Molecular data
| Molecular formula | C₁₀H₁₇N₃O₆S |
|---|---|
| Molecular weight | 307.32 Da |
| Sequence | γ-L-Glutamyl-L-Cysteinyl-Glycine (Glu-Cys-Gly) |
| Sequence length | 3 residues |
| CAS / identifier | 70-18-8 |
| Physical form | Lyophilized powder |
| Available sizes | 1500mg |
How it works
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
- Oxidative damage to proteins, lipids and DNA measured
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
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 the research shows
Oxidative Stress & Antioxidant Capacity
GSH is the central reference antioxidant for studying redox signaling, free-radical chemistry, and cellular oxidative-stress responses.
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.
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 |
Frequently asked questions
What is L-Glutathione?
L-Glutathione (GSH) is a tripeptide composed of glutamate, cysteine, and glycine. It is the most abundant intracellular antioxidant in human cells, with a central role in redox homeostasis, enzymatic detoxification, and protection against oxidative damage.
How does glutathione work as an antioxidant?
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.
What is the GSH:GSSG ratio?
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.
What is the difference between reduced and oxidized glutathione?
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.
What research contexts use glutathione?
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.
How should research-grade L-Glutathione be stored?
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.
For laboratory research use only. Not a drug, supplement, or medical product; not for human or animal use. All findings referenced are from published preclinical/laboratory research.