

Glutathione 1500 MG
In stock
Quantity discounts

Product Description
Glutathione
Product Overview
Glutathione is a naturally occurring tripeptide composed of three amino acids: glutamate, cysteine, and glycine. Present in most cells, it plays an important role in maintaining cellular redox balance and supporting the body's endogenous antioxidant defense systems. Its chemical structure enables it to participate in reactions that help regulate oxidative processes within biological systems.
Glutathione exists primarily in two forms: reduced glutathione (GSH), which can donate electrons during antioxidant reactions, and oxidized glutathione (GSSG), which forms when two glutathione molecules are linked through a disulfide bond. The balance between these forms is commonly studied as an indicator of cellular redox status.
Scientific research has examined glutathione's involvement in oxidative stress responses, cellular detoxification pathways, mitochondrial function, and the regulation of redox-sensitive proteins. Researchers also investigate its role in maintaining intracellular conditions that support normal cellular activity.
Glutathione is of scientific interest in biochemical, cellular, and metabolic research exploring antioxidant mechanisms and the relationship between redox regulation and cellular function. Research findings depend on the formulation, route of exposure, and experimental context, and should not be interpreted as establishing the efficacy of every glutathione product or formulation.
Key Research Areas
Cellular antioxidant defense and redox balance
Oxidative stress and reactive oxygen species research
Glutathione metabolism and GSH/GSSG redox signaling
Cellular detoxification and conjugation pathways
Mitochondrial function and cellular metabolic processes
Peptide composition, stability, and analytical characterization
Handling & Reconstitution
For laboratory use, reconstitute with Bacteriostatic Water (BAC) or sterile saline. After reconstitution, the solution should be stored at 2–8°C (36–46°F) and used within the appropriate experimental window to maintain peptide stability.
Additional information
| Size |
|---|

