VASP Antibodies, cDNA Clones Research Reagents

VASP (Vasodilator Stimulated Phosphoprotein), located on 19q13.32, is a Protein Coding gene. The gene produces a 39830 Da protein composed of 380 amino acids. VASP is a member of the Ena-VASP protein family. Ena/VASP proteins are conserved regulators of actin dynamics that have important roles in several physiological processes. VASP is phosphorylated in human platelets in response to both the cAMP- and cGMP-elevating agents and its phosphorylation correlates with platelet inhibition. Diseases such as Thrombosis and Clopidogrel Resistance are associated with VASP.

VASP Antibody (2)

    VASP cDNA Clone (30)

    VASP qPCR Primer (1)

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    VASP Background

    Vasodilator-stimulated phosphoprotein (VASP) is a member of actin regulatory proteins implicated in platelet adhesion. Ena/VASP proteins are conserved regulators of actin dynamics that have important roles in several physiological processes such as morphogenesis, axon guidance, endothelial barrier function, and cancer cell invasion and metastasis. Ena/VASP proteins act as actin polymerases that drive the processive elongation of filament barbed ends in membrane protrusions or at the surface of bacterial pathogens. Ena/VASP tetramers are processive actin elongation factors that localize to diverse F-actin networks composed of filaments bundled by different cross-linking proteins, such as filopodia (fascin), lamellipodia (fimbrin), and stress fibers (α-actinin). Also, phosphorylation of VASP is utilized for the assessment of platelet reactivity in patients treated with P2Y12 receptor antagonists, a class of antiplatelet agents.

    VASP References

    • Ito Y, et al. (2018) Vasodilator-stimulated phosphoprotein (vasp) is not a major mediator of platelet aggregation, thrombogenesis, haemostasis, and antiplatelet effect of prasugrel in rats. Sci Rep 8 (1): 9955.
    • Harker AJ, et al. (2019) Ena/vasp processive elongation is modulated by avidity on actin filaments bundled by the filopodia cross-linker fascin. Mol Biol Cell 30 (7): 851-862.
    • Gau D, et al. (2019) The vasp-profilin1 (pfn1) interaction is critical for efficient cell migration and is regulated by cell-substrate adhesion in a pka-dependent manner. J Biol Chem 294 (17): 6972-6985.
    • Estin ML, et al. (2017) Ena/vasp proteins regulate activated t-cell trafficking by promoting diapedesis during transendothelial migration. Proc Natl Acad Sci U S A 114 (14): E2901-e2910.

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