Vasodilator-Stimulated Phosphoprotein (VASP) is a key regulatory protein involved in actin cytoskeleton dynamics, cell motility, adhesion, and proliferation. It belongs to the Ena/VASP family, which interacts with profilin and other actin-binding proteins to modulate filament elongation and bundling. VASP contains conserved domains, including the EVH1 (Enabling/VASP homology 1) domain for protein-protein interactions and the EVH2 domain for actin binding. Its activity is tightly regulated by phosphorylation, particularly at Ser157. Ser239. and Thr278. mediated by cyclic nucleotide-dependent kinases (e.g., PKA, PKG) in response to cellular signals like cAMP/cGMP.
VASP antibodies are essential tools for studying its expression, localization, and post-translational modifications. They are widely used in techniques such as Western blotting, immunofluorescence, and immunoprecipitation to explore VASP's role in cellular processes. For instance, these antibodies help elucidate how VASP phosphorylation influences endothelial barrier function, platelet activation, or cancer cell migration. Dysregulation of VASP is linked to cardiovascular diseases, metastatic cancers, and immune disorders, making it a potential therapeutic target. Researchers also employ VASP antibodies to assess the efficacy of pharmacological agents targeting cAMP/PKG pathways. Specific monoclonal or polyclonal antibodies are validated for detecting distinct phosphorylation states or total protein levels, ensuring precision in mechanistic studies. Overall, VASP antibodies serve as critical reagents for advancing understanding of cytoskeletal dynamics in health and disease.