
01The PureChain Standard
Purity And Documentation
Your results are only as good as the compound you start with.
Every vial is labelled with its compound, vial size and molecular weight, and ships for laboratory research use only. Third-party testing details will be published here.
Supplied for in-vitro laboratory research only. Not for human or veterinary use, and not intended to diagnose, treat, cure or prevent any disease.
- Size
- 1500mg
- Form
- Lyophilized powder
- Storage
- −20 °C, protected from light
- Molar mass
- 307.33 Da
About This Compound
About Glutathione
Glutathione is a tripeptide of glutamate, cysteine and glycine and one of the most studied small molecules in cell biology. Its defining structural feature is the gamma peptide bond: glutamate is joined through its side-chain carboxyl rather than its alpha carbon, which is why ordinary peptidases do not cleave it and why its turnover runs through a dedicated enzymatic cycle. The reactive group is the cysteine thiol, and the ratio between reduced glutathione (GSH) and its oxidised disulfide dimer (GSSG) is the measurement most often used as a readout of a cell’s redox state. PureChain Labs supplies glutathione as a lyophilised powder for in-vitro laboratory research only.
Endogenous Thiol Tripeptide
Molecular Formula
Molecular Weight
Form
CAS Number
02Molecular Structure
The Glutathione molecule
An illustrative atomic representation generated from the compound record, alongside its verified molecular data. The structure figure is schematic – not a measured conformation.
- C
- H
- N
- O
- S/P
Molecular data from the public PubChem record (CID 124886). View on PubChem
By The Numbers
Glutathione Research, By The Numbers
The figures that define Glutathione and how it is being studied. For laboratory research use only.
Amino Acids
Glutamate, cysteine and glycine, joined by a gamma peptide bond
Redox Couple Studied
The reduced-to-oxidised ratio is the standard redox readout
Molecular Weight (g/mol)
C10H17N3O6S, PubChem CID 124886
Research Areas
- Redox Biology
- Thiol Chemistry
- Phase II Conjugation Studies
- Oxidative Stress Models
How It Works
How Glutathione Works
The pathways Glutathione acts on, and what each one does. Described from preclinical and receptor-pharmacology literature.
Resistance To Peptidases
The glutamate is linked through its side-chain carboxyl, not the alpha carbon. Standard peptidases cannot cleave that bond, so glutathione is turned over by a dedicated route rather than by general proteolysis - the structural fact behind most of its handling in experimental systems.
- Glutamate linked via its side-chain carboxyl
- Not a substrate for standard peptidases
- Turned over by a dedicated enzymatic route
GSH To GSSG And Back
The cysteine thiol is the reactive centre. Oxidation couples two molecules into the GSSG disulfide; glutathione reductase returns them using NADPH. Research uses the ratio between the two forms as a quantitative measure of redox state in a preparation.
- Cysteine thiol is the reactive centre
- GSSG is the disulfide dimer
- Glutathione reductase regenerates GSH using NADPH
Glutathione S-Transferase Substrates
Glutathione S-transferases attach the thiol to electrophilic compounds, forming conjugates. This is a core assay system in in-vitro metabolism and toxicology research, where glutathione is the substrate rather than the subject.
- Glutathione S-transferases form the conjugates
- A core in-vitro metabolism assay system
- Glutathione is the substrate here
Uses And Applications
What Glutathione Is Researched For
The main areas Glutathione is studied in, and the qualitative magnitudes reported alongside them.
Redox Biology
The primary research use. The GSH/GSSG ratio is a standard quantitative readout of redox state in cells and tissue preparations.
Thiol Chemistry
Used as a reference thiol in disulfide exchange and free-thiol quantification assays.
Conjugation And Metabolism Assays
The substrate in glutathione S-transferase assay systems used in in-vitro metabolism work.
Oxidative Stress Models
Depletion and repletion of glutathione is a common experimental manipulation in cell models of oxidative stress.
Compound Information
Full Specification
| Chemical Name | Glutathione (GSH) |
|---|---|
| Sequence | gamma-Glu-Cys-Gly |
| Molecular Weight | 307.33 Da |
| Molecular Formula | C10H17N3O6S |
| CAS Number | 70-18-8 |
| Form | Lyophilized powder |
| Solubility | Water-soluble |
| Storage | Store lyophilized at −20 °C, protected from light and moisture |
| Vial Size | 1500mg |
| PubChem CID | 124886 |
FAQ
Common Questions About Glutathione
What Is Glutathione?
Glutathione is a tripeptide of glutamate, cysteine and glycine. PubChem lists it under CID 124886 with the formula C10H17N3O6S and a molecular weight of 307.33 g/mol. Its CAS number is 70-18-8.
What Is The Gamma Peptide Bond?
Glutamate is joined to cysteine through its side-chain carboxyl group rather than its alpha carboxyl. That linkage is called a gamma bond, and it is why ordinary peptidases do not cleave glutathione.
What Is The Difference Between GSH And GSSG?
GSH is the reduced form, with a free cysteine thiol. GSSG is the oxidised dimer, two molecules joined by a disulfide bond. The ratio between them is the measurement most often reported in redox research.
Why Is Glutathione Used In Metabolism Assays?
Glutathione S-transferases conjugate the thiol to electrophilic compounds. Those assays are a standard in-vitro tool, and glutathione is supplied as the substrate for them.
Is Glutathione Approved For Human Use?
No. Nothing supplied by PureChain Labs is approved for human use or sold for it. This material is supplied as a research chemical for in-vitro laboratory work only.
How Should Research-Grade Glutathione Be Stored?
As supplied it is a lyophilised powder; the vial directs storage in a cool, dry place in the lyophilised state, and refrigeration once reconstituted.
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Not for human or veterinary use. For in-vitro laboratory research only. These statements have not been evaluated by the FDA or Health Canada; this product is not intended to diagnose, treat, cure or prevent any disease.