GLUTATHIONE S-TRANSFERASE Property

storage temp. 

-70°C

form 

lyophilized powder

color 

White to off-white

Safety

Hazard Codes 

B

WGK Germany 

3

Hazard and Precautionary Statements (GHS)

GLUTATHIONE S-TRANSFERASE Chemical Properties,Usage,Production

Uses

Glutathione S-Transferase from human placenta has been used in antigen microarray and informatics analysis.

General Description

Glutathione S-transferase (GST) is a major detoxification enzyme, and exists as multiple cytoplasmic and membrane-bound isozymes. These isozymes differ in their catalytic activity, as well as in their non-catalytic binding properties. Cytoplasmic isoforms of GST are encoded by five genes, namely α, θ, μ, σ and π. α, μ and π are the most abundant forms in mammals. Membrane bound GST forms are encoded by a single gene.

Biochem/physiol Actions

Glutathione S-transferase (GST) catalyzes conjugation reactions during phase II metabolism. This enzyme also confers protection against catabolic products of peroxidized lipid and oxidized DNA, and ROS (reactive oxygen species) or electrophiles.

Purification Methods

It is purified by affinity chromatography using a column prepared by coupling glutathione to epoxy-saturated Sepharose. After washing contaminating proteins, the pure transferase is eluted with buffer containing reduced glutathione. The solution is then concentrated by ultrafiltration, dialysed against phosphate buffer at pH ~7 and stored in the presence of dithiothreitol (2mM) in aliquots at <-20o. [Simons & Vander Jag Anal Biochem 52 334 1977.]