Lyophilized powderGlutathione
Glutathione (reduced, GSH)
Glutathione is a tripeptide with an unusual γ-peptide bond between glutamate and cysteine, which confers resistance to standard peptidase cleavage. Its free thiol group makes it the dominant intracellular redox buffer, and the GSH/GSSG ratio is a standard readout of cellular oxidative state. It is also an obligate cofactor for glutathione peroxidases and S-transferases.
Research applications
- GSH/GSSG ratio measurement as an oxidative stress readout
- Glutathione peroxidase and S-transferase activity assays
- Xenobiotic conjugation and detoxification pathway studies
- Ferroptosis research (GPX4 dependence on GSH)
Storage
Store lyophilized at -20°C protected from light. The free thiol oxidizes readily — minimize air exposure and prepare solutions fresh.
Reconstitution
Reconstitute with bacteriostatic water. Oxidation to GSSG begins on exposure to air; use promptly for redox-sensitive work.
Published literature
204,553 papers indexed on PubMed for Glutathione. Showing 6, reviews first.
- 01Glutathione
Meister A, Anderson ME · Annu Rev Biochem · 1983
- 02Efficient production of l-glutathione by whole-cell catalysis with ATP regeneration from adenosine
Zuo S et al. · Biotechnol Bioeng · 2024
- 03The effect of reduced L-glutathione supplementation on TNF-α, hs-CRP, and neutrophil-lymphocyte ratio in maintenance hemodialysis patients
Supriyadi R et al. · Eur Rev Med Pharmacol Sci · 2024
- 04
- 05L-glutathione 1% promotes neuroprotection of nitrergic neurons and reduces the oxidative stress in the jejunum of rats with Walker-256-bearing tumor
de Oliveira AP et al. · Neurogastroenterol Motil · 2023
- 06
Indexed from PubMed, 2026-07-19. We link to sources rather than reproducing them.
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