Glutathione
Glutathione, reduced (GSH; gamma-glutamyl-cysteinyl-glycine tripeptide) · ≥98% (HPLC)
Glutathione (reduced, GSH) is a characterized tripeptide-thiol reference material supplied for in-vitro studies of cellular redox-buffering pathways. Research Use Only.
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Research profile & documentation
- Why researchers study it
- Studied as a central cellular redox-buffering tripeptide and enzyme cofactor, used as a reference standard in oxidative-stress and antioxidant-pathway research.
- Mechanism themes in research
- Substrate for glutathione peroxidase (GPx) enzyme systemsCofactor for glutathione-S-transferase (GST) conjugation reactionsReduced/oxidized (GSH/GSSG) redox-couple biochemistryNon-standard γ-glutamyl N-terminal linkage chemistry
- What the evidence does not establish
- Published references are in-vitro or pre-clinical and describe research context only. They do not establish safety, efficacy, or any outcome in humans or animals, and Get Peptides makes no such claims.
- Quality markers
- ≥98% (HPLC)MS identityLot COACold-chain
- What ships
- The sealed lot-controlled vial, a measured ampoule of bacteriostatic water, and a printed handling & reconstitution card — plus the per-lot COA. Everything to prepare it, in one box.
Reduced glutathione (GSH) is a well-characterized tripeptide-thiol reference material used in redox biochemistry, enzyme assays, oxidative-stress models, and GSH/GSSG measurement. This page explains the molecule’s research role and analytical context without making therapeutic claims.
Molecular identity
Reduced glutathione is a γ-glutamyl-cysteinyl-glycine tripeptide with a reactive cysteine thiol. It is commonly identified as GSH and is distinct from oxidized glutathione (GSSG), in which two GSH molecules form a disulfide. Researchers should specify the redox form, salt or counter-ion, purity method, and storage history when comparing standards or interpreting measurements.
Redox-buffering research
GSH participates in the cellular redox couple GSH/GSSG and is a substrate for glutathione peroxidase and glutathione-S-transferase systems. In cell-free work it can be used to test enzyme kinetics, peroxide reduction, thiol-disulfide exchange, and conjugation reactions. In cultured-cell studies, GSH measurements require careful control of extraction, oxidation during handling, normalization, and assay specificity.
| Full name | Glutathione, reduced (GSH; gamma-glutamyl-cysteinyl-glycine tripeptide) |
| Research theme | Mitochondrial & energy |
| CAS number | 70-18-8 |
| Molecular formula | C₁₀H₁₇N₃O₆S |
| Molecular weight | 307.32 g/mol |
| Purity | ≥98% (HPLC) |
| Physical form | Lyophilized powder |
| Storage | −20 °C, desiccated, protected from light |
Sequence
Reported research areas
- Cellular redox-buffering and oxidative-stress pathway research
- Substrate/cofactor studies for glutathione peroxidase and glutathione-S-transferase systems
- Non-standard γ-glutamyl linkage chemistry
- Analytical reference standard for identity and purity (HPLC/MS)
Credible sources
- PubChem — Glutathione
- PubMed — glutathione redox biochemistry
- PubMed — glutathione peroxidase and GST assays
COA with every lot
Each Glutathione lot is characterized by reversed-phase HPLC for purity and by mass spectrometry for identity, then documented in a per-lot Certificate of Analysis. Unique lot numbers tie the vial back to its synthesis batch and analytical data.
- RP-HPLC purity result (≥98% (HPLC))
- Mass-spectrometry identity confirmation
- Appearance, molecular weight, and storage
- Lot number and testing status
Specimen Certificate of Analysis
| Product | Glutathione (reference) |
| Lot | HXR-2406-119 |
| Purity (RP-HPLC) | 98%+ |
| Identity (MS) | Confirmed · 307.32 g/mol |
| Appearance | Lyophilized powder |
| Storage | −20 °C, desiccated |
Representative document. Each lot has its own COA — these are quality documents, not medical claims.
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