VASP (Thr-278), Phosphospecific Antibody

Actin filament tethering and bundling are important mechanisms involved in actin superstructure assembly. The ENA/VASP family includes VASP, mena, and Ena-Vasp-like (EVL) . These multidomain proteins localize to the leading edge of filopodia where they associate with AFs, interact with profilin, and compete with capping proteins at the barbed end of AFs. Artificial relocalization of VASP from the plasma membrane to mitochondrial membranes inhibits filopodial formation and axon branching, while deletion of all three ENA/VASP proteins produces defects in cortical axon-tract formation. Regulation of VASP protein activity occurs through phosphorylation at Ser-157, Ser-239, and Thr-278. AMPK phosphorylates Thr-278, leading to impaired actin stress fiber assembly and changes in cell morphology.

The antibody detects a 50 kDa* band corresponding to VASP in Western blots of human A431 and HeLa cells, as well as mouse C2C12 cells that have been treated with calyculin A. This sequence has significant homology to the conserved site in rat and mouse VASP, but is not conserved in mena or EVL proteins.