The product is distributed Australian-domestic from Sydney, NSW, for in vitro and laboratory research applications. Glutathione is supplied strictly for laboratory research, development or analytical use and is not intended for human consumption.

Product specifications

• Compound: L-Glutathione (reduced; γ-L-glutamyl-L-cysteinyl-glycine)
• CAS number: 70-18-8
• Molecular formula: C₁₀H₁₇N₃O₆S
• Molecular weight: ~307.32 g/mol
• Sequence: γ-Glu-Cys-Gly (tripeptide)
• Form: Lyophilised powder
• Purity: >99% by HPLC
• Available size: 1500mg vial
• Storage: 2–8°C, protect from light. Reconstituted: 2–8°C, used within 30 days.
• Origin: Manufactured to research-grade specifications, third-party HPLC verified
• Shipping: Australia-wide domestic dispatch from Sydney, NSW

Research background

Glutathione was first isolated from yeast in 1888 and structurally characterised in the 1920s by Frederick Gowland Hopkins, who established its tripeptide identity. Since then it has become one of the most extensively studied small molecules in biochemistry, with the GSH/GSSG (reduced/oxidised) ratio used as a standard biomarker of intracellular redox state in cell-culture and animal model research.

• Antioxidant defence: in cell-culture studies, glutathione donates electrons via glutathione peroxidase (GPx) to neutralise hydrogen peroxide and lipid peroxides, with oxidised GSSG recycled by glutathione reductase using NADPH.
• Phase II detoxification: in hepatocyte and liver-tissue research, glutathione conjugation via glutathione S-transferases (GSTs) is a primary mechanism for clearing electrophilic xenobiotics, including paracetamol-derived NAPQI in animal toxicology models.
• Mitochondrial redox: mitochondrial glutathione (mtGSH) is studied in models of oxidative phosphorylation dysfunction, complex I inhibition and age-related mitochondrial decline.
• Immune cell function: in T-cell and macrophage research, intracellular GSH levels modulate cytokine profiles, NF-κB signalling and proliferation under oxidative challenge.
• Protein S-glutathionylation: reversible binding of GSH to protein cysteine residues is a regulatory post-translational modification studied in cardiac, neuronal and skeletal muscle models.
• Glutathione depletion models: buthionine sulfoximine (BSO) is used in rodent and cell research to inhibit γ-glutamylcysteine synthetase and study GSH depletion phenotypes.
• Skin and melanocyte cell research: in cell-culture studies, glutathione has been examined for its role in tyrosinase activity and pheomelanin/eumelanin balance.

For a more detailed research summary, see our glutathione antioxidant research guide and our what are peptides explainer. Researchers working with reconstitution should also reference our peptide reconstitution guide.

Reconstitution and handling

Unlike most short-chain research peptides, glutathione is highly water-soluble and can be reconstituted at relatively high concentrations. A common laboratory approach for the 1500mg vial is reconstitution in 5ml of bacteriostatic water to yield a 300mg/ml working stock, or in 10ml for a 150mg/ml stock.

Glutathione is sensitive to oxidation in solution, particularly at neutral and alkaline pH, so reconstituted solutions should be aliquoted, kept refrigerated at 2–8°C and protected from light. For dilution maths across alternative volumes, see our reconstitution calculator guide. For long-term storage protocols, see our peptide storage guide.

Commonly stacked research peptides

In published research and laboratory protocols, glutathione is often examined alongside other antioxidant, longevity and mitochondrial-function compounds:

• NAD+ — co-investigated in mitochondrial redox and longevity research; NAD+ supports the NADPH pool that regenerates reduced glutathione.
• SS-31 — mitochondrial-targeted peptide commonly studied alongside GSH in oxidative phosphorylation and cardiolipin protection models.
• MOTS-c — mitochondrial-derived peptide investigated for metabolic and redox effects in parallel with glutathione status.
• GHK-Cu — copper peptide studied alongside glutathione in skin, fibroblast and antioxidant gene-expression research.
• Epithalon — telomere and longevity research peptide frequently grouped with GSH in anti-ageing study designs.

For broader context on combined research designs, see our peptide research stacks overview.

Frequently asked questions

Is glutathione legal in Australia?

Glutathione is a naturally occurring tripeptide and is not a scheduled substance under the Australian Poisons Standard. However, products supplied for laboratory research are regulated differently from therapeutic goods. Optic Labs supplies glutathione strictly for laboratory, research and analytical use only, not as a therapeutic good.

For a full overview of how the Therapeutic Goods Administration treats research peptides in Australia, see our peptide legality and TGA compliance guide.

What is glutathione?

Glutathione is a tripeptide of glutamate, cysteine and glycine, found at high intracellular concentrations in virtually all mammalian cells. It is the body's major non-enzymatic thiol antioxidant and a central substrate in phase II liver detoxification. For a plain-language overview of peptides and how they differ from small-molecule drugs, see our what are peptides explainer.

What does glutathione do in published research?

In published in vitro and animal research, glutathione is studied as an electron donor for glutathione peroxidase (neutralising peroxides), as a conjugation partner in xenobiotic clearance via glutathione S-transferases, as a regulator of protein function via reversible S-glutathionylation, and as a marker of redox state through the GSH/GSSG ratio.

Researchers also examine its role in mitochondrial redox balance and immune cell signalling. These observations are research findings only and do not constitute therapeutic claims.

What is typically considered when working with glutathione in solution?

Researchers commonly account for glutathione's susceptibility to oxidation in aqueous solution, particularly at neutral or alkaline pH and in the presence of trace metals. Working stocks are usually prepared fresh, aliquoted to minimise freeze-thaw cycles, kept cold and shielded from light. In cell-culture work, GSH is often paired with chelators or prepared in degassed buffer to limit auto-oxidation prior to assay.

How is glutathione supplied?

Optic Labs supplies glutathione as a lyophilised powder in glass research vials at a 1500mg fill. Each vial is sealed with a tamper-evident closure. Certificates of analysis showing HPLC purity testing are available on request.

How much bacteriostatic water do I mix with a 1500mg glutathione vial?

For a 1500mg vial, 5ml of bacteriostatic water yields a 300mg/ml working stock; 10ml yields a 150mg/ml stock; 15ml yields a 100mg/ml stock. Choose a volume based on the concentrations required by the research protocol. For a step-by-step worked example with unit conversions, see our reconstitution calculator guide.

How should reconstituted glutathione be stored?

Reconstituted glutathione should be stored at 2–8°C, protected from light, and used within approximately 30 days. For longer-term storage, aliquoting and freezing at −20°C or below is preferred to limit oxidation and freeze-thaw degradation. Full handling protocols are covered in our peptide storage research guide.

Where does Optic Labs ship to?

Optic Labs ships Australia-wide from Sydney, NSW. Standard dispatch is next business day on orders received before the daily cut-off. International shipping is not currently offered.

Legal disclaimer

All products on this site are supplied for laboratory research, development or analytical use only. They are not for human consumption, clinical use, or any diagnostic, cosmetic or veterinary application. These products and statements have not been evaluated by the Therapeutic Goods Administration (TGA) or the APVMA and are not intended to diagnose, treat, cure or prevent any disease.

Optic Labs is not a compounding pharmacy or manufacturing facility as defined under the Therapeutic Goods Act 1989, and is not a registered provider of scheduled medicines or therapeutic goods.