GST M3-3, Recombinant Human

NA.26

Glutathione S-transferase mu 3 (GSTM3) is an enzyme that in humans is encoded by the GSTM3 gene. Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTs are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.
This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual′s susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Mutations of this class mu gene have been linked with a slight increase in a number of cancers, likely due to exposure with environmental toxins. Alternative splicing results in multiple transcript variants.

100

human

expressed in E. coli

>95% (SDS-PAGE)

frozen liquid

5.72 units/mg protein (using spectrophotometric determination of 1-chloro-2,4-dinitrobenzene (CDNB) conjugation with reduced glutathione (1 mM) in 100 mM NaPO4 (pH 6.5) at room temperature. )

2.95 mg/mL

−70℃

human ... GSTM3(2947)

The enzyme should be used by the end-user customer within 1 year of receipt.

10 - Combustible liquids

WGK 1