epitope mapping within an N-terminal extracellular domain of mGluR-7 of human origin
recommended for detection of mGluR-7 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
mGluR-7 Background Information The mGluR proteins (metabotropic glutamate receptors) are members of the G protein-coupled receptor family and are functionally and pharmacologically distinct from the GluR proteins (ionotropic glutamate receptors). The eight currently known mGluR proteins are mediated by two G-proteins with opposing regulation of adenylate cyclase pathways. The activities of mGluR1 and mGluR5 are mediated by a G protein that activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current. The remainder of the eight subtypes of mGluR have an activity mediated by a G protein that inhibits adenylate cyclase activity. mGluR-7, which can interact with PRKCABP, acts as a receptor for glutamate. It is highly expressed in various areas of the brain, but highest levels are detected in cerebellum, cerebral cortex and hippocampus.