Heterotrimeric G proteins function to relay information from cell surface receptors to intracellular effectors. In mammals, G protein alpha, beta and gamma polypeptides are encoded by at least 16, 4 and 7 genes, respectively. Most interest in G proteins has been focused on their alpha subunits, since these proteins bind and hydrolyze GTP and most obviously regulate the activity of the best studied effectors. Four Galpha GTPase-activating proteins (GAPs) have been identified and are designated RGS1 (regulator of G protein signaling), RGS4, RGS10 and GAIP (Galpha-interacting protein). Each of these proteins has been shown to deactivate specific Galpha isoforms by increasing the rate at which they convert GTP to GDP, RGS1, RGS4 and GAIP bind tightly to and exhibit GAP activity towards Galpha i , Galpha o and Galpha t , but not Galpha s. RGS10 increases the GTP hydrolytic activity of several members of the Galpha i subfamily including Galpha i-3, Galpha z and Galpha o.
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:
WB: 1:500~1:1000
Application Notes:
RGS19 (phospho-S151) polyclonal antibody detects endogenous levels of RGS19 protein only when phosphorylated at Ser151.
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