More about L-Glutathione (600mg)
L-Glutathione is a low-molecular-weight tripeptide composed of glutamate, cysteine, and glycine. Its cysteine residue contains a reactive thiol group that makes the compound relevant to controlled laboratory studies involving oxidation-reduction chemistry, conjugation reactions, thiol-dependent enzymes, and intracellular biochemical measurements.
In experimental systems, glutathione may be evaluated in its reduced form, GSH, and its oxidized disulfide form, GSSG. Researchers may measure these forms individually or as a ratio when characterizing redox conditions within a defined sample, cell system, or biochemical assay.
Glutathione is also examined as a substrate or cofactor-associated molecule in enzyme systems involving glutathione peroxidases, glutathione reductase, and glutathione S-transferases. These investigations may characterize reaction kinetics, substrate interactions, enzyme activity, and measurable biochemical changes under controlled experimental conditions.
L-Glutathione (600mg) – Research Specifications:
| Compound |
L-Glutathione |
| Quantity |
600mg per vial |
| Compound Type |
Tripeptide |
| Molecular Formula |
C10H17N3O6S |
| Molecular Weight |
307.32 g/mol |
| CAS Number |
70-18-8 |
| Sequence |
γ-L-Glutamyl-L-cysteinylglycine |
| Appearance |
Lyophilized powder |
| Purity / Identity |
Refer to the lot-specific Certificate of Analysis for reported analytical results |
| Storage Conditions |
Store sealed in a cool, dry environment protected from heat, light, and moisture |
| Research Use Only |
Supplied exclusively for controlled laboratory research. Not for human or animal consumption. |
What Is L-Glutathione? Research Background
L-Glutathione is an endogenous tripeptide identified across numerous biological systems. Its chemical structure includes a gamma-glutamyl linkage between glutamate and cysteine, followed by glycine. This structure distinguishes glutathione from peptides containing only conventional alpha-peptide linkages.
The thiol group within the cysteine component participates in reversible oxidation-reduction reactions. Two reduced glutathione molecules may form oxidized glutathione through a disulfide bond. This reversible relationship makes the GSH/GSSG system a frequently measured variable in laboratory redox experiments.
Controlled studies may also examine glutathione in relation to glutathione-dependent enzymes. Glutathione peroxidases, glutathione reductase, and glutathione S-transferases represent distinct enzyme families involved in reactions that use, transform, or regenerate glutathione. Experimental results depend on the selected assay, substrate, biological model, concentration, temperature, pH, and other controlled variables.
Glutathione research may intersect with analytical chemistry, enzymology, molecular biology, cellular metabolism, and toxicology. These research areas evaluate defined biochemical mechanisms without establishing diagnostic, therapeutic, veterinary, or consumer applications for the supplied material.
Important Research Notice: NordSci research materials are accompanied by lot-specific analytical documentation when available. Researchers should consult the applicable Certificate of Analysis to review the reported identity, purity, testing methods, and other specifications for the individual lot.
THIS PRODUCT IS INTENDED EXCLUSIVELY FOR LABORATORY RESEARCH USE. NOT FOR HUMAN OR ANIMAL CONSUMPTION. NOT FOR DIAGNOSTIC, THERAPEUTIC, VETERINARY, FOOD, DRUG, COSMETIC, OR DIETARY-SUPPLEMENT USE.
L-Glutathione – Key Research Applications
1. Oxidation-Reduction Research
Laboratory studies may use L-Glutathione to characterize oxidation-reduction reactions under controlled conditions. Researchers may measure GSH, GSSG, or the relationship between these forms as experimental variables within biochemical assays.
2. Enzyme-System Studies
L-Glutathione may be examined in experimental systems involving glutathione peroxidases, glutathione reductase, glutathione S-transferases, and other thiol-associated enzymes. Research may evaluate reaction kinetics, substrate dependence, enzyme activity, or measurable changes produced by controlled experimental conditions.
3. Thiol Chemistry Research
The cysteine thiol group makes glutathione relevant to studies of thiol-disulfide exchange, protein thiolation, conjugation reactions, and related chemical mechanisms. These investigations require controlled handling to limit unintended oxidation and sample variability.
4. Analytical Method Development
Researchers may use L-Glutathione when developing or validating laboratory methods involving chromatography, mass spectrometry, spectroscopy, electrochemical analysis, or other analytical platforms. Method parameters must be established for the specific instrument, sample matrix, and research objective.
Handling and Research Use Considerations
L-Glutathione (600mg) should be handled only by qualified personnel using established laboratory procedures for research chemicals. Appropriate personal protective equipment, environmental controls, documentation practices, and material-handling protocols should be selected according to the laboratory’s risk assessment.
Researchers should consult the product label, lot-specific Certificate of Analysis, and applicable Safety Data Sheet before beginning laboratory work. Experimental procedures should account for variables that may affect material stability or analytical results, including temperature, light exposure, atmospheric oxygen, moisture, pH, sample matrix, and storage duration.
Protocol Design Considerations: Glutathione-related measurements can be influenced by oxidation during collection, preparation, storage, and analysis. Laboratories should use validated controls and consistent sample-processing procedures when comparing experimental groups or analytical runs.
No dosing, administration, clinical-use, veterinary-use, or consumer-application guidance is provided for this material.
This information is provided solely as a technical reference for qualified laboratory personnel conducting controlled research.
L-Glutathione (600mg) – Certificate of Analysis (COA)
Lot-specific Certificates of Analysis provide the analytical information reported for individual NordSci production lots. Depending on the applicable testing protocol, documentation may include compound identity, purity, analytical method information, and additional lot-specific results.
Researchers should review the Certificate of Analysis associated with the exact lot received rather than relying on specifications reported for another batch.
Where to Buy L-Glutathione for Research
NordSci Peptides supplies L-Glutathione (600mg) for controlled laboratory research and analytical evaluation. Product documentation is organized to provide research laboratories with access to relevant compound specifications and lot-specific analytical information.
When sourcing research compounds, laboratories should evaluate material identity, analytical documentation, batch traceability, storage requirements, and compatibility with the intended experimental method.
IMPORTANT: L-Glutathione (600mg) is supplied exclusively for laboratory research use. It is not intended for human or animal consumption and is not offered for diagnostic, therapeutic, veterinary, food, drug, cosmetic, or dietary-supplement applications. Researchers are responsible for complying with all applicable institutional and regulatory requirements governing research materials.
Scientific References
-
Meister A, Anderson ME. Glutathione. Annual Review of Biochemistry. 1983;52:711–760.
-
Forman HJ, Zhang H, Rinna A. Glutathione: Overview of its protective roles, measurement, and biosynthesis. Molecular Aspects of Medicine. 2009;30(1–2):1–12.
-
Lu SC. Glutathione synthesis. Biochimica et Biophysica Acta. 2013;1830(5):3143–3153.
-
Aquilano K, Baldelli S, Ciriolo MR. Glutathione: New roles in redox signaling for an old antioxidant. Frontiers in Pharmacology. 2014;5:196.