Examples of anti-VASP applications

immunoblot using anti-VASP serum M4 (immunoGlobe.com)
Fig. 1: Monitoring cAMP-/cGMP-dependent protein kinase activity with a VASP Western blot. The shift from 46 to 50 kDa indicates Ser-157 phosphorylation. (Modified from EMBO J. 11:2063-2070; by permission of Oxford University Press)
immunoblot using anti-VASP serum M4 (immunoGlobe.com)
Fig. 2: Anti-VASP Western Blot of human platelets (left lane) and human skin fibroblasts (right lane). (Modified from EMBO J. 11:2063-2070; by permission of Oxford University Press)
immunofluorescence using anti-VASP serum M4 (immunoGlobe.com)
Fig. 3: VASP localization in a human skin fibroblast (immunofluorescence): association with focal contacts and actin filaments.
immunofluorescence using anti-VASP serum M4 (immunoGlobe.com)
Fig. 4: VASP localization at cell-cell contacts in canine MDCK cells
immunofluorescence using anti-VASP serum M4 (immunoGlobe.com)
Fig. 5: VASP immunofluorescence of a spreading platelet. (modified from EMBO J. 11:2063-2070; by permission of Oxford University Press)

immunoGlobe VASP Antibodies in Basic and Clinical Research

 


The tool for your research in:
  • actin cytoskeleton
  • actin-based motility of bacteria & viruses
  • monitoring cAMP- and cGMP-dep. kinase activity
  • efficacy of NO-donors
Background information
VASP (vasodilator stimulated phosphoprotein) is a proline-rich 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:
a) the conserved N-terminal Ena-VASP homology domain 1 (EVH1), which mediates binding to a novel proline-rich motif,
b) a more divergent proline-rich central domain (which is responsible for profilin binding), and
c) a conserved C-terminal EVH2 domain.

VASP is a substrate of cAMP- and cGMP-dependent protein kinases, which is expressed in most mammalian cell types and tissues. Phosphorylation of VASP at Ser-157 causes a mobility shift in SDS gel electrophoresis from 46 to 50 kDa that has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity in living cells and tissues without the need of isotopic labeling. Anti-VASP blots of platelet samples (which contain particularly high VASP levels) are useful tools to assess the efficacy of pharmacological NO donors and natural vasodilators, e.g. during coronary passage.

 

VASP phosphorylation has been reported to correlate with inhibition of platelet integrin GPIIbIIIa.

 

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.