Rabbit anti-Human GSTM3 Polyclonal Antibody

Uniprot Id

P21266

Target Species

Human

Target Name

GSTM3

Target Full Name

Glutathione S-transferase Mu 3

Target Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers.

Target Subcellular Location

Cytoplasm.

Target Protein Families

GST superfamily, Mu family

Target Tissue Specificity

Testis and brain.

Target Research Area

Metabolism

Target Synonyms

brain GST; brain type mu glutathione S transferase; glutathione S alkyltransferase M3 ; glutathione S aryltransferase M3; glutathione S transferase M3 (brain); glutathione S transferase M3; Glutathione S transferase Mu 3 ; glutathione S transferase, Mu 3 ; Glutathione S-transferase Mu 3; GST class mu 3; GST class-mu 3; GST5; GSTB; Gstm3; GSTM3-3; GSTM3_HUMAN; GTM3; hGSTM3-3; MGC3310; MGC3704; S (hydroxyalkyl)glutathione lyase M3

Target Background

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. 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.