Description

Glutathione (GSH) is a tripeptide made of glutamate, cysteine and glycine (γ-L-glutamyl-L-cysteinyl-glycine). The unusual gamma bond between glutamate and cysteine protects it from most peptidases, and the free thiol on cysteine gives it its reducing activity. This product supplies reduced L-glutathione for laboratory research.

What is Glutathione?

Glutathione is the most abundant low-molecular-weight thiol in animal cells, typically present at millimolar concentrations. Cells synthesise it in two ATP-dependent steps catalysed by glutamate-cysteine ligase and glutathione synthetase. It serves as the electron donor for glutathione peroxidases, the substrate for glutathione S-transferases in conjugation reactions, and a buffer that keeps protein thiols reduced. The ratio of reduced to oxidised glutathione (GSH/GSSG) is one of the most widely used markers of cellular redox state.

Research Applications

Oxidative stress and redox signalling assays
GSH/GSSG ratio measurement and calibration standards
Glutathione peroxidase and glutathione S-transferase enzyme kinetics
Xenobiotic conjugation and detoxification pathways in cell models
Protein S-glutathionylation studies

Product Specifications

Compound: reduced L-glutathione (GSH), CAS 70-18-8
Molecular formula: C10H17N3O6S, molar mass 307.32 g/mol
Size: as listed in the product options
Form: lyophilized powder in a sealed vial
Purity: ≥99% (HPLC), manufactured in the USA
Certificate of Analysis available for each batch
Storage: store lyophilized product at -20°C, protected from light

For research use only. Not for human or veterinary use. Not a drug, food, or cosmetic. Sold to qualified researchers for in-vitro and laboratory research.