Glutathione

Glutathione: The cell’s own tripeptide

Glutathione is a tripeptide made of glutamate, cysteine and glycine (gamma-Glu-Cys-Gly). It has an unusual bond: the glutamate is linked through its side-chain gamma-carboxyl group rather than the usual alpha position, which protects it from most peptidases. The cysteine’s thiol group is the reactive part of the molecule. In its reduced form (GSH) it donates electrons; two molecules then pair up through a disulfide bond to form oxidized glutathione (GSSG).

Its role in research

Glutathione is found at high levels in most animal cells and is central to redox biology. Researchers measure the GSH/GSSG ratio as an indicator of oxidative stress, and glutathione is studied in cell and animal models involving detoxification enzymes such as glutathione S-transferases, mitochondrial function and responses to reactive oxygen species. It is also a routine reagent in biochemistry for maintaining reducing conditions. Protein chemists use reduced and oxidized forms together to help proteins refold correctly.

Handling considerations

Reduced glutathione oxidizes in solution over time, especially at neutral or higher pH and in the presence of metal ions. Many labs prepare solutions fresh and record the preparation time with the lot.

The glutathione vial

The grid shows a single glutathione vial listing. Compared with most peptides in the Resolve catalog, the amount per vial is large, stated in hundreds of milligrams or more on the label, reflecting the higher working concentrations typical in redox studies. The material is supplied freeze-dried in a stoppered vial.

Linking your vial to its COA

Read the lot number on the vial and find the certificate carrying the same lot in our COA / Lab Reports. Confirm the quantity on the report matches the large amount stated on your label. Certificates are being posted progressively, and support can confirm a lot by email.

Glutathione from Resolve is for laboratory research use only.