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.
Target:
Fascin (Ser-39)
Application Dilute:
WB(1:300-5000), IHC()
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