Identity (HPLC)
High-performance liquid chromatography records the compound’s retention profile against a reference.
Research peptide
Glutathione
Lyophilized powder, catalogued by compound identity and backed by a certificate of analysis for its production batch.
For laboratory research only. Not for human or veterinary use.
$110.00Coming soon
Size
Coming soon1,500 mg
View specifications Batch documentation Certificate of analysis
- Third-party tested
- Secure packaging
- Supplied for laboratory research
- Identity by HPLC & LC-MS Compound identity documented per batch.
- Batch-specific COA A certificate of analysis per batch.
- Secure packaging Sealed, labelled research vials.
- Tested at USC University of Southern California, every batch.
Documented by batch
Every batch is catalogued, tested and recorded.
Overview
Glutathione is a naturally occurring tripeptide composed of glutamate, cysteine, and glycine. It is commonly abbreviated as GSH in its reduced form and is widely studied in biochemistry, cell biology, oxidative chemistry, and redox research.
Glutathione is present across many living systems and participates in thiol chemistry, redox buffering, enzymatic reactions, and cellular signaling. Because of these roles, it is frequently used as a reference compound or research analyte in studies of oxidative balance, cellular metabolism, protein thiol regulation, and glutathione-dependent enzyme systems.
Documented by batchCatalogued by compound identity
Compound identityCAS · Molecular weight · Sequence
Batch recordsBatch · Lot · Production date
Independent testingHPLC · LC-MS
Specifications
Product specifications
Format
Lyophilized powder
Appearance
White lyophilized powder
Molecular weight
307.32 g/mol
CAS number
70-18-8
Sequence
L-gamma-glutamyl-L-cysteinyl-glycine (tripeptide, 3 residues)
Storage
Store refrigerated at 2–8°C, protected from light and moisture. For extended storage, follow your laboratory's standard storage procedures.
Quality & testing
Certificate of analysis
Every batch is third-party tested for identity and analytical purity. Where the certificate for the current batch is published it appears below; otherwise it is available on request.
Every batch is third-party tested; the batch-specific certificate of analysis is available on request.
Testing records
What each batch record documents
Every batch is accompanied by laboratory records. The entries below describe what each record documents.
Mass (LC-MS)
Mass spectrometry records the compound’s measured mass to document molecular identity.
Appearance
The physical appearance of the material is recorded, for example a white lyophilized powder.
Batch record
Each batch is logged with a lot number and production date for traceability.
These are records of laboratory testing carried out on the batch. They document compound identity for research use and are not a statement of safety, suitability, or fitness for any use.
Research information
Reduced and oxidized glutathione
Reduced glutathione is commonly represented as GSH. Upon oxidation, glutathione can form glutathione disulfide, commonly abbreviated GSSG. The relationship between GSH and GSSG is widely investigated as part of cellular redox biology.
Redox biology
Glutathione is one of the major low-molecular-weight thiols studied in cellular systems. The GSH/GSSG couple is used extensively in research examining redox homeostasis, oxidative stress, thiol-disulfide exchange, and the response of cells to changing oxidative conditions.
Glutathione-dependent enzyme systems
Glutathione participates in several enzyme systems, including glutathione peroxidases, glutathione reductase, glutathione S-transferases, and glutaredoxins. Research on these pathways examines peroxide reduction, conjugation reactions, recycling of oxidized glutathione, protein thiol chemistry, and redox-dependent signaling.
S-glutathionylation
A major research area involving glutathione is reversible protein S-glutathionylation. This process involves formation of mixed disulfides between glutathione and protein thiols and is studied as a mechanism involved in redox regulation, protection of protein cysteine residues, and cell signaling.
Analytical research
Glutathione and GSSG can be investigated using a range of analytical methods, including chromatographic, electrophoretic, spectrometric, photometric, fluorimetric, and electrochemical approaches. Method selection, sample preparation, oxidation control, and storage conditions are especially important because glutathione is redox-active and can change during sample handling.
Common research areas
- GSH/GSSG redox balance
- Oxidative stress models
- Reactive oxygen species research
- Thiol-disulfide exchange
- Glutathione peroxidase and glutathione reductase systems
- Glutathione S-transferase activity
- Glutaredoxin-dependent reactions
- Protein S-glutathionylation
- Cellular and mitochondrial redox studies
- Analytical method development for GSH and GSSG
Research handling considerations
Because GSH can oxidize to GSSG, researchers should consider temperature, oxygen exposure, light, pH, sample preparation, storage time, and analytical workflow when designing experiments. Appropriate controls and validated methods are important for obtaining reproducible results.
Frequently asked questions
Questions and documentation
What is glutathione?
Glutathione is a tripeptide composed of glutamate, cysteine, and glycine. It is widely studied as a low-molecular-weight thiol involved in cellular redox chemistry.
What does GSH mean?
GSH is the common abbreviation for reduced glutathione. Its cysteine thiol group is central to many of the redox reactions investigated in glutathione research.
What is GSSG?
GSSG is glutathione disulfide, the oxidized form produced when two glutathione molecules form a disulfide bond.
Why do researchers study the GSH/GSSG relationship?
The balance between reduced and oxidized glutathione is widely used in research examining cellular redox state, oxidative conditions, and thiol homeostasis.
What enzyme systems involve glutathione?
Major research systems include glutathione peroxidases, glutathione reductase, glutathione S-transferases, and glutaredoxins.
What is S-glutathionylation?
S-glutathionylation is a reversible post-translational modification in which glutathione forms a mixed disulfide with a protein cysteine residue. It is studied in redox signaling and protein thiol regulation.
How can glutathione be analyzed in research?
Researchers use methods including HPLC, capillary electrophoresis, mass spectrometry, photometric, fluorimetric, and electrochemical detection. The appropriate technique depends on the sample and research objective.
Why is sample handling important when studying glutathione?
Glutathione is redox-active and can oxidize during collection, preparation, or storage. Poor handling can alter measured GSH and GSSG values and reduce reproducibility.
What factors can affect glutathione stability in a research workflow?
Relevant factors include temperature, oxygen exposure, pH, light, storage duration, freeze-thaw cycles, matrix composition, and sample preparation procedures.
What information should be checked on a glutathione research product?
Researchers may review product identity, stated purity, lot number, storage information, analytical method, certificate of analysis, and any additional batch-specific specifications.
Does an HPLC purity result prove molecular identity?
No. HPLC can provide information about chromatographic purity under a defined method, but molecular identity generally requires a separate identity method. Claims should match the actual analytical testing performed.
Does LC-MS alone prove purity?
Not necessarily. Mass spectrometry can support molecular identity by measuring mass-to-charge information, while purity is typically assessed using a validated separation method. The exact conclusion depends on the analytical method and data.
Why is batch-specific documentation useful?
Batch-specific documentation helps researchers connect experimental results to a defined lot and supports repeatability, quality review, and investigation of unexpected results.
Is livvmore Glutathione intended for human or veterinary use?
No. livvmore Glutathione is presented for laboratory research use only and is not intended for human or veterinary use.
What does research use only mean?
All products are supplied strictly for in-vitro laboratory research and are not for human or veterinary use, diagnosis, treatment, or personal consumption.
How are the products documented?
Every production batch is independently identity- and purity-tested at a university laboratory, the USC Alfred E. Mann Multi-Omics Mass Spectrometry Core, with a certificate of analysis documented for each batch. Published results are collected in the COA library.
Is a certificate of analysis available?
A certificate of analysis is documented for each production batch, recording the batch number, identity confirmation, estimated purity, method and test date. Published results are in the COA library; the batch-specific certificate for a given order is available on request.
Who can purchase?
By placing an order, purchasers acknowledge that the product is intended solely for laboratory research use and agree to the Research Use Terms.
Fulfilment
How orders are handled
-
Secure packaging
Sealed, labelled research vials, packed to protect integrity in transit.
-
Third-party tested
Every batch is third-party tested; the certificate of analysis is available on request.
-
Research customers only
Supplied to qualified researchers for laboratory research use.
Shipping options and timelines are shown at checkout.
- Third-party tested Independent testing per batch
- Documented by batch Batch and lot records
- Certificate of analysis Available on request
- Identity by HPLC & LC-MS Compound identity documented
- Secure packaging Sealed, labelled research vials
- Supplied for laboratory research Research use only
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Glutathione
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