Anti-GSTM3 / Glutathione S-Transferase mu 3, clone CPTC-GSTMu3-1

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide. Members of the glutathione S-transferase (GST) family of proteins function in the detoxification of xenobiotics to protect cells against toxicant-induced damage. There are eight families of GST proteins, each of which are composed of proteins that have a variety of functions throughout the cell. The GSTM proteins (GSTM1-GSTM5 in human and GSTM1-GSTM7 in mouse) are members of the mu class of enzymes that conjugate with glutathione and function in the detoxification of carcinogens, environmental toxins and products of oxidative stress. 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. Null mutations of this class mu gene have been linked with an increase in a number of cancers, likely due to an increased susceptibility to environmental toxins and carcinogens. Multiple protein isoforms are encoded by transcript variants of this gene. GSTM3 protein is selectively expressed in the testis and brain. GSTM3 may also be tumor suppressive in RCC, as low expression has been demonstrated to correlate with RCC risk and poor prognosis in post-op patients. Protein 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. [The UniProt Consortium]