Oxidative Stress & Antioxidant Capacity
GSH is the central reference antioxidant for studying redox signaling, free-radical chemistry, and cellular oxidative-stress responses.
≥99% Purity
L-Glutathione
Oxidative Stress Studies
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About this compound
L-Glutathione is a peptide made of three amino acids. It is the most common antioxidant found inside mammalian cells. It cycles between two forms, and the ratio between them is a standard way to measure oxidative stress. Studies have examined that ratio, along with its role in detoxification reactions. One of its chemical bonds is built differently from a normal peptide bond. That is why most enzymes cannot break it apart.
Thiol-containing tripeptide (Glu-Cys-Gly)
- Formula
- C₁₀H₁₇N₃O₆S
- Molecular weight
- 307.32 g/mol
- Form
- Lyophilized powder
- CAS / ID
- 70-18-8
0
Amino Acids
Glu-Cys-Gly tripeptide
0:1
GSH:GSSG Ratio
Physiological redox couple
0
Research Areas
Oxidative Stress & Antioxidant Capacity · Ferroptosis & Lipid Peroxidation · Nrf2/HO-1 Pathway Signalling & 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
- Oxidative damage to proteins, lipids and DNA measured
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.
Nrf2/HO-1 Pathway Signaling
In vitro studies report lower oxidative cytotoxicity alongside Nrf2/HO-1 antioxidant-response pathway activation.
Xenobiotic Conjugation & Redox Balance
Glutathione is studied as the principal substrate of the GST detoxification system and the master buffer of intracellular redox state.
Molecular Structure
The L-Glutathione molecule
An interactive 3D model rendered from the compound record — rotate and explore its structure.
C₁₀H₁₇N₃O₆S
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 | -20°C for long-term stability |
| Solubility | Water-soluble |
| 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 capacity, ferroptosis and lipid peroxidation (via GPx4), xenobiotic conjugation, the Nrf2/HO-1 cytoprotective pathway, and redox involvement in models of ageing and neurodegeneration.
Lyophilized L-Glutathione should be stored at -20°C, protected from light and moisture. Reduced glutathione oxidizes readily in solution, so the lyophilized material is the stable form for storage.
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.