Glutathione
Glutathione (GSH) is a naturally occurring tripeptide composed of glutamine, cysteine, and glycine.
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Glutathione (GSH) is a naturally occurring tripeptide composed of glutamine, cysteine, and glycine. It plays a central role in intracellular redox regulation and oxidative balance research within cellular systems.
As a key antioxidant molecule, glutathione is widely studied in laboratory environments for its involvement in:
- Cellular redox homeostasis
- Reactive oxygen species (ROS) regulation
- Enzyme-dependent detoxification pathways
- Mitochondrial signaling systems
- Oxidative stress research models
Reduced glutathione (GSH) serves as a primary intracellular antioxidant and is fundamental to biochemical studies involving cellular protection mechanisms and redox cycling frameworks.
Product Details:
– Form: Lyophilized reduced glutathione (GSH)
– Purity: ≥99% (analytically verified)
– Molecular Classification: Tripeptide antioxidant
– Certificate of Analysis (COA): Available upon request
– Intended Use: Laboratory research only
Glutathione functions as a central redox-active molecule within cellular systems.
Redox Cycling
Glutathione participates in redox reactions by donating electrons to neutralize reactive oxygen species, becoming oxidized to glutathione disulfide (GSSG) in the process. It is then recycled back to its reduced form via glutathione reductase in NADPH-dependent reactions.
This redox cycle is studied in:
- Oxidative stress modeling
- Mitochondrial function research
- Enzymatic detoxification pathway studies
Enzyme Interactions
Glutathione is involved in:
- Glutathione peroxidase systems
- Glutathione S-transferase pathways
- Cellular detoxification cascade research
Cellular Signaling
Research models investigate glutathione’s role in:
- Redox-sensitive transcription factor regulation
- Mitochondrial signaling pathways
- Intracellular antioxidant balance
- Protein thiol regulation studies
All research must comply with institutional and regulatory guidelines.
Glutathione is utilized in laboratory environments for:
- Oxidative stress pathway research
- Redox balance modeling
- Antioxidant system studies
- Mitochondrial function investigation
- Enzyme-mediated detoxification research
- Cellular signaling cascade analysis
Its widespread role in intracellular processes makes it a foundational compound in biochemical research systems.
Glutathione is composed of:
- Glutamate
- Cysteine
- Glycine
Its unique gamma-peptide bond between glutamate and cysteine contributes to its stability and biological activity in redox reactions.
Reduced glutathione (GSH) differs structurally from its oxidized form (GSSG), allowing dynamic cycling in cellular redox systems.
Each batch of Glutathione undergoes analytical verification including:
- High-Performance Liquid Chromatography (HPLC) purity testing
- Identity confirmation analysis
- Batch-level traceability documentation
- Controlled lyophilization processes
- Sterile sealed packaging
Certificates of Analysis are available upon request.
Glutathione is supplied as a sterile lyophilized powder.
Storage Guidelines:
- Store refrigerated at 2–8°C
- Protect from light exposure
- Minimize moisture contact
- Avoid repeated freeze-thaw cycles
- Follow appropriate laboratory handling protocols
The compound is supplied dry and is not pre-reconstituted.
This product is intended strictly for laboratory research purposes only.
It is not intended for human consumption, veterinary use, therapeutic application, cosmetic use, or diagnostic purposes.
By purchasing this product, the buyer affirms compliance with all applicable research regulations and governing laws.
Glutathione is a naturally occurring tripeptide involved in cellular redox regulation and antioxidant pathway research.
It is supplied as reduced glutathione (GSH) in sterile lyophilized powder form for laboratory research.
Yes. Glutathione is a tripeptide composed of glutamate, cysteine, and glycine.
No. This product is strictly intended for laboratory research use only.
Each batch is analytically verified to ≥99% purity. COA documentation is available upon request.
Store refrigerated at 2–8°C, protected from light and moisture, and handled according to laboratory protocols.
Combination research must comply with institutional and regulatory guidelines.
COA documentation may be requested by contacting support with your order details.
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