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Rabbit Polyclonal Phospho-VASP (S157) antibody (STJ90777)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, IHC, ELISA
Recommended dilution: WB 1:500-1:2000; IHC 1:100-1:300; ELISA 1:5000;
Recommended protocols: check protocols
Click or hover above images to see image description for VASP (phospho Ser157) Polyclonal Antibody.
Check alternative names for the antibodyExpand
SCBT cat No: To be updated
VASP (phospho Ser157) Polyclonal Antibody
|Catalogue No.|| |
Human, Mouse, Rat
Phospho-VASP (S157) Polyclonal Antibody detects endogenous levels of VASP protein only when phosphorylated at S157.
Synthesized phospho-peptide derived from VASP (phospho Ser157) at AA range 100-180
WB, IHC, ELISA
|Recommended dilution|| |
WB 1:500-1:2000; IHC 1:100-1:300; ELISA 1:5000;
|Molecular weight|| |
VASP (phospho Ser157) Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
VASP (phospho Ser157) Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Vasodilator-stimulated phosphoprotein antibody, VASP antibody
|Protein names|| |
Vasodilator-stimulated phosphoprotein , VASP
|Protein 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, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.
|Protein tissue specificity|| |
Highly expressed in platelets.
|Protein sequence and 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. / The WH1 domain mediates interaction with XIRP1. / Belongs to the Ena/VASP family. / Contains 1 WH1 domain.
|Protein post-translational modifications|| |
Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-157, the preferred site for PKG/PRKG1, Ser-239. In ADP-activated platelets, phosphorylation by PKA or PKG on Ser-157 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-278 requires prior phosphorylation on Ser-157 and Ser-239. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-278 by AMPK does not require prior phosphorylation at Ser-157 or Ser-239. Phosphorylation at Ser-157 by PKA is required for localization to the tight junctions in epithelial cells. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Phosphorylation at Ser-322 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-157, while nitric oxide (NO) promotes phosphorylation at Ser-157, but also at Ser-239. Response to NO and CO is blunted in platelets from diabetic patients, and VASP is not phosphorylated efficiently at Ser-157 and Ser-239.
|Protein cellular localization|| |
Cytoplasm / Cytoplasm > cytoskeleton / Cell junction > focal adhesion / Cell junction > tight junction / Cell projection > lamellipodium membrane / Cell projection > filopodium membrane
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St John’s Laboratory Ltd.
|Product type|| |
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