| Overview |
| bs-70498r-100ul |
| Fascin (Ser-39), Phosphospecific Antibody |
| WB |
| This antibody was cross-adsorbed to a phospho-serine peptide before Affinity purification using phosho-fascin (Ser-39) peptide (without carrier). The antibody detects a 55 kDa* band corresponding to fascin on SDS-PAGE immunoblots of mouse C2C12 and human HeLa cells treated with Calyculin A. |
| Human, Mouse, Rat, Chicken |
| Specifications |
| Unconjugated |
| Rabbit |
| Fascin (Ser-39) synthetic peptide (coupled to carrier protein) corresponds to amino acids surrounding serine 39 in human fascin. |
| Ser-39 |
| Polyclonal |
| IgG |
| Antigen Affinity purification |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. |
| Target |
| Q16658 |
| p55 |
| 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. |
| Application Dilution |
| WB |
1:300-5000 |
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