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Ena/VASP function in retinal axons is required for terminal arborization but not pathway navigation.
VASP phosphorylation assay could be useful in studies aimed at investigating relations between clopidogrel active metabolite bioavailability and clinical events.
VASP, zyxin (show ZYX ELISA Kits) and TES (show TES ELISA Kits) are tension-dependent members of focal adherens junctions independent of the alpha-catenin (show CTNNA1 ELISA Kits)-vinculin (show VCL ELISA Kits) 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 ELISA Kits)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 ELISA Kits)-complexed G-actin (show ACTB ELISA Kits) are important for its effect, whereas Ena/VASP tetramerization is not necessary.
In clinical practice,LCR and CYP2C19 (show CYP2C19 ELISA Kits) 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.
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 ELISA Kits)) 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 ELISA Kits)-actin rod formation was mediated via the Ga13/RhoA (show RHOA ELISA Kits)/PKA/VASP pathway.
Ena/VASP regulates mDia2 (show DIAPH3 ELISA Kits)-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 ELISA Kits) resistance were recapitulated by VASP knockout, implying a role for VASP to constrain inflammatory signaling and maintain insulin (show INS ELISA Kits) 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 ELISA Kits) in NIH-Src (show SRC ELISA Kits) cells and was essential for podosome formation.
A VASP to Rac (show AKT1 ELISA Kits) 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