Redox Homeostasis
Research frequently examines glutathione as part of the cellular systems that maintain oxidation-reduction balance and respond to oxidative stress.
For laboratory research use only. Not for human consumption.
Free U.S. shipping on $200+GLPZone / The research collection

Nordicstar Analytical Sciences
Glutathione 600 MG
Metabolic Research
Thiol chemistry & cellular redox systems
A pair saves 10%. A set of three saves 15%.
For laboratory research use only.
Not for human consumption or clinical use.
The records shown here are illustrative. Request laboratory-issued documentation for your lot before ordering.
Priority, tracked shipping within the United States, free on orders of $200 or more after savings. Add Priority dispatch at checkout to have your order packed first; Private Clients receive it on every order. Follow the product documentation for laboratory handling requirements.
Shipping information01 / The compound
Thiol chemistry & cellular redox systems
Glutathione is a tripeptide composed of glutamate, cysteine, and glycine. In redox research, its reduced form is commonly abbreviated GSH.
Its structure includes an unusual gamma-glutamyl linkage between glutamate and cysteine. The cysteine residue also contains a reactive thiol group, making glutathione important in research involving cellular redox chemistry, oxidative-stress models, and thiol-dependent biochemical processes.
02 / Research profile
Glutathione is widely investigated as part of cellular redox systems. Research commonly examines the relationship between its chemical structure, thiol reactivity, reduced and oxidized forms, and redox-sensitive cellular processes.
Research frequently examines glutathione as part of the cellular systems that maintain oxidation-reduction balance and respond to oxidative stress.
Reduced glutathione is represented as GSH. Upon oxidation, glutathione can form the disulfide GSSG. The relationship between GSH and GSSG is widely studied in cellular redox biology.
The cysteine residue in glutathione contains a reactive thiol group that participates in redox reactions and other thiol-dependent biochemical processes.
Glutathione is also studied in reversible S-glutathionylation, a redox-sensitive protein modification involved in the regulation of protein function and cellular signaling. Published findings describe the biochemical and biological properties of glutathione and do not constitute claims about the performance or intended use of GLPZone material.
Reading the evidence
The cited findings describe the compound in the experimental systems used. Cellular, biochemical and animal results should be interpreted according to their model, methods and endpoints; they do not establish the performance of a GLPZone lot.
03 / Reference data
Reference specifications describe a compound. The final lot documentation identifies the material supplied.
| Compound | Glutathione |
|---|---|
| Research area | Metabolic Research |
| CAS number | 70-18-8 |
| Molecular formula | C10H17N3O6S |
| Molecular weight | 307.32 g/mol |
| Physical form | Lyophilized |
| Vial options | 600 MG |
| Intended use | Laboratory research only |
Variant amounts are nominal catalog quantities. They are not instructions for use.
HPLC separates components under a defined method. Read the reported percentage alongside the chromatogram, wavelength, integration method, and scope of the test.
Mass spectrometry provides molecular-mass evidence. Identity and chromatographic purity answer different questions; one cannot stand in for the other.
Connect the product name, variant, lot identifier, report date, and issuing laboratory. A report is useful only when its sample can be linked to the material being reviewed.
Every Glutathione lot is analyzed by Nordicstar Analytical Sciences for identity, content, and purity by HPLC with LC-MS confirmation. Each certificate carries a report number and verification key that can be checked at nordicstarlabs.com/verify. Research references below describe published science, not a certificate for a vial.
Read a COA with confidence| Presentation | Lot | HPLC purity | Tested | Certificate |
|---|---|---|---|---|
| 600 MG Current lot | GLZ-26-GSH-1034 | 99.759% | 22 Sep 2026 | NS-2026-06035 |
| 600 MG | GLZ-26-GSH-766 | 99.636% | 18 Aug 2026 | NS-2026-06141 |
| 600 MG | GLZ-26-GSH-666 | 99.743% | 11 Jul 2026 | NS-2026-06142 |
05 / Storage & handling
Store unopened Glutathione research material according to the product's specified storage conditions.
Reduced glutathione in aqueous solution is susceptible to oxidation to GSSG when exposed to air, so redox state and solution stability should be considered in laboratory workflows.
Explore the handling guide06 / Common questions
Yes. Glutathione is a tripeptide composed of three amino acids: glutamate, cysteine, and glycine. It contains an unusual gamma-glutamyl linkage between glutamate and cysteine.
GSH is the abbreviation commonly used for reduced glutathione in scientific literature. Its oxidized disulfide form is known as GSSG, and the relationship between these forms is widely studied in cellular redox research.
Glutathione contains three amino-acid residues: glutamate, cysteine, and glycine.
07 / Further reading
Selected literature for context. Read each study’s methods, experimental model, and limitations alongside its findings.
Curated pairings