Catalog # FP2661
Fascin (Ser-39), phospho-specific Antibody
Size 100 μl
Species Reactivity Hu, Rt, Ms, Ck
MW 55 kDa
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.
Kraft, R. et al. (2006) J Neurosci 26:8734.
Vignjevic, D. et al. (2006) J Cell Biol. 174(6):863.
Adams, J.C. (2004) Curr Opin Cell Biol. 16(5):590.
*For more information, see UniProt Accession Q16658
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Bulek, K et al. (2019) J Immunol. 202(5):1540. (WB: mouse smooth muscle)
Rodriques, PC et al. (2017) Oncotarget. 8(43):74736. (WB: oral squamous cell carcinoma)
Kliewe, F. et al. (2017) Sci Rep. 7(1):9916. (WB: mouse podocytes)
Saad, A. et al. (2016) Sci Rep. 6:36699. (WB,IP,ICC,IHC: Breast Cancer cells/tissue)
Van Audenhove, I. (2014) FASEB Journal 28(4): 1805. (WB: human prostate PC-3)
This kit contains: