Longevity & Cellular Renewal
Glutathione
Reduced L-glutathione
Reduced L-Glutathione (GSH)
Research context
Glutathione is a tripeptide with an unusual gamma peptide bond conferring resistance to standard peptidases. Research applications include redox buffering in cell culture, measurement of GSH/GSSG ratio as an oxidative stress indicator, and enzyme kinetics with glutathione-dependent enzymes.
Common assays: GSH/GSSG ratio · Thiol quantification (DTNB) · Glutathione peroxidase kinetics
Specification
| Designation | Reduced L-glutathione |
|---|---|
| Full name | Reduced L-Glutathione (GSH) |
| Sequence | γ-Glu-Cys-Gly |
| CAS number | 70-18-8 |
| Molecular formula | C10H17N3O6S |
| Molecular weight | 307.32 g/mol |
| Formats | 10 mL Vial |
| Solubility | Water (highly soluble) |
| Storage | Sealed, 2–8 °C, protected from light and air |
Published literature
Selected peer-reviewed references describing research involving this compound. Listed for reference only; inclusion is not a claim about any outcome.
- Meister A, Anderson ME.GlutathioneAnnual Review of Biochemistry · 1983 Find on PubMed ↗
Common questions
Why does reduced glutathione require protection from air?
The free thiol oxidises readily to the disulfide dimer GSSG. Oxidation state is what distinguishes reduced from oxidised glutathione, so exposure changes what you are actually working with.
What is the significance of the gamma peptide bond?
The bond between glutamate and cysteine forms at the gamma carboxyl rather than the alpha, making glutathione resistant to most peptidases and accounting for its intracellular stability.
Same pathway
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