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Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Additionally we are shipping VASP Kits (24) and VASP Proteins (8) and many more products for this protein.
Showing 10 out of 263 products:
Human Polyclonal VASP Primary Antibody for IF, WB - ABIN197436
Zhao, Jiang, Kroll, Huber: A proline-rich protein binds to the localization element of Xenopus Vg1 mRNA and to ligands involved in actin polymerization. in The EMBO journal 2001
Show all 5 references for ABIN197436
Dog (Canine) Monoclonal VASP Primary Antibody for IF, IP - ABIN967976
DeMali, Barlow, Burridge: Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. in The Journal of cell biology 2002
Show all 5 references for ABIN967976
Human Polyclonal VASP Primary Antibody for IHC (p), WB - ABIN196882
Millard, Bompard, Heung, Dafforn, Scott, Machesky, Fütterer: Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53. in The EMBO journal 2005
Show all 5 references for ABIN196882
Human Polyclonal VASP Primary Antibody for IHC (p), WB - ABIN196950
Kühnel, Jarchau, Wolf, Schlichting, Walter, Wittinghofer, Strelkov: The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat. in Proceedings of the National Academy of Sciences of the United States of America 2004
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Human Polyclonal VASP Primary Antibody for IHC (p), WB - ABIN197382
Melichar, Behr-Roussel, Zabel, Uttenthal, Rodrigo, Rupin, Verbeuren, Kumar H S, Schmidt: Reduced cGMP signaling associated with neointimal proliferation and vascular dysfunction in late-stage atherosclerosis. in Proceedings of the National Academy of Sciences of the United States of America 2004
Show all 3 references for ABIN197382
Human Monoclonal VASP Primary Antibody for EIA, FACS - ABIN126908
Iyú, Glenn, White, Fox, Heptinstall: Adenosine derived from ADP can contribute to inhibition of platelet aggregation in the presence of a P2Y12 antagonist. in Arteriosclerosis, thrombosis, and vascular biology 2011
Ena/VASP function in retinal axons is required for terminal arborization but not pathway navigation.
VASP, zyxin (show ZYX Antibodies) and TES (show TES Antibodies) are tension-dependent members of focal adherens junctions independent of the alpha-catenin (show CTNNA1 Antibodies)-vinculin (show VCL Antibodies) module.
Data show that the phosphorylation status of vasodilator-stimulated phosphoprotein (VASP) at serine S322 can be predictive for breast cancer progression to an aggressive phenotype.
The authors propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their actin polymerase activity by tethering them to actin filaments.
Data show that tumor necrosis factor-alpha (TNF-alpha) increased A549 l (show HIF1A Antibodies)ung adenocarcinoma cell permeability by repressing vasodilator-stimulated phosphoprotein (VASP) expression through the activation of hypoxia inducible factor 1 alpha subunit (HIF-1alpha).
The authors demonstrate that vasodilator-stimulated phosphoprotein (VASP), which is critical for regulation of actin assembly, cell adhesion and motility, is a direct substrate of Yersinia pestis YpkA kinase activity.
Ena/VASP's ability to bind F-actin and profilin (show PFN1 Antibodies)-complexed G-actin (show ACTB Antibodies) are important for its effect, whereas Ena/VASP tetramerization is not necessary.
In clinical practice,LCR and CYP2C19 (show CYP2C19 Antibodies) gene polymorphism should be assessed in NCIS patients receiving clopidogrel treatment.
VASP phosphorylation at Ser(157) mediates its localization at the membrane, but that VASP Ser(157) phosphorylation and membrane localization are not sufficient to activate its actin catalytic activity
PKA regulates VASP phosphorylation in Ras-transformed cells in a non-cell-autonomous manner.
Serine phosphorylation of vasodilator-stimulated phosphoprotein (VASP) regulates colon cancer cell survival and apoptosis.
Thus, unlike host proteins characterized in Shigella pathogenesis that promote bacterial spread, VASP and EVL function to limit it.
Data show that the hypoxia inducible factor 1 alpha subunit (HIF-1alpha (show HIF1A Antibodies)) protein level in lung tissues increased significantly at four hours and eight hours, whereas the vasodilator-stimulated phosphoprotein (VASP) protein level decreased significantly.
Collectively, our studies highlighted that the CuB-induced actin aggregation and cofilin (show CFL1 Antibodies)-actin rod formation was mediated via the Ga13/RhoA (show RHOA Antibodies)/PKA/VASP pathway.
Ena/VASP regulates mDia2 (show DIAPH3 Antibodies)-initiated filopodial morphology, dynamics, and function.
cancer cells reaching liver sinusoids induced up-regulation of VASP
Low VASP activation was associated with high fat diet (HFD). Effects of HFD on aortic inflammation and insulin (show INS Antibodies) resistance were recapitulated by VASP knockout, implying a role for VASP to constrain inflammatory signaling and maintain insulin (show INS Antibodies) sensitivity.
Mena/VASP and alphaII-Spectrin complexes regulate cytoplasmic actin networks in cardiomyocytes and protect from conduction abnormalities and dilated cardiomyopathy.
CDC42 activation inhibits this activity and promotes IRSp53-dependent recruitment and clustering of VASP to drive actin assembly.
VASP physically interacted with IRSp53 (show BAIAP2 Antibodies) in NIH-Src (show SRC Antibodies) cells and was essential for podosome formation.
A VASP to Rac (show AKT1 Antibodies) to soluble guanylyl cyclase negative feedback loop limited cGMP production, thereby regulating adipogenesis and energy homeostasis.
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.
, Vasodilator-stimulated phosphoprotein