Reference entry · Endogenous tripeptide antioxidant
Glutathione
Also known as: GSH · γ-L-glutamyl-L-cysteinylglycine · reduced glutathione
- Class
- Endogenous tripeptide antioxidant
- Size
- 3 amino acids
- Primary targets (literature)
- Glutathione peroxidase/reductase systems; redox homeostasis
- Regulatory context
- Dietary supplement and research material in various jurisdictions — not an FDA-approved injectable drug. Form and stability documentation are critical.
Overview
Glutathione is the central intracellular tripeptide antioxidant studied across redox biology, detoxification, and aging research. Catalog supply includes reduced (GSH) and oxidized (GSSG) forms requiring explicit specification.
Mechanism in research literature
GSH participates in enzymatic detoxification, protein glutathionylation, and maintenance of cellular redox balance — foundational biochemistry rather than receptor pharmacology.
Common research focus areas
- Redox and oxidative-stress research models
- Reduced vs. oxidized form stability
- Tripeptide identity and purity analytics
- Comparison with copper-peptide antioxidant literature
Full literature roundup
Read the cited research summary
The central intracellular tripeptide antioxidant. Redox biology, aging research literature, and how to evaluate reduced versus oxidized catalog forms.
Glutathione research roundup · 7 minEvaluate catalog material
- COA literacy — read batch documentation before comparing vendors.
- Peptide identity testing — why sequence confirmation matters beyond purity %.
- How we vet sources — our score methodology for recommended vendors.