Examples of anti-VASP applications
immunoGlobe VASP Antibodies in Basic and Clinical Research
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.