Fascin (Ser-39), Phosphospecific Antibody

Fascin is an actin filament bundling protein localized to lamellipodia and filopodia where it has important roles in cell motility. Regulation of fascin occurs through PKC-mediated phosphorylation of Ser-39 in the F-actin binding site. Cell permeant peptides that block PKC phosphorylation of Ser-39 increase cell migration, while peptides that block fascin binding to F-actin alter lamellipodial morphology and cause aberrant cell motility. Studies using RNA interference of fascin show that fibroblasts have reduced number and abnormal morphology of filopodia, while Ser-39 phosphorylation status may determine filopodial frequency. In Drosophila neurons, fascin deficiency causes alterations in actin filaments and leads to abnormal morphology of developing neurons. Thus, fascin is a critical element of actin-based motility in various cell types.

Clone M315 was generated from a phospho-Fascin (Ser-39) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding serine 39 in human fascin.

The antibody detects a 55 kDa* band corresponding to fascin on SDS-PAGE immunoblots of mouse C2C12 cells treated with Calyculin A. This band is not observed after lambda phosphatase treatment. This sequence has high homology to the conserved site in rat and mouse fascin, as well as to the conserved region in fascin-2, but has low homology to the conserved region in fascin-3.