Phospho-Filamin A (Ser2152) Antibody detects endogenous levels of filamin A only when phosphorylated at serine 2152. This antibody also reacts with filamin C when it is phosphorylated at serine 2146.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with synthetic phosphopeptides corresponding to residues surrounding Ser2152 of human filamin A and Ser2146 of human filamin C. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Filamins are a family of dimeric actin binding proteins that function as structural components of cell adhesion sites. They also serve as a scaffold for subcellular targeting of signaling molecules (1). The actin binding domain (alpha-actinin domain) is located at the very amino-terminus, followed by as many as 24 tandem repeats of about 96 residues, and the dimerization domain is located at the carboxy-terminal end of th protein. In addition to actin filaments, filamins associate with other structural and signaling molecules such as beta-integrins, Rho/Rac/Cdc42, PKC, and insulin receptor, primarily through their carboxy-terminal half (1-3). Filamin A, the most abundant, and filamin B, less abundant, are widely expressed isoforms, while filamin C is predominantly expressed in muscle (1). Serine 2152 of filamin A is phosphorylated by PAK1, and this phosphorylation is required for PAK1-mediated actin cytoskeleton reorganization (4).