● In Stock
L-Glutathione
≥99% Purity | HPLC Verified
$100.00
PASSED
Sterility & Endotoxins
PASSED
Net Content & Purity
Purity:
≥99%
Store at
-20°C
L-Glutathione is a high-purity research compound for research use only.
Additional product information will be available soon.
1000+
Published Studies
Redox biology & antioxidant research
3
Amino Acids
Glu-Cys-Gly tripeptide
100:1
GSH:GSSG Ratio
Physiological redox couple
99%+
Purity Verified
HPLC tested, COA included
How L-Glutathione Works
The master endogenous antioxidant studied across redox signaling, detoxification, and oxidative-stress research models
Direct Antioxidant
Free Radical Scavenging
L-Glutathione (GSH) is a thiol-containing tripeptide that acts directly as an antioxidant, neutralizing reactive oxygen species, free radicals, peroxides, and lipid peroxides. The reactive cysteine thiol group donates electrons to stabilize oxidative species.
- Directly scavenges ROS, free radicals and peroxides
- Cysteine thiol group serves as the redox-active site
- Protects cellular proteins, lipids and DNA from oxidative damage
Enzyme Cofactor
GPx & GST Catalysis
GSH is the essential co-substrate for the glutathione peroxidase (GPx) family — including GPx4, which converts toxic lipid peroxides into non-toxic alcohols and is central to ferroptosis research — and for glutathione S-transferases (GST).
- Co-substrate for selenium-dependent GPx enzymes
- GPx4 cofactor — a key node in ferroptosis research
- Drives glutathione S-transferase detoxification reactions
Redox & Detox
Cellular Redox Homeostasis
The GSH:GSSG (reduced:oxidized) couple is the principal buffer of intracellular redox state. GSH also conjugates electrophilic xenobiotics for elimination and has been linked to activation of the Nrf2/HO-1 cytoprotective pathway.
- GSH:GSSG ratio sets cellular redox tone (~100:1 when healthy)
- Conjugates xenobiotics and electrophiles for detoxification
- Associated with Nrf2/HO-1 antioxidant-response signaling
What Research Has Shown
Key findings from biochemical and in vitro publications
⚠️ RESEARCH NOTE
L-Glutathione is an endogenous tripeptide found naturally in human cells. The research-grade L-Glutathione offered here is supplied strictly for in vitro laboratory research and is not intended for human or veterinary therapeutic use.
Research Applications
Primary areas of glutathione investigation
REDOX BIOLOGY
Oxidative Stress & Antioxidant Defense
GSH is the central reference antioxidant for studying redox signaling, free-radical chemistry, and cellular oxidative-stress responses.
CELL BIOLOGY
Ferroptosis & Lipid Peroxidation
As the GPx4 cofactor, glutathione is a key node in ferroptosis research — the iron-dependent, lipid-peroxidation form of regulated cell death.
CYTOPROTECTION
Nrf2/HO-1 Pathway Signaling
In vitro studies report glutathione protects cells from oxidative cytotoxicity in part by activating the Nrf2/HO-1 antioxidant-response pathway.
BIOCHEMISTRY
Detoxification & Redox Defense
Glutathione is studied as the principal substrate of the GST detoxification system and the master buffer of intracellular redox state.
Safety Profile from Research
Biochemical and in vitro observations
✓Glutathione is an endogenous molecule present in virtually all human cells; its biochemistry is extensively characterized.
✓In healthy cells, more than 90% of the glutathione pool is normally maintained in the reduced (GSH) form.
✓Reduced glutathione oxidizes readily in solution; handling under inert conditions preserves the reduced form for research use.
✓Research-grade L-Glutathione is for in vitro laboratory research use only and is not for human or veterinary use.
Compound Information
Technical specifications
| Chemical Name | L-Glutathione (reduced, GSH) |
| Sequence | γ-L-Glutamyl-L-Cysteinyl-Glycine |
| Molecular Weight | 307.32 g/mol |
| Molecular Formula | C₁₀H₁₇N₃O₆S |
| Content | 1500 mg per vial |
| Form | Lyophilized powder |
| Purity | ≥99% (HPLC verified) |
| Testing | Third-party HPLC, Mass Spec, Endotoxin |
| Storage (lyophilized) | -20°C for long-term stability |
| Storage (reconstituted) | 2–8°C, use promptly (oxidizes readily) |
| Solubility | Sterile or bacteriostatic water for reconstitution |
| COA | Included with every order |
Frequently Asked Questions
Common questions about L-Glutathione
L-Glutathione (GSH) is a tripeptide composed of glutamate, cysteine, and glycine. It is the most abundant intracellular antioxidant in human cells and is often called the "master antioxidant" for its central role in redox homeostasis, enzymatic detoxification, and protection against oxidative damage.
Glutathione works in two ways: directly, by using its reactive cysteine thiol group to neutralize free radicals and peroxides; and indirectly, as the essential co-substrate for glutathione peroxidase (GPx) and glutathione S-transferase (GST) enzymes that detoxify hydrogen peroxide, lipid peroxides, and electrophilic compounds.
The GSH:GSSG ratio compares reduced glutathione (GSH) to its oxidized disulfide form (GSSG). In healthy cells this ratio is high — roughly 100:1 — and it serves as a key indicator of cellular redox status. A falling ratio is widely used in research as a marker of oxidative stress.
Reduced glutathione (GSH) is the active antioxidant form with a free thiol group. When it neutralizes an oxidant, two GSH molecules join to form oxidized glutathione (GSSG). The enzyme glutathione reductase regenerates GSH from GSSG, keeping the antioxidant pool replenished.
Research-grade glutathione is used to study oxidative stress and antioxidant defense, ferroptosis and lipid peroxidation (via GPx4), xenobiotic detoxification, the Nrf2/HO-1 cytoprotective pathway, and redox involvement in models of aging and neurodegeneration.
Lyophilized L-Glutathione should be stored at -20°C, protected from light and moisture. Because reduced glutathione oxidizes readily once in solution, reconstituted material should be kept at 2–8°C and used promptly to preserve the reduced (GSH) form.
Sources & References
JOURNAL
Glutathione System Enhancement for Cardiac Protection: Options Against Oxidative Stress and Ferroptosis
2023
PMC
Protective Effect of Glutathione Against Oxidative Stress-Induced Cytotoxicity in RAW 264.7 Macrophages via the Nrf2/HO-1 Pathway
2019
JOURNAL
Glutathione: Role in Oxidative/Nitrosative Stress, Antioxidant Defense, and Treatments
2021
Published research on this compound is available through PubMed and other scientific databases.
Certificate of Analysis
| Analysis Date: | Available on request |
| Lot Number: | Batch-specific |
| Purity: | >99% (HPLC) |
Third-Party Testing
- ✓ Identity verification (Mass Spectrometry)
- ✓ Purity analysis (HPLC)
- ✓ Sterility testing
- ✓ Endotoxin screening
Storage Conditions
- Lyophilized: Store at -20°C, protected from light
- Reconstituted: Store at 2-8°C, use within 30 days
- Stability: 24 months from manufacture date when stored properly
Handling Guidelines
- Use sterile technique when reconstituting
- Allow vial to reach room temperature before opening
- Reconstitute with bacteriostatic water or sterile saline
- Avoid repeated freeze-thaw cycles
RESEARCH INSIGHTS
3D Structure
L-Glutathione
This compound has been extensively studied in peer-reviewed literature. Eon Peptides provides this product exclusively for legitimate in-vitro research and analytical applications.
- • High-purity research compound
- • Full analytical documentation included
- • Third-party verification available
PRODUCT SPECIFICATIONS
LOT DATA
| Lot Number | Assigned on shipment |
| Verified Purity | >99% |
| Quantity | 5mg |
MOLECULAR DATA
| Molecular Formula | Available on request |
| Form | Lyophilized Powder |
| Appearance | White to off-white powder |
