
Glutathione
A gamma-glutamyl-cysteinyl-glycine tripeptide that constitutes the principal low-molecular-weight thiol buffer of the cell.
- Purity
- 99.2%
- Lot
- PU-2CC1
- CAS
- 70-18-8
- MW
- 307.32 g/mol
- Format
- Lyophilized powder
- Third-party tested
- Discreet packaging
- Same-day shipping
- Encrypted checkout
For research use only. Not for human consumption.
Mechanism of Action
Glutathione is the tripeptide gamma-L-glutamyl-L-cysteinyl-glycine and the dominant low-molecular-weight thiol in most cells. The unusual gamma-linkage protects it from ordinary aminopeptidases, which is why it persists in the cytosol at millimolar concentration.
Its function is to buffer the cellular redox environment: the ratio of reduced glutathione to its oxidised disulfide is a standard index of redox state. Compartment-specific pools - mitochondrial, nuclear and peroxisomal - are maintained separately, and reviews in Redox Biology and Biochimica et Biophysica Acta treat those compartments as distinct systems.
Research Findings
The indexed literature is foundational biochemistry rather than product literature: oxidative stress reviewed in the Annual Review of Biochemistry, redox regulation of immune responses in Cellular and Molecular Immunology, and glutathione metabolism in ferroptosis in Cancer Letters.
Applied work has examined the redox contribution to Parkinson's disease models and strategies in glucose-6-phosphate dehydrogenase deficiency, where NADPH supply for glutathione recycling is the limiting factor.
Storage & Reconstitution
Sealed lyophilized vials are stored in the dark. The peptide-formulation literature regards the dry solid as the stable state and the solution as the fragile one: refrigeration at 2-8 degrees C is standard for short holding periods, and minus 20 degrees C or colder for long-term storage. Vials are brought to room temperature before opening so that atmospheric moisture does not condense onto the cold solid. Reduced glutathione oxidises readily on exposure to air and to trace metals; solutions are prepared fresh and the dry solid is kept sealed and cold.
For reconstitution, the diluent is added slowly down the inner wall of the vial rather than directly onto the cake, and the vial is swirled rather than shaken - agitation at an air-liquid interface is a well-documented driver of peptide aggregation. The solid should dissolve to a clear, particle-free solution; persistent cloudiness or visible particulate indicates the material should not be used.
Reconstituted solution is held at 2-8 degrees C and protected from light. Freeze-thaw cycling is the single most avoidable cause of loss, so where a solution must be frozen it is aliquoted first into single-use volumes. Working aliquots are labelled with the lot number so that any result can be traced back to the certificate of analysis for that lot.
- Physical form
- Lyophilized powder, sealed vial
- Sealed storage
- 2-8 C short term / -20 C long term
- Reconstituted
- 2-8 C, protected from light
- Diluent
- Bacteriostatic water, added down the vial wall
- Avoid
- Shaking, freeze-thaw cycling, direct light
Handling summary
References
Every entry below links to its PubMed record. Publication is not endorsement: several of these papers report limitations, negative findings or adverse events, and they are listed for that reason.
- [1]Oxidative Stress(opens PubMed in a new tab)
Annu Rev Biochem · 2017 · PMID 28441057
- [2]Mitochondrial Glutathione in Cellular Redox Homeostasis and Disease Manifestation(opens PubMed in a new tab)
Int J Mol Sci · 2024 · PMID 38279310
- [3]Redox regulation of the immune response(opens PubMed in a new tab)
Cell Mol Immunol · 2022 · PMID 36056148
- [4]The role of oxidative stress in Parkinson's disease(opens PubMed in a new tab)
J Parkinsons Dis · 2013 · PMID 24252804
- [5]Glutathione metabolism in ferroptosis and cancer therapy(opens PubMed in a new tab)
Cancer Lett · 2025 · PMID 40189013
- [6]An Update on Glutathione's Biosynthesis, Metabolism, Functions, and Medicinal Purposes(opens PubMed in a new tab)
Curr Med Chem · 2024 · PMID 37921175