Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG.1) Zhao WM, et al. (2001) EMBO J 20 (9): 2315-2325. Millard TH, et al. (2005) EMBO J 24 (2): 240-250. Kühnel K, et al. (2004) Proc Natl Acad Sci U S A 101 (49): 17027-17032. Haffner C, et al. (1995) EMBO J 14 (1): 19-27. Ramesh N, et al. (1997) Proc Natl Acad Sci U S A 94 (26): 14671-14676.
Immunogen
VASP (Ab-157) antibody was raised against a peptide sequence around aa.155~159 (R-V-S-N-A) derived from Human VASP.
Key Feature
Clonality
Polyclonal
Host Species
Rabbit
Tested Applications
IFWB
Western Blot: 1:500~1:1000, Immunofluorescence: 1:100~1:200: