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Glutathione · 600mg
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99%+ HPLC Purity — Independently verified by accredited US laboratory -
Endotoxin-Screened — LAL tested, LPS-free, endotoxin report available
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GMP-Certified Manufacturing — USA facility, ISO 9001:2015
-
Lyophilized for Stability — Shipped cold-packed, intact for reconstitution
Molecular Weight
Third Party Tested
APPLICATION
For Research Use only
Form
Lyophilized Powder
Storage
-20°C Long Term
Purity (HPLC)
99%+ Third Party Verified
Manufacture
USA / GMP
4.9 847 verified reviews
Glutathione · 600mg
Total Price
$179.97
Discounted Price
$149.37
Vials
3 vials
You Save
$30.60
17% OFF
Select Strength (mg)
99% HPLC Purity
Select Vials
Bulk pricing applied
📈 Upgrade to 10 vials and save an extra vs. buying 5 — nearly 3 free vials.
Select Purchase Option:
-
99%+ HPLC Purity —
Independently verified by accredited US laboratory
-
Endotoxin-Screened —
LAL tested, LPS-free, endotoxin report available
-
GMP-Certified Manufacturing —
USA facility, ISO 9001:2015
-
Lyophilized for Stability —
Shipped cold-packed, intact for reconstitution
Molecular Weight
Third Party Tested
APPLICATION
For Research Use only
Form
Lyophilized Powder
Storage
-20°C Long Term
Purity (HPLC)
99%+ Third Party Verified
Manufacture
USA / GMP
Glutathione 600mg is supplied strictly for laboratory research use only. This material is intended for analytical and controlled research applications. It is not approved or intended for human or animal use, ingestion, dosing, or therapeutic application.
Glutathione is a tripeptide (glutamate–cysteine–glycine) widely used as a reference compound in redox-biology and enzymology research. Published in-vitro literature has characterised it in the following experimental contexts:
Redox chemistry. The reduced (GSH) and oxidised (GSSG) forms are commonly quantified as a ratio in cell-culture models used to describe oxidative state. Interconversion between the two forms is catalysed by glutathione reductase.
Conjugation chemistry. Glutathione S-transferase enzymes catalyse conjugation of glutathione to electrophilic substrates, a reaction frequently used in enzymology and metabolite-identification assays.
Antioxidant cycling models. Its chemical interaction with ascorbate and tocopherol has been described in model systems.
Cell-signalling literature. Intracellular glutathione concentration is reported as an experimental variable in published lymphocyte and natural-killer-cell assay models.
Enzyme-inhibition literature. Interaction with tyrosinase has been described in in-vitro pigment-chemistry studies.
The material is produced as a high-purity research reagent under controlled conditions, with batch-level quality control to support reproducibility across laboratory studies.
This product is intended strictly for research and laboratory use only. Not for human or animal use. No statement on this page describes or implies any physiological, cosmetic, diagnostic, or therapeutic effect in humans or animals.
Glutathione at a glance
| Molecular formula | C10H17N3O6S |
|---|---|
| Molecular weight | 307.33 g/mol |
| CAS number | 70-18-8 |
| Application | Research use only |
What is Glutathione?
Glutathione is the tripeptide γ-L-glutamyl-L-cysteinylglycine, the most abundant low-molecular-weight thiol in mammalian cells. Its reactivity comes from the cysteine sulfhydryl group, and it cycles between a reduced (GSH) and an oxidised disulfide (GSSG) form.4
Why is Glutathione studied?
Glutathione has been a central subject of biochemistry since Meister and Anderson’s 1983 review in Annual Review of Biochemistry, which consolidated its role in thiol–disulfide chemistry, detoxification conjugation and amino-acid transport.4 It remains a standard analyte because the GSH:GSSG ratio is widely used as a readout of cellular redox state.5
How is Glutathione studied in the lab?
Laboratory work in this area measures intracellular GSH and GSSG pools, the activity of the two synthetic enzymes glutamate-cysteine ligase and glutathione synthetase, and the transcriptional regulation of those enzymes; Lu’s 2013 review in Biochimica et Biophysica Acta describes the synthesis pathway and its regulation in detail.5
What has preclinical research reported?
Antioxidant and redox activity
Glutathione is a major intracellular antioxidant that helps control reactive oxygen species and maintain cellular redox balance. Its reduced form (GSH) can be oxidized to GSSG and subsequently regenerated through the glutathione reductase system.
Detoxification and glutathione S-transferases
Glutathione participates in cellular detoxification by serving as a substrate for glutathione S-transferases (GSTs). These enzymes facilitate the conjugation of GSH with various electrophilic compounds, helping cells process and eliminate certain endogenous and foreign substances.
Glutathione and immune-cell function
Research indicates that intracellular glutathione contributes to normal immune-cell activity, including T-cell proliferation and other functions of innate and adaptive immunity.
Role in melanogenesis and tyrosinase activity
Glutathione has been investigated for its effects on melanin production. Proposed mechanisms include modulation of tyrosinase activity and a shift in melanin synthesis toward pheomelanin.
Biosynthesis and regulation
Lu reviewed glutathione synthesis, reporting that the pathway is controlled at the level of glutamate-cysteine ligase and is responsive to oxidative and nutritional signals.5
Forms studied and handling
Supplied as a lyophilised powder. Thiols oxidise on exposure to air, so store as stated in the specification box above, keep the vial sealed and protected from light, and prepare working solutions immediately before use.
References
- Forman, H. J., Zhang, H., & Rinna, A. (2009). Glutathione: overview of its protective roles, measurement, and biosynthesis. Molecular aspects of medicine, 30(1-2), 1–12. https://doi.org/10.1016/j.mam.2008.08.006. View record
- Townsend DM, Tew KD, Tapiero H. The importance of glutathione in human disease. Biomed Pharmacother. 2003;57(3-4):145-155. doi:10.1016/s0753-3322(03)00043-x. View record
- Dröge, W., & Breitkreutz, R. (2000). Glutathione and immune function. The Proceedings of the Nutrition Society, 59(4), 595–600. https://doi.org/10.1017/s0029665100000847. PMID 11115795
- Meister A, Anderson ME. Glutathione. Annu Rev Biochem. 1983;52:711–760. doi:10.1146/annurev.bi.52.070183.003431
- Lu SC. Glutathione synthesis. Biochim Biophys Acta. 2013;1830(5):3143–3153. doi:10.1016/j.bbagen.2012.09.008
For laboratory research use only. Products on this website are intended solely for in-vitro research. They are not medicines, have not been evaluated by the FDA, and are not intended to diagnose, treat, cure, or prevent any disease. Any administration to humans or animals is strictly prohibited.
What are these peptides made for?
Our peptides are produced exclusively for laboratory and scientific research purposes.
Licensed Peptides™ products are developed using industry-standard synthesis and purification protocols, making them suitable for in vitro research, analytical testing, and experimental models.
Research-grade standards
- Synthesized via Solid Phase Peptide Synthesis (SPPS)
- Purified using advanced HPLC methods
- Verified through analytical quality control processes
- Screened for heavy metals and endotoxins
Consistency across batches
Strict process controls ensure reproducibility, allowing researchers to work with confidence across experiments.
Applications
Our peptides are commonly used in research involving:
- Cellular signaling pathways
- Tissue remodeling and repair mechanisms
- Extracellular matrix regulation
- Molecular biology and biochemical studies
All products are intended for research use only and are not for human or animal consumption, therapeutic use, or clinical application.
Why buy from Licensed Peptides
At Licensed Peptides™, quality isn’t a claim — it’s a controlled, repeatable process.
Every peptide we produce follows a strict, pharma-grade workflow designed to ensure purity, stability, and consistency from synthesis to delivery.
What sets us apart
ISO-certified cleanroom manufacturing
All peptides are synthesized in sterile, controlled environments to eliminate contamination risk and ensure batch consistency.
>99% verified purity (HPLC tested)
We use advanced High-Performance Liquid Chromatography (HPLC) to separate and verify peptide purity with precision.
Comprehensive safety testing
Each batch undergoes heavy metal and endotoxin screening to ensure it is free from hidden contaminants.
Pharma-grade raw materials
We start with rigorously tested amino acids and reagents, ensuring integrity at the molecular level.
Lyophilized for stability
Freeze-dried peptides maintain long-term stability, potency, and reliability for research applications.
Nitrogen-sealed vials
Every vial is protected from oxygen and moisture, preserving structural integrity during storage and transit.
Built for serious research
From synthesis to delivery, every step is engineered to meet the expectations of professionals who require accuracy, consistency, and reliability.
For laboratory research use only. Not for human or veterinary use.
How orders ship
We understand that timing and product integrity are critical for research.
| Ships to | United States (including minor outlying islands) |
|---|---|
| Processing days | Monday to Friday, excluding holidays |
| Daily cut-off | Paid orders placed before 4:00 PM PST are typically shipped the same business day |
| Free shipping | FedEx 2-Day Express on orders over $200 and for VIP members |
| Standard | USPS Ground Advantage, 3–7 business days (not guaranteed) — $8.95 |
| Expedited | FedEx 2-Day $11.95 · UPS 2-Day $19.95 · FedEx Next Day $44.99 |
| Signature | Required on delivery for orders of $1,000 or more |
How orders are handled
Cold chain protection
Products are stored in industrial-grade freezers prior to shipment to maintain stability and purity.
Secure & protective packaging
Each order is carefully packed to protect against temperature fluctuations, moisture exposure, and physical damage during transit.
Tracking
Once your order has shipped you will receive a tracking number by email, so you can monitor delivery progress.
Shipped from the United States
Orders are dispatched domestically from a U.S.-based operation, so there are no international customs steps.
Delivery times
Shipping times are estimates and begin after order processing. Delays may occur due to carrier issues, weather, or other unforeseen factors, and delivery dates are not guaranteed. Full terms are in our Shipping & Delivery Policy.
For laboratory research use only. Not for human or veterinary use.
Storage conditions at a glance
| Lyophilized, in transit | Stable for shipping for up to 3–4 months |
|---|---|
| Lyophilized, short term | Room temperature is usually adequate for several weeks; refrigeration under 4°C (39°F) is generally acceptable |
| Lyophilized, long term | Freezer at -80°C (-112°F) for several months to years |
| After reconstitution | Refrigerated; stable for up to 30 days |
| Light and moisture | Keep cold and away from light in the original sealed vial |
Why the powder is stable
All of our products are manufactured using the lyophilization (freeze drying) process, which keeps them stable for shipping for up to 3–4 months.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until it is reconstituted with bacteriostatic water.
Storing vials on arrival
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used in the next several days, weeks or months, short-term refrigeration under 4°C (39°F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
For longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80°C (-112°F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide’s stability.
After reconstitution
Once the peptides are reconstituted with bacteriostatic water, they must be stored in the fridge to maintain stability. After reconstitution, the peptides will remain stable for up to 30 days.
For laboratory research use only. Not for human or veterinary use.
99%+ Every Batch
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