Glutathione 1500mg
Glutathione is a naturally occurring tripeptide composed of glutamate, cysteine, and glycine that is widely studied in biochemical research for its role in cellular redox regulation, antioxidant defense, and metabolic detoxification pathways. In experimental systems, glutathione participates in maintaining intracellular redox balance and protecting cellular components from oxidative stress through interactions with reactive oxygen species and enzymatic antioxidant networks.
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What Is Glutathione?
Glutathione is an endogenous tripeptide present in most mammalian cells and is widely studied in biochemical and physiological research for its role in cellular antioxidant systems and redox homeostasis. Structurally composed of glutamate, cysteine, and glycine, glutathione functions as a key intracellular molecule involved in maintaining cellular oxidative balance and supporting metabolic detoxification pathways.
In laboratory research, glutathione is frequently examined as a regulator of oxidative stress signaling, mitochondrial function, and cellular detoxification mechanisms. Through its thiol (-SH) functional group, glutathione participates in redox reactions that neutralize reactive oxygen species and maintain intracellular redox equilibrium.
Across experimental models, glutathione has been associated with changes in endpoints commonly measured in oxidative stress research, including reactive oxygen species (ROS) activity, antioxidant enzyme signaling, and mitochondrial redox balance. These observations are interpreted mechanistically through biochemical pathway interactions rather than as claims of applied use.
Glutathione Structure
Peptide Class: Tripeptide antioxidant
Amino Acid Sequence: γ-L-glutamyl-L-cysteinyl-glycine
Molecular Formula: C10H17N3O6S
Molecular Weight: 307.32 g/mol
CAS Number: 70-18-8
Synonyms: reduced glutathione, GSH
Glutathione contains a unique γ-peptide bond linking glutamate and cysteine, which contributes to its stability and biological function. The cysteine thiol group enables glutathione to participate in redox reactions and serve as a substrate for antioxidant enzymes such as glutathione peroxidase and glutathione reductase.
In biochemical systems, glutathione exists in two primary forms:
- Reduced glutathione (GSH)
- Oxidized glutathione (GSSG)
The ratio of these forms is often used as an indicator of cellular oxidative stress and redox balance in laboratory studies.
Glutathione Research
Glutathione is widely used in laboratory investigations examining oxidative stress pathways, cellular detoxification systems, and mitochondrial redox regulation. Experimental studies frequently employ glutathione in assays designed to evaluate cellular responses to reactive oxygen species and oxidative damage.
Common research endpoints include:
- intracellular redox balance
- antioxidant enzyme activity
- mitochondrial oxidative stress markers
- cellular detoxification pathways
- reactive oxygen species signaling
In experimental models, glutathione is also investigated in relation to protein oxidation, lipid peroxidation, and metabolic stress responses, allowing researchers to explore the role of cellular antioxidant systems in maintaining physiological homeostasis.
Referenced Citations
[1] Lu SC.
Glutathione synthesis.
https://pubmed.ncbi.nlm.nih.gov/20001662/[2] Pizzorno J.
Glutathione: systemic protectant against oxidative and free radical damage.
https://pubmed.ncbi.nlm.nih.gov/24067339/[3] Townsend DM, Tew KD, Tapiero H.
The importance of glutathione in human disease.
https://pubmed.ncbi.nlm.nih.gov/18058139/[4] Wu G, Fang YZ, Yang S, Lupton JR, Turner ND.
Glutathione metabolism and its implications for health.
https://pubmed.ncbi.nlm.nih.gov/15691726/[5] PubChem.
Glutathione compound summary.
https://pubchem.ncbi.nlm.nih.gov/compound/Glutathione
Storage Instructions:
All of our products are manufactured using the Lyophilization (Freeze Drying) process, which ensures that our products remain 100% stable for shipping for up to 3-4 months.
Once the peptides are reconstituted (mixed with bacteriostatic water), they must be stored in the fridge to maintain stability. After reconstitution, the peptides will remain stable for up to 30 days.
Lyophilization is a unique dehydration process, also known as cryodesiccation, where the peptides are frozen and then subjected to low pressure. This causes the water in the peptide vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure known as lyophilized peptide. The puffy white powder can be stored at room temperature until you’re ready to reconstitute it with bacteriostatic water.
Once peptides have been received, it is imperative that they are kept cold and away from light. If the peptides will be used immediately, or in the next several days, weeks or months, short-term refrigeration under 4C (39F) is generally acceptable. Lyophilized peptides are usually stable at room temperatures for several weeks or more, so if they will be utilized within weeks or months such storage is typically adequate.
However, for longer term storage (several months to years) it is more preferable to store peptides in a freezer at -80C (-112F). When storing peptides for months or even years, freezing is optimal in order to preserve the peptide’s stability.
For further information on proper storage techniques, click the link below:
Peptide Storage