ANTI-PHOSPHO-VASP [PSER239], ANTIBODY&

Description_x000D_ General description_x000D_ Monoclonal Anti-WASH1 (mouse IgG1 isotype) is derived from the hybridoma WASH1-27 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to an internal region of human WASH1. VASP (vasodilator-stimulated phosphoprotein) belongs to the family of Ena/VASP actin-regulatory proteins. VASP is localized at highly dynamic membrane regions, focal adhesion sites, lamellipodia protrusions, filopodia tips and along stress fibers._x000D_ Immunogen_x000D_ synthetic peptide containing phosphorylated Ser239 of human VASP conjugated to KLH. The corresponding sequence is identical in mouse and rat VASP._x000D_ Application_x000D_ Anti-phospho-VASP [pSer239] antibody produced in rabbit has been used in:_x000D_ • immunoblotting_x000D_ • immunoprecipitation_x000D_ • immunofluorescence_x000D_ Physical form_x000D_ Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide._x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_ Biochem/physiol Actions_x000D_ VASP (vasodilator-stimulated phosphoprotein) is implicated in cell motility and adhesion. VASP is localized at cell matrix and cell-cell contacts and plays an important role in adherens junction formation and stabilization in epithelial cells. VASP is a substrate for cAMP- and cGMP-dependent protein kinases. It is phosphorylated at multiple sites including Ser157, Ser239 and Thr278. cGMP-dependent protein kinase I (cGKI) phosphorylates VASP in a variety of cells, including platelets, fibroblasts and endothelial cells. In platelets, cGMP-mediated phosphorylation of VASP correlates with inhibition of agonist-induced platelet aggregation. Ena/VASP proteins are required for neurite initiation and extension in the developing cortex. VASP has been shown to be required for endothelial barrier function in vivo. Knockout of Ena/VASP proteins in mice leads to increased endothelial permeability causing fatal vascular leakage and haemorrhaging during late embryonic development. In contrast, overexpression of VASP enhances barrier function of endothelial cells in vitro and increases their force generation.