Anti-VASP (C-terminal) antibody produced in rabbit

VASP (vasodilator stimulated phosphoprotein) is localized at highly dynamic membrane regions, focal adhesion sites, lamellipodia protrusions, filopodia tips, and along stress fibers. VASP is also localized at cell matrix and cell-cell contacts.

Vasodilator stimulated phosphoprotein (VASP) is encoded by the gene mapped to human chromosome 19q13.32. The encoded protein belongs to the Ena/VASP protein family. VASP is characterized with an N-terminal EVH1 domain, C-terminal EVH2 domain and proline-rich region.

Anti-VASP (C-terminal) antibody produced in rabbit has been used in immunoblotting and immunofluorescence.

VASP (vasodilator stimulated phosphoprotein) 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.

Vasodilator stimulated phosphoprotein (VASP) acts as an actin-polymerization regulator and plays a vital role in regulation of cell migration by interacting with Migfilin, a cell-extracellular matrix (ECM) adhesion protein. Elevated expression of VASP contributes to the development of breast cancer (BC). Hence, this protein can be used as a potential biomarker for BC metastasis. Phosphorylation of VASP by protein kinase A (PKA) at phosphorylation site S157 aids in localization of cell periphery into focal adhesions, but phosphorylation of VASP at S239 and T278 aids in regulation of F-actin assembly.

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

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