GLUTATHIONE 600MG

£40.00

L-Glutathione is a naturally occurring tripeptide developed for experimental investigation of cellular redox regulation, antioxidant defence mechanisms, and thiol-dependent biochemical signalling pathways.

Purity: Conforms to internal specification
CAS Number: 70-18-8
Compound Type: Naturally occurring tripeptide

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The products offered on this website are furnished for in-vitro studies only. In-vitro studies are performed outside of the body. These products are not medicines or drugs and have not been approved to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden.

Reconstitution

Use bacteriostatic water. Add solvent slowly along vial wall. Do not shake gently swirl.

Cold Chain

Store lyophilised at 2–8°C. Once reconstituted, keep at 2–8°C and use within 28 days.

Certificate of Analysis

CoA available on request for each batch. HPLC and MS data provided.

Description

Batch HPLC tested at 98.5%+ purity.
Store frozen long term or refrigerated when ready for use.
Sold for research purposes only.
Contact us for wholesale orders.

L-Glutathione

Synonyms / Designations: L-Glutathione, Reduced Glutathione, GSH, γ-L-Glutamyl-L-cysteinylglycine
CAS Number: 70-18-8
Molecular Formula: C₁₀H₁₇N₃O₆S
Molecular Weight: 307.32 g/mol
Chemical Classification: Naturally occurring tripeptide; intracellular antioxidant
Purity: Conforms to internal specification
Appearance: Clear liquid
Storage: Best stored frozen. Discard 30 days after opening.

Description & Mechanism

L-Glutathione is a naturally occurring tripeptide composed of glutamic acid, cysteine, and glycine. It is ubiquitously present in mammalian cells and plays a central role in redox balance, cellular detoxification processes, and maintenance of intracellular thiol status.

In biochemical and cellular research systems, L-Glutathione is widely used as a reference compound for studying oxidative stress, redox signalling, enzymatic detoxification pathways, and glutathione-dependent enzyme activity. Experimental investigations commonly focus on its interaction with glutathione peroxidases, glutathione S-transferases, and redox-sensitive signalling proteins. Observed effects are dependent on concentration, cellular context, and experimental design, and are used to investigate molecular mechanisms rather than defined physiological outcomes.

Applications in Research

Redox biology and oxidative stress studies.
Investigation of antioxidant defence mechanisms.
Enzymatic assays involving glutathione-dependent enzymes.
Cellular detoxification and thiol metabolism research.
Reference standard for antioxidant and redox-active compounds.

Handling & Stability

Best stored frozen. Discard 30 days after opening.

Precautions & Notes

L-Glutathione is readily oxidised to glutathione disulfide (GSSG).
Buffer composition and pH may influence stability and redox state.
Appropriate controls are recommended when studying redox-sensitive systems.
Intended strictly for laboratory research use; not for human or veterinary application.

References

Meister, A., & Anderson, M. E. Glutathione. Annual Review of Biochemistry, 1983.
https://doi.org/10.1146/annurev.bi.52.070183.002551
Forman, H. J., Zhang, H., & Rinna, A. Glutathione: overview of its protective roles, measurement, and biosynthesis. Molecular Aspects of Medicine, 2009.
https://doi.org/10.1016/j.mam.2008.08.006
Lu, S. C. Regulation of glutathione synthesis. Molecular Aspects of Medicine, 2009.
https://doi.org/10.1016/j.mam.2009.01.005
Jones, D. P. Redefining oxidative stress. Antioxidants & Redox Signaling, 2006.
https://doi.org/10.1089/ars.2006.8.1865