For Research Use Only | Not for Human or Veterinary Use

Description

Glutathione (GSH) is a naturally occurring tripeptide thiol composed of glutamate, cysteine, and glycine. It is one of the major low-molecular-weight thiols found in cells and is extensively studied in redox biology, thiol metabolism, and cellular signaling.

This research material is supplied as a lyophilized powder for laboratory research, analytical testing, and related scientific applications.

PubChem identifies reduced glutathione as a tripeptide with the molecular formula C₁₀H₁₇N₃O₆S, molecular weight of approximately 307.33 g/mol, and CAS number 70-18-8.

Research & Scientific Context

Glutathione contains a reactive cysteine thiol group that allows it to participate in a wide range of cellular redox reactions. Research has examined GSH metabolism in relation to redox signaling, thiol regulation, and cellular responses to reactive compounds.

GSH also participates in enzyme-mediated reactions. Glutathione peroxidases use GSH in peroxide-reduction reactions, while glutathione S-transferases use it in conjugation reactions involving electrophilic compounds. Oxidized glutathione (GSSG) can subsequently be converted back to GSH through glutathione reductase and NADPH-dependent reactions.

Key Research Areas

Cellular glutathione metabolism

Thiol and redox biology

GSH/GSSG redox systems

Glutathione-dependent enzyme activity

Protein S-glutathionylation

Cellular signaling and redox regulation

Glutathione Structure

Glutathione is a tripeptide, but its structure differs from a conventional three-amino-acid peptide. The glutamate and cysteine residues are connected through the γ-carboxyl group of glutamate, creating the characteristic γ-glutamyl linkage of GSH.

Component	Role in GSH
Glutamate	Forms the N-terminal γ-glutamyl portion
Cysteine	Contains the reactive thiol group
Glycine	Forms the C-terminal residue

The cysteine-derived thiol is central to the redox chemistry of glutathione and its interactions with proteins and reactive molecules.

GSH and GSSG

Glutathione exists primarily in reduced (GSH) and oxidized (GSSG) forms. During certain redox reactions, two GSH molecules can form glutathione disulfide, while cellular glutathione reductase systems help regenerate GSH.

Characteristic	GSH	GSSG
State	Reduced	Oxidized
Structure	Single glutathione molecule	Two GSH units linked by a disulfide bond
Research relevance	Thiol chemistry and redox reactions	Indicator and product of glutathione oxidation
Relationship	Reduced form	Oxidized form

This reversible relationship makes the GSH/GSSG system an important subject in studies of cellular redox state and signaling.

Analytical Documentation

A Certificate of Analysis (COA) is included in the product image gallery. Researchers should review the batch-specific documentation to verify the reported purity, identity, and other available analytical characteristics.

For glutathione research, the exact chemical state is also relevant because reduced GSH and oxidized GSSG are chemically distinct species.

Frequently Asked Questions

1. Is glutathione a peptide?

Yes. Glutathione is a tripeptide consisting of glutamate, cysteine, and glycine. Its unusual γ-glutamyl linkage distinguishes it from many conventional peptides.

2. What is the reduced form of glutathione?

Reduced glutathione is commonly abbreviated GSH. It contains a free cysteine thiol that participates in redox and thiol-exchange reactions.

3. What is GSSG?

GSSG is glutathione disulfide, the oxidized form produced when two GSH molecules become linked through their cysteine sulfur atoms. GSSG can be converted back to GSH through glutathione reductase-dependent reactions.

4. Why is the cysteine residue important?

The cysteine residue contains the reactive thiol group that gives glutathione much of its redox chemistry. This group participates in reactions involving peroxides, electrophiles, and protein thiols.

5. What enzymes interact with glutathione?

Research has examined glutathione as a substrate or cofactor for enzymes including glutathione peroxidases, glutathione S-transferases, and glutaredoxins. These systems are involved in redox regulation and cellular thiol chemistry.

6. What should researchers check on the glutathione COA?

The batch-specific COA should be reviewed for identity, reported purity, analytical results, and the chemical form of the supplied material before it is incorporated into laboratory or analytical work.

Research Materials & Documentation

Glutathione | The 10-Pack contains 1500 mg total lyophilized research material with ≥99% HPLC-certified purity. A Certificate of Analysis is included in the product image gallery for laboratory review.

Researchers should verify the batch-specific documentation before using the material in experimental or analytical workflows.

For Research Use Only | Not for Human or Veterinary Use.