Fascin (unphosphorylated Ser-39) Blocking Peptide
€155.00
In stock
SKU
ECM-FX2215
Background:
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.
Sequence: Unphosphorylated fascin (Ser-39) synthetic peptide corresponds to amino acids surrounding serine 39 in human fascin. 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.
Specificity: This peptide is an unphosphorylated control peptide for Fascin (Ser-39) phospho-specific antibody (FP2661). The peptide can be used along with phosphorylated Fascin (Ser-39) peptide (FX2665) in ELISA, Western blot and immunocytochemistry antibody blocking experiments.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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.
Sequence: Unphosphorylated fascin (Ser-39) synthetic peptide corresponds to amino acids surrounding serine 39 in human fascin. 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.
Specificity: This peptide is an unphosphorylated control peptide for Fascin (Ser-39) phospho-specific antibody (FP2661). The peptide can be used along with phosphorylated Fascin (Ser-39) peptide (FX2665) in ELISA, Western blot and immunocytochemistry antibody blocking experiments.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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