Glutathione
Thiol-containing tripeptide studied in oxidative stress, antioxidant capacity, ferroptosis, redox balance, and cellular signaling research.
$90.00
- FormatLyophilized Powder / 1500 mg
- Storage-20°C for long-term stability
Glutathione is a naturally occurring tripeptide composed of three amino acids and is one of the most abundant antioxidants found within mammalian cells. It…
50 in stock
About Glutathione
L-Glutathione is a thiol-containing tripeptide composed of glutamate, cysteine, and glycine. It is widely studied as an intracellular antioxidant and redox regulator, with research examining free-radical scavenging, glutathione peroxidase and glutathione S-transferase activity, ferroptosis, Nrf2/HO-1 signaling, detoxification reactions, and cellular redox homeostasis.
Full Specification
| Molecular Formula | C10H17N3O6S (CAS 70-18-8) |
| Molecular Weight | 307.32 g/mol |
| Purity | ≥99% HPLC |
| Appearance | White to off-white lyophilized powder |
| Storage | -20°C for long-term stability |
| Format | Lyophilized Powder / 1500 mg |
The Glutathione Molecule
An illustrative representation generated from the compound's molecular formula, alongside its logged molecular data. This figure is schematic — not a measured conformation.
How Glutathione Works
The pathways 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 AntioxidantL-Glutathione acts as a thiol-containing antioxidant, donating electrons to stabilize reactive oxygen species, free radicals, peroxides, and lipid peroxides.
GPx & GST Catalysis
Enzyme CofactorGSH serves as a co-substrate for glutathione peroxidase enzymes, including GPx4, and supports glutathione S-transferase detoxification reactions.
Cellular Redox Homeostasis
Redox & DetoxThe GSH:GSSG couple is a major intracellular redox buffer, while GSH participates in xenobiotic conjugation and Nrf2/HO-1 antioxidant-response signaling.
What Glutathione Is Researched For
Oxidative Stress & Antioxidant Capacity
Studied in redox signaling, free-radical chemistry, and cellular oxidative-stress models.
Ferroptosis & Lipid Peroxidation
Studied in ferroptosis research through the role of glutathione and GPx4 in lipid peroxide regulation.
Nrf2/HO-1 Pathway Signaling
Studied in relation to antioxidant-response signaling and cellular oxidative-stress responses.
Xenobiotic Conjugation & Redox Balance
Studied as a substrate of the GST detoxification system and as a regulator of intracellular redox balance.
Common Questions About Glutathione
L-Glutathione is a reduced thiol-containing tripeptide composed of glutamate, cysteine, and glycine that is widely studied in cellular redox and oxidative-stress research.
Glutathione contains a reactive cysteine thiol group that can donate electrons to stabilize reactive oxygen species, free radicals, peroxides, and lipid peroxides.
The GSH:GSSG ratio compares reduced glutathione with oxidized glutathione and is commonly used as an indicator of cellular redox state. The source describes approximately 100:1 as a healthy reference ratio.
Reduced glutathione (GSH) contains the active thiol form, while oxidized glutathione (GSSG) represents glutathione after oxidation. Their ratio is used to study cellular redox balance.
L-Glutathione is studied in oxidative stress, antioxidant capacity, ferroptosis, lipid peroxidation, Nrf2/HO-1 signaling, xenobiotic conjugation, and cellular redox homeostasis.
The supplied specification recommends storage at -20°C for long-term stability.