Oxidative Stress & Antioxidant Defense
GSH is the central reference antioxidant for studying redox signaling, free-radical chemistry, and cellular oxidative-stress responses.
Frontiers Pharmacol. 2014≥99% Purity
L-Glutathione
The body's master antioxidant for detox and skin health
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About this compound
L-Glutathione is the body's master antioxidant, researched for detoxification, immune support, protecting cells from oxidative stress, and skin brightening.
Thiol-containing tripeptide (Glu-Cys-Gly)
- Formula
- C₁₀H₁₇N₃O₆S
- Molecular weight
- 307.32 g/mol
- Form
- Lyophilized powder
- CAS / ID
- 70-18-8
0+
Published Studies
Redox biology & antioxidant research
0
Amino Acids
Glu-Cys-Gly tripeptide
0:1
GSH:GSSG Ratio
Physiological redox couple
0
Research Areas
Oxidative Stress & Antioxidant Defense · Ferroptosis & Lipid Peroxidation · Nrf2/HO-1 Pathway Signaling & more
How It Works
How L-Glutathione works
The pathways L-Glutathione acts on — and what each one does. The animation traces its signal outward from the compound to every target it engages.
Signalling pathways studied in preclinical models · illustrative
Free Radical Scavenging
Direct Antioxidant
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
GPx & GST Catalysis
Enzyme Cofactor
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
Cellular Redox Homeostasis
Redox & Detox
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
Uses & Applications
What L-Glutathione is researched for
The main areas L-Glutathione is being studied for — and the study-reported figures behind them.
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.
Cell Death & Disease 2023Nrf2/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.
Lee et al. 2019Detoxification & Redox Defense
Glutathione is studied as the principal substrate of the GST detoxification system and the master buffer of intracellular redox state.
Rai R. 2021Molecular Structure
The L-Glutathione molecule
An interactive 3D model rendered from the compound record — rotate and explore its structure.
C₁₀H₁₇N₃O₆S
Third-Party Verified
Independently tested. Verifiably pure.
Every batch of L-Glutathione is sent to an accredited independent laboratory before it ships. Here is what we screen for.
- HPLC Purity AnalysisConfirms the peptide is ≥99% pure
- Mass SpectrometryVerifies the exact molecular identity
- Heavy Metals ScreeningLead, arsenic, cadmium & mercury — Pass
- Endotoxins (LAL)Bacterial endotoxin levels — Pass
- Sterility TestingNo microbial contamination — Pass
- Net Peptide ContentActual peptide mass per vial verified
Certificate of Analysis · Freedom DiagnosticPASS
- HPLC Purity
- ≥99%
- Identity
- Mass-spec confirmed
- Endotoxin (LAL)
- Pass
- Net content
- Verified
Compound Information
Full specification
| 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 |
FAQ
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.
Published Literature
Cited Sources
Peer-reviewed literature
Independent published research indexed from PubMed and peer-reviewed journals — not Eon Peptides claims.
[1]
JOURNAL
[2]Glutathione: New Roles in Redox Signaling for an Old Antioxidant
View source JOURNAL
[3]Glutathione System Enhancement for Cardiac Protection: Options Against Oxidative Stress and Ferroptosis
View source PMC
[4]Protective Effect of Glutathione Against Oxidative Stress-Induced Cytotoxicity in RAW 264.7 Macrophages via the Nrf2/HO-1 Pathway
View source JOURNAL
Glutathione: Role in Oxidative/Nitrosative Stress, Antioxidant Defense, and Treatments
View source For Research Use Only.
Not for human or veterinary use. For in-vitro laboratory research only. These statements have not been evaluated by the FDA; this product is not intended to diagnose, treat, cure, or prevent any disease. Sold exclusively to qualified researchers and institutions.