Phospho-Ras-GRF1 (Ser916) Antibody detects transfected levels of Ras-GRF1 only when phosphorylated at serine 916. This antibody does not cross-react with phosphorylated Ras-GRF2.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding serine 916 of mouse Ras-GRF1. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Ras activity is regulated by GAP (GTPase activating proteins) and GEFs (guanine nucleotide exchange factors). Ras-GRF1 (also known as CDC25Mm) is neuronal RasGEF and is regulated by heterotrimeric G proteins and calcium influx (1,2). Binding to calmodulin and phosphorylation stimulate Ras-GRF1 activity (1,2). Multiple PKA phosphorylation sites on Ras-GRF have been identified. Phosphorylation on the two major sites, Ser54 and Ser822, inhibits Ras-GRF activity (3). Carbachol (a muscarinic agonist)-induced phosphorylation on Ser916 is essential but not sufficient for maximal Ras-GRF activity (4). It has been reported that Ras-GRF1 also shows GEF activity toward Rac after phosphorylation by the tyrosine kinase Src (5).