Reactive species
Human;Mouse;Rat
Antibody type
Polyclonal Antibody
Protein name
VASP (Ser239)
Immunogen
Synthesized phosho peptide around human VASP (Ser239)
Specificity
This antibody detects endogenous levels of Human Mouse Rat VASP (phospho-Ser239)
Constitute
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Source
Polyclonal, Rabbit,IgG
Dilution rate
WB 1:1000-2000
Purification process
The antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
Other name
Vasodilator-stimulated phosphoprotein (VASP)
Background
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. [provided by RefSeq, Jul 2008],
Function
domain:The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.,domain:The WH1 domain mediates interaction with XIRP1.,function:Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. VASP promotes actin nucleation and increases the rate of actin polymerization in the presence of capping protein. Plays a role in actin-based activity of Listeria monocytogenes in platelets.,PTM:Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred
