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VASP monoclonal antibody (IE273)

ALX-804-177-C050 50 µg 397.00 USD
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Product Details

Alternative Name:Vasodilator stimulated phosphoprotein
Immunogen:Purified human VASP (vasodilator stimulated phosphoprotein).
UniProt ID:P50552
Species reactivity:Human
Bovine, Porcine, Rabbit
Specificity:Recognizes both the 46kDa (Ser157 dephospho-) and 50kDa (Ser157 phospho-) form of VASP.
Applications:ICC, IP, WB
Recommended Dilutions/Conditions:Immunocytochemistry (1-5µg/ml)
Western Blot (0.01-0.25µg/ml)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
Formulation:Liquid. In PBS containing 2mg/ml BSA and 0.02% sodium azide.
Handling:Avoid freeze/thaw cycles.
Shipping:Blue Ice
Short Term Storage:+4°C
Long Term Storage:-20°C
Scientific Background:VASP (vasodilator stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. Phosphorylation of VASP at Ser-157 causes a mobility shift in SDS gel electrophoresis from 46 to 50 kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity. VASP is the founding member of the Ena-VASP protein family, comprising the Drosophila protein Enabled (Ena), its mouse homologue Mena (mammalian Enabled), and mouse EVL (Ena-VASP-like protein). With these proteins VASP shares a conserved overall domain organization:
  1. the conserved N-terminal Ena-VASP homology domain 1 (EVH1), which mediates binding to a proline-rich motif,
  2. a more divergent proline-rich central domain (which is responsible for profilin binding), and
  3. a conserved C-terminal EVH2 domain.
Particularly high VASP levels are present in platelets, although VASP is expressed in a wide variety of cell types and tissues. In cultured cells, VASP is associated with focal adhesions, cell-cell contacts, microfilaments, and highly dynamic membrane regions. From in vitro binding data VASP has been suggested to link profilin to zyxin, vinculin, and the Listeria spp. surface protein ActA, respectively. Functional evidence indicates that VASP is a crucial factor involved in the enhancement of actin filament formation and the actin-dependent motility of intracellular bacterial pathogens.
Regulatory Status:RUO - Research Use Only

Product Literature References

Effects of In Vivo Nitroglycerin Treatment on Activity and Expression of the Guanylyl Cyclase and cGMP-Dependent Protein Kinase and Their Downstream Target Vasodilator-Sitmulated Phosphoprotein in Aorta: A. Mülsch, et al.; Circulation 103, 2188 (2001), Abstract; Full Text
A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family: K. Niebuhr, et al.; EMBO J. 16, 5433 (1997), Abstract;
Monoclonal antibodies against the focal adhesion protein VASP revealing epitopes involved in the interaction with two VASP binding proteins and VASP phosphorylation: Abel, et al.; Eur. J. Cell Biol. 69 (Suppl. 42), 39a (1996), Abstract;

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