Heterotrimeric G proteins function to relay information from cell surface receptors to various intracellular effectors. G proteins comprise å, ß and g subunits, and following activation the a subunit binds GTP and dissociates from the ßg complex (1). 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 Gå isoforms by increasing the rate at which they convert GTP to GDP (2,3). 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 g subunit-like domain, which mediates binding to Gß 5 subunits (4,5). This subfamily, which includes RGS6, RGS7, RGS9 and RGS11, associates with Gß 5 to form active GAP complexes that are predominantly localized to the cytosol (6). RGS/ß5 complexes preferentially target Gåo subunit for hydrolysis and inhibit Gß1g2-mediated activation of phospholipase C (7).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of RGS9 of mouse, rat and human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 444-674 of RGS9 of human origin
Tissue Specificity
epitope corresponding to amino acids 444-674 of RGS9 of human origin