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Glutathione, 600mg
Glutathione (GSH) is a tripeptide thiol composed of glutamate, cysteine, and glycine, and is among the most extensively studied low-molecular-weight redox-active molecules in biological systems.
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Spedizione
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Vedi i risultati di laboratorio →Glutathione (GSH) is a tripeptide thiol composed of glutamate, cysteine, and glycine, and is among the most extensively studied low-molecular-weight redox-active molecules in biological systems. Through its reactive sulfhydryl group, GSH participates in oxidation-reduction reactions, thiol-disulfide exchange processes, and cofactor-dependent enzymatic mechanisms.
It serves as an obligate co-substrate for multiple enzyme families, including glutathione peroxidases (GPx), glutathione S-transferases (GST), and glutaredoxins, where it contributes to redox-regulated biochemical pathways and enzyme-mediated signaling processes.
Experimental investigations have extensively utilized GSH for studies of redox biology, thiol chemistry, enzyme-cofactor interactions, glutathione-dependent regulatory networks, and signal transduction mechanisms involving sulfur-containing biomolecules. Research applications include glutathione system characterization, GPx and GST pathway investigation, glutaredoxin-associated signaling studies, redox system analysis, and mechanistic evaluation of thiol-dependent biochemical processes.
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- Independently Lab Tested
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- For Laboratory Research Use Only
3D Molecular Structure
Drag to rotate · scroll to zoom| Chemical Formula | C10H17N3O6S |
|---|---|
| Synonyms | 0-18-8, L-Glutathione, Glutathion, Isethion, L-gamma-glutamyl-L-cysteinylglycine |
| Molar Mass | 307.33 g/mol |
| CAS Number | 70-18-8 |
| PubChem CID | 124886 |
| Total Compound Content | 600 mg per vial |
| Shelf Life | 24 months |
Glutathione (γ-L-Glutamyl-L-cysteinylglycine) is a tripeptide synthesized from glutamate, cysteine, and glycine through a two-enzyme biosynthetic pathway involving γ-glutamylcysteine synthetase and glutathione synthetase. The molecule contains a reactive thiol group that participates in oxidation-reduction reactions, thiol-disulfide exchange processes, and redox-regulated biochemical mechanisms. Reduced glutathione (GSH) and oxidized glutathione (GSSG) form a dynamic redox couple maintained through glutathione reductase-dependent recycling systems.
GSH serves multiple biochemical functions, including acting as a co-substrate for glutathione peroxidases (GPx), glutathione S-transferases (GST), and glutaredoxin-associated enzyme systems. These interactions place glutathione at the center of numerous redox-regulated signaling networks, enzyme-cofactor relationships, and thiol-dependent regulatory pathways. Research applications include glutathione system characterization, GPx and GST pathway investigation, glutaredoxin-associated signaling studies, redox biology research, and mechanistic evaluation of thiol-dependent biochemical processes. Supplied as a lyophilized preparation. Independently third-party HPLC-tested; COA available per batch.
Results refer to the tested sample. Check the batch and date in the report.
What distinguishes glutathione from glutathione precursor compounds in biochemical research?
Glutathione (GSH) is the fully assembled tripeptide consisting of glutamate, cysteine, and glycine, whereas precursor compounds participate in upstream glutathione biosynthetic pathways. As the completed molecule, GSH serves directly as a substrate and cofactor for multiple glutathione-dependent enzyme systems, making it a valuable research tool for investigating redox chemistry, thiol-disulfide exchange processes, enzyme-cofactor interactions, and glutathione-associated regulatory mechanisms.
What is the relationship between glutathione and the Nrf2/ARE signaling pathway?
The Nrf2/ARE pathway is a well-characterized transcriptional regulatory system associated with glutathione-related biochemical processes. Experimental investigations have examined interactions between glutathione-dependent redox systems, Nrf2-associated signaling mechanisms, and the regulation of enzymes involved in glutathione biosynthesis and utilization.
These relationships make glutathione a useful research tool for studies of redox-regulated signaling networks, transcriptional regulation, and thiol-dependent biochemical pathways.
How is glutathione commonly analyzed in laboratory research?
Glutathione is frequently characterized using analytical techniques including high-performance liquid chromatography (HPLC), liquid chromatography-mass spectrometry (LC-MS), fluorescence-based derivatization methods, and colorimetric thiol assays.
These approaches enable investigation of GSH/GSSG redox systems, glutathione-associated enzyme activity, thiol chemistry, and redox-regulated biochemical processes. Such analytical methods have established glutathione as a widely utilized molecule in studies of redox biology, enzyme kinetics, and cofactor-dependent signaling mechanisms.
Customer Reviews (7)
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Excellent service, postage to Australia takes around 3-4 weeks. Responsive customer service.
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Worked awesome! Love it. Ordering again!
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Exceptional service on the super fast shipping, purity is outstanding. A trustworthy supplier. Our research results have been outstanding.
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Great quality on the ordering process and the chemical quality is top notch. Our research results have been outstanding. Highly recommend this vendor.
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The experimental results were exceptional. Cannot recommend enough the support team and the compound is pure and high quality. Reordering next week.
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So happy with how fast it shipped. the quality is absolutely top-tier. Will buy again. The experimental results were exceptional.
