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 sub-types of mGluR have an activity mediated by a G-protein that inhibits adenylate cyclase activity. mGluR-3, which may interact with GRASP, acts as a receptor for glutamate.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
IHC: 1:50~1:200
Application Notes:
mGluR-2/3 (N867) polyclonal antibody detects endogenous levels of mGluR-2 and mGluR-3 protein
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