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80 mg vial
Research use only. AminoBlend supplies research compounds for laboratory and in-vitro use, not for human or animal consumption. By continuing you confirm you are 18 or older and buying for research.

In stock, ready to ship from Australia
Size: 1,500 mg vial
Buy glutathione peptide online in Australia as a 1,500 mg fill of reduced L-glutathione for $69, packed into a 10 mL glass vial to hold the larger quantity. Glutathione (GSH) is the gamma-glutamyl-cysteinyl-glycine tripeptide that cells rely on as their main small-molecule antioxidant, and laboratories order it as a substrate for glutathione peroxidase and transferase assays, as a redox standard and for melanocyte culture work. Verify the identity data before you pay, namely C10H17N3O6S, 307.3 g/mol and CAS 70-18-8. Each lot is tested by mass spectrometry for identity and by HPLC for purity, a trace that also reveals how much has oxidised to GSSG, and the certificate is published ahead of checkout. Shop NAD+ in the same order for a metabolic counterpart. The powder ships without solvent, so dissolve weighed portions in bacteriostatic water or your assay buffer and set concentrations with the peptide calculator. Hold the sealed glutathione vial at -20 °C, dry and dark. It is sold as a laboratory reagent to adults aged 18 and over.
For laboratory research use only. Not for human or veterinary use. Not TGA approved. See our research use policy.
| Name | Glutathione, reduced (GSH, L-glutathione) |
|---|---|
| Sizes and prices (AUD) | 1,500 mg in a 10 mL vial, $69 |
| Sequence or structure | gamma-L-glutamyl-L-cysteinyl-glycine, with glutamate linked through its side-chain carboxyl |
| Length | 3 amino acids |
| Molecular formula | C10H17N3O6S |
| Molar mass | 307.3 g/mol |
| CAS number | 70-18-8 |
| Form | White lyophilised powder in a clear 10 mL glass vial with an amber cap |
| Testing | Identity by mass spectrometry, with purity and the oxidised GSSG share by HPLC, certificate for each lot |
| Contents | One vial holding 1,500 mg of reduced glutathione, solvent not included |
| Storage | -20 °C sealed, dark and dry, then 2 to 8 °C once dissolved |
| Availability | In stock |
| Use | Laboratory in vitro research only |
Order a fill sized for assays that consume glutathione by the milligram rather than the microgram. At roughly 4.9 millimoles per vial, one lot can carry a long run of plates.
Glutathione is a three amino acid molecule that cells build for themselves and use as their main chemical buffer against oxidation, handing electrons to damaging oxidants so that proteins, lipids and DNA do not have to. Calling it a glutathione peptide is accurate, although it differs from most peptides in how it is made, how it is linked and how cells move it around.
The story starts in 1888, when the French scientist Joseph de Rey-Pailhade described a sulfur-reducing substance in yeast that he named philothion. Hopkins isolated the compound in 1921 but first reported it as a two-residue molecule of glutamate and cysteine. Only in 1929 did improved purification show a third residue, glycine, and the tripeptide sequence was confirmed by chemical synthesis by Harington and Mead in 1935.
The reactive part is the sulfur on the cysteine residue. Its thiol group has a pKa of around 9, so at neutral pH most of it sits in the less reactive protonated form, and enzymes such as the glutathione S-transferases speed reactions partly by pulling that proton off. Concentrations vary widely by location. Cytosol holds it in the low millimolar range, blood plasma carries only micromolar amounts, and mitochondria cannot make their own supply and import it from the cytosol. The endoplasmic reticulum is the striking exception. There, a far more oxidised GSH to GSSG balance, reported at between 1 to 1 and 3 to 1 by Hwang, Sinskey and Lodish in Science in 1992, is what lets newly made proteins form their disulfide bonds correctly.
The thing we see misunderstood most often in culture work is uptake. Adding reduced glutathione to medium does not reliably raise the level inside the cells, because most cell types do not import the intact tripeptide; surface enzymes break it down and the cell rebuilds it from the parts. Researchers who need to raise intracellular glutathione usually turn to a cell-permeable ester such as glutathione monoethyl ester or to the cysteine donor N-acetylcysteine, and keep the free reagent for enzyme assays, standards and extracellular redox work, where it performs exactly as expected. The full guide to glutathione explains the GSH and GSSG cycle in more depth.
Cells make glutathione from glutamate, cysteine and glycine. Its distinctive feature is the gamma link between the first two residues, which runs through the glutamate side chain and protects the molecule from ordinary peptidases, letting cells hold it at millimolar levels. The working part is the cysteine thiol, which gives up electrons to reactive species and pairs with a second molecule to form the oxidised disulfide, GSSG. Synthesis takes two steps, through glutamate-cysteine ligase and glutathione synthetase, which is why depletion studies often pair the reagent with inhibitors of those enzymes.
That chemistry opens several uses. Reduced glutathione is the substrate for glutathione peroxidases and glutathione S-transferases, the GSH to GSSG ratio is a standard readout of oxidative stress, and melanocyte culture studies use it in tyrosinase and pigment pathway work, which is where a glutathione peptide for skin cell research fits. Shop it as a reagent, not a supplement or medicine, in our longevity peptides range.
Frederick Gowland Hopkins at Cambridge gave glutathione its name in 1921, and a century on it remains one of the most measured small molecules in biochemistry. Most peptides in our range mirror sequences that cells make on ribosomes, but glutathione is assembled by two enzymes instead, which is why its glutamate joins cysteine through a side chain. What we supply is the reduced form as a white powder, 1,500 mg of it in one 10 mL vial, with no capsule shell, liposome, flavouring or tablet binder alongside.
That last point matters, because the glutathione Australia shoppers meet in pharmacies and health food stores is a different kind of product. Oral glutathione is accepted as an ingredient in listed complementary medicines, the tier that carries an AUST L number and appears on the ARTG after the sponsor certifies it meets the rules rather than after a full TGA evaluation. Those products may make only low-level permitted claims, and the TGA has said it has not considered glutathione for skin lightening. Injectable glutathione is another matter again: in a 2023 enforcement action over advertised intravenous infusions, the TGA described glutathione as a prescription-only ingredient that cannot be promoted to the public. Our glutathione supplements guide explains the AUST L system in more detail.
So is glutathione legal in Australia? In capsules and tablets as a listed medicine, yes; injectable use sits inside the prescription framework. Neither route covers a reagent-grade bulk vial, which is why glutathione powder for assay work comes from laboratory suppliers. When you buy glutathione in Australia from AminoBlend, the vial comes from local stock as a research chemical, ordered by adults aged 18 and over for in vitro use, and it is not for human or veterinary use.
The single 1,500 mg format at $69 reflects how glutathione is used. Assays and culture media consume it in quantities far above those of signalling peptides, so a small vial would run dry after a few plates. The larger fill needs more headroom, which is why it ships in 10 mL glass instead of the 3 mL vials used across most of our catalogue.
Buy all the vials a project needs together so they share one lot wherever stock allows and one certificate, keeping redox baselines consistent across runs. Teams running enzyme kinetics often prepare a fresh standard each day, and the large fill means those daily weighings come from one lot for weeks. Orders are accepted from adults aged 18 and over, who declare their age at checkout.
For a thiol reagent, purity means more than unrelated contaminants. The HPLC trace on each certificate separates reduced GSH from oxidised GSSG, so you can see how much of the material is in the form your assay expects. Mass spectrometry confirms the 307.3 g/mol parent, and the report records the analysis date and lot code.
The oxidised dimer appears near 612.6 g/mol, so a lot carrying significant GSSG is easy to spot in the mass data too. Look up the lot in the COA library before ordering, and note that a lot missing specification is never offered for sale.
AminoBlend has no physical shop. Glutathione is ordered online and sent from stock held in Australia, with same-day dispatch for orders placed before 3pm on a business day and tracked delivery across the country.
Because the vial holds far more than one experiment uses, most labs weigh out portions rather than dissolving the whole fill. As a worked example, 100 mg dissolved in 2 mL of diluent gives 50 mg/mL. Use degassed water or buffer where possible, since dissolved oxygen speeds oxidation to GSSG, and let the peptide calculator handle other volumes. The bacteriostatic versus sterile water guide explains which diluent suits which assay.
Store the sealed vial at -20 °C and keep it dry, since the powder takes up moisture every time it is opened. Prepared solutions belong at 2 to 8 °C in small aliquots and should be used within 28 days, though fresher solutions give cleaner redox baselines. Close the vial tightly between weighings and return it to the freezer straight away.
Catalogues list it as glutathione, L-glutathione, reduced glutathione, GSH and gamma-L-glutamyl-L-cysteinylglycine, and older literature abbreviates the sequence as gamma-Glu-Cys-Gly. The oxidised form, glutathione disulfide or GSSG, is a different compound and is not what this vial contains.
Redox vocabulary linked to it includes thiol, glutathione peroxidase, glutathione reductase, glutathione S-transferase, NADPH and the GSH to GSSG ratio. CAS 70-18-8 ties every one of these names to reduced glutathione, which sulfur metabolism texts also discuss beside cysteine and methionine.
Pick glutathione when the question concerns thiol redox buffering, peroxide clearance or conjugation reactions. Pick NAD+ when it concerns energy metabolism, sirtuin activity or NAD-dependent enzymes. NAD+ is a coenzyme, not a peptide, and the two often run side by side in oxidative stress designs.
Shop SS-31 as a third angle when damage at the inner mitochondrial membrane itself is under study. Each product carries its own lot certificate, and pigmentation projects can browse the skin and hair peptides range.
Glutathione is a tripeptide with a reactive sulfur group that neutralises oxidants and feeds detoxifying enzymes.
One 10 mL vial holding 1,500 mg of reduced glutathione is priced at $69. No solvent is supplied, so add bacteriostatic water or use your own buffer.
Labs use it as an enzyme substrate, a redox standard and in melanocyte culture studies, always as a laboratory reagent.
NAD+ drives energy metabolism as a coenzyme, whereas glutathione buffers oxidants directly, and many studies measure both.
Keep the sealed vial at -20 °C away from moisture. Dissolved glutathione oxidises with time, so refrigerate aliquots and use them promptly.
HPLC on every lot shows purity and the share of oxidised GSSG, while mass spectrometry confirms identity. Certificates live in the COA library.
Add the 1,500 mg vial to your cart on this page and check out. It costs $69 and ships from Australian stock, with same-day dispatch for orders placed before 3pm on a business day. No solvent comes in the box, so order bacteriostatic water with it or prepare your own buffer.
AminoBlend makes no claims about skin, because this vial is a research reagent and not a cosmetic, supplement or medicine. In the laboratory, glutathione appears in melanocyte culture studies of tyrosinase and pigment pathways, measured in cells rather than people. It is sold for in vitro work only, to adults aged 18 and over.
The fill is 1,500 mg, far larger than the milligram quantities of most research peptides, because assays use glutathione in bulk as a substrate. A 3 mL vial could not hold that much powder with room to work, so it is filled into 10 mL glass under an amber cap.
Yes, every lot is analysed by mass spectrometry for identity and by HPLC for purity, and the HPLC trace also shows the proportion of oxidised GSSG. The report is listed in the COA library under the lot code printed on your vial and can be read before you order.
Buy glutathione for thiol redox buffering, peroxidase and transferase assays, or GSH to GSSG measurements. Buy NAD+ for energy metabolism and NAD-dependent enzymes. They cover different sides of oxidative stress, so many projects order both, each supplied with its own lot certificate.
Order it from the AminoBlend online store, which delivers from local stock to every Australian state and territory. There is no retail shop, so every lab orders the same way and can read the lot certificate before paying, including the HPLC figure for the reduced form.