Research chemical sequence
Glutathione
Glutathione is listed as a research-use-only chemical sequence. Research use only. Not for human or veterinary use. Public catalog information is limited to chemical identity, analytical documentation, and external reference records.
Research-use boundary: Research use only. Not for human or veterinary use. Public catalog information is limited to chemical identity, analytical documentation, and external reference records.
Public identity
- Publication state
- published
- Reviewed designation
- Reduced Glutathione (L-γ-Glutamyl-L-cysteinylglycine / GSH)
- Designation kind
- registered
- Entity kind
- modified sequence
- Exact form
- Endogenous antioxidant tripeptide with isopeptide gamma-glutamyl linkage
- Sequence notation (three letter)
- γ-Glu-Cys-Gly
- Structure (other)
- CAS: 70-18-8 | GSH
- Sequence
- γ-Glu-Cys-Gly
Available variants
| Size | SKU | Price (USD) | Availability | Representative purity |
|---|---|---|---|---|
| 1500mg | DFP-031 | $0.00 | Out of stock | 99.0% |
Analytical boundary
Representative catalog purity: 99.0%
No active-batch certificate of analysis is currently published.
Purity figures shown here are representative catalog specifications, not lot-specific measurements.
Evidence inventory
- Record state
- reviewed records
- Public records
- 407
- Reviewed summaries
- 26
- Verified citations
- 0
- Human study: 100
- In vivo: 112
- In vitro: 189
- Special category: 0
- Unclassified: 6
These counts describe linked records and review status. They do not establish efficacy, safety, or fitness for any use.
Technical record
- Molecular weight
- 307.32 Da
- Sequence class
- small molecule
- Appearance
- White lyophilized powder
- Solubility
- Soluble in sterile water; highly susceptible to oxidation in solution
- Mechanism record
- Glutathione (γ-Glu-Cys-Gly) is the body's primary endogenous antioxidant 3-residue chemical sequence, maintaining cellular redox homeostasis via the GSH/GSSG ratio. It serves as substrate for glutathione peroxidase (GPx) in peroxide neutralization, glutathione S-transferase (GST) in xenobiotic conjugation, and activates the Nrf2 antioxidant response element. The unusual γ-chemical sequence bond between glutamate and cysteine confers resistance to most peptidases.
- Half-life record
- ~10 minutes (IV, plasma); intracellular GSH pool longer
Recorded receptors
- GPx enzymatic
- GST detoxification
- Nrf2 antioxidant
External literature records
- External literature record
- External literature record
Limitations and research boundary
Research use only. Not for human or veterinary use. Public catalog information is limited to chemical identity, analytical documentation, and external reference records.
External records are attributed references. Their presence does not convert a source-reported observation into a product claim.