RGS7 polyclonal antibody

Heterotrimeric G proteins function to relay information from cell surface receptors to various intracellular effectors. G proteins comprise α, β and γ subunits, and following activation the α subunit binds GTP and dissociates from the βγ complex. A large group of proteins have been identified as GTPase-activating proteins (GAPs), including the RGS (regulator of G protein signaling) family, which serve to deactivate specific Gα isoforms by increasing the rate at which they convert GTP to GDP. A subfamily of RGS proteins expressed in the central nervous system contain, in addition to the highly conserved RGS domain, a characteristic GGL domain, or G protein γ subunit-like domain, which mediates binding to Gβ 5 subunits. This subfamily, which includes RGS6, RGS7, RGS9 and RGS11, associates with Gβ 5 to form active GAP complexes that are predominantly localized to the cytosol. RGS/β5 complexes preferentially target Gαo subunit for hydrolysis and inhibit Gβ1γ2-mediated activation of phospholipase C.