L-Glutathione
Master antioxidant tripeptide. Oxidative-stress research.
Specification
- Catalogue ID: SP120
- HPLC purity: 99.0%
- Formulation: Lyophilized
- Quantity: 1500mg / Vial
- Price: £70.00
Oxidative-stress research · redox homeostasis · GST substrate
Glutathione (γ-glutamyl-cysteinyl-glycine; GSH) is the most abundant intracellular low-molecular-weight thiol, present in mammalian cells at millimolar concentrations. Its tripeptide structure contains an unusual γ-amide bond between the glutamate side-chain carboxyl group and the cysteine amino group — a non-standard linkage that confers resistance to most peptidases.
The thiol (–SH) group of the cysteine residue is the reactive centre of glutathione's antioxidant function. GSH donates electrons to reactive oxygen species (ROS) and oxidised protein thiols, becoming oxidised glutathione disulphide (GSSG). Glutathione peroxidase (GPx) catalyses this reaction as part of the cellular antioxidant cycle; GSSG is recycled by glutathione reductase using NADPH as the electron donor.
In vitro, glutathione is used extensively to study intracellular redox homeostasis, cysteine availability for protein folding and S-glutathionylation signalling, and as a substrate for glutathione-S-transferase (GST) enzyme activity assays. It is also a core reagent in hepatocyte cell models studying Phase II detoxification pathways.
No physiological or therapeutic properties are claimed; supplied for in-vitro laboratory research use only.
Compound identity
- CAS number: 70-18-8
- Molecular formula: C₁₀H₁₇N₃O₆S
- Molecular weight: 307.32 Da
- Sequence: γ-Glu-Cys-Gly
- Solubility: Soluble in water at ≥10 mg/mL
- Reconstitution: Dissolve in sterile water to required concentration; prepare fresh — oxidises progressively in aqueous solution
For in-vitro laboratory research use only. Not for human or veterinary use, consumption, or therapeutic application. No medical claims are made.