Glutathione
Glutathione (GSH) is a tripeptide of glutamate, cysteine and glycine, the principal intracellular thiol antioxidant. Molecular mass 307.3 g/mol.
1 vial · 1500 mg total
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Intracellular Thiol Antioxidant
Tripeptide thiol that reacts directly with reactive oxygen species in cell models
Conjugation Substrate
Substrate for glutathione-S-transferase conjugation reactions
GSH/GSSG Redox Cycling
Oxidised GSSG is regenerated to GSH by glutathione reductase using NADPH
Mechanism of Action
About Glutathione
Glutathione (GSH) is a tripeptide of glutamate, cysteine and glycine (molecular mass 307.3 g/mol). Its reactive thiol (-SH) group on the cysteine residue is the chemically active site, and it is the principal intracellular thiol antioxidant. Milo-Lab supplies it as a 1500mg vial.
Research Areas
- Redox biochemistry and oxidative stress markers in cell models
- Glutathione peroxidase and glutathione reductase enzyme systems
- Glutathione-S-transferase conjugation chemistry
- GSH/GSSG cycling and NADPH-dependent regeneration
- Thiol chemistry and stability of glutathione in solution
How Glutathione Works
Glutathione’s reactive thiol (-SH) group reacts directly with reactive oxygen species. It also serves as the electron donor for glutathione peroxidase enzymes, which reduce hydrogen peroxide and lipid peroxides. In glutathione-S-transferase reactions it is conjugated to electrophilic substrates. The oxidised form (GSSG) is recycled to GSH by glutathione reductase using NADPH.
Storage
Lyophilised vials: store at -20°C, protected from light.
For research purposes only. Not for human consumption.
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