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VASP (Ab-239) Antibody

  • 货号：
    CSB-PA206698
  • 规格：
    ￥2024
  • 图片：
    • Western blot analysis of extracts from 293 and C6 cells using VASP(Ab-239) Antibody.
  • 其他：

产品详情

  • 产品名称：
    Rabbit anti-Homo sapiens (Human) VASP Polyclonal antibody
  • Uniprot No.：
    P50552
  • 基因名：
  • 宿主：
    Rabbit
  • 反应种属：
    Human,Mouse
  • 免疫原：
    Peptide sequence around aa. 236~240 (K-V-S-K-Q) derived from Human VASP.
  • 免疫原种属：
    Homo sapiens (Human)
  • 克隆类型：
    Polyclonal
  • 纯化方式：
    Antibodies were produced by immunizing rabbits with synthetic peptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific peptide.
  • 浓度：
    It differs from different batches. Please contact us to confirm it.
  • 产品提供形式：
    Liquid
  • 应用范围：
    ELISA,WB
  • 推荐稀释比：
    Application Recommended Dilution
    WB 1:500-1:1000
  • Protocols：
  • 储存条件：
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 货期：
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

产品评价

靶点详情

  • 功能：
    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.
  • 基因功能参考文献：
    1. VASP role in the actin filament elongation PMID: 28667124
    2. Our results reveal a dual role of VASP in endothelial permeability. In addition to its well-documented function in barrier integrity, we show that S-nitrosylation of VASP contributes to the onset of endothelial permeability. PMID: 28526707
    3. findings have uncovered a PKG/VASP signaling pathway in Vascular Smooth Muscle Cells as a key molecular mechanism underlying T3-induced vascular relaxation. PMID: 28376489
    4. This study provides the first evidence of VASP manipulation by an intravacuolar bacterial pathogen PMID: 27711191
    5. VASP silencing downregulated Migfilin, beta-catenin and uPA and impaired spheroid invasion. PMID: 28209486
    6. VASP phosphorylation assay could be useful in studies aimed at investigating relations between clopidogrel active metabolite bioavailability and clinical events. PMID: 26576037
    7. VASP, zyxin and TES are tension-dependent members of focal adherens junctions independent of the alpha-catenin-vinculin module. PMID: 26611125
    8. 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. PMID: 26336132
    9. The s propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their actin polymerase activity by tethering them to actin filaments. PMID: 26295568
    10. Data show that tumor necrosis factor-alpha (TNF-alpha) increased A549 lung adenocarcinoma cell permeability by repressing vasodilator-stimulated phosphoprotein (VASP) expression through the activation of hypoxia inducible factor 1 alpha subunit (HIF-1alpha). PMID: 25051011
    11. The s 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. PMID: 25298072
    12. Ena/VASP's ability to bind F-actin and profilin-complexed G-actin are important for its effect, whereas Ena/VASP tetramerization is not necessary. PMID: 25355952
    13. In clinical practice,LCR and CYP2C19 gene polymorphism should be assessed in NCIS patients receiving clopidogrel treatment. PMID: 25457586
    14. 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 PMID: 25759389
    15. PKA regulates VASP phosphorylation in Ras-transformed cells in a non-cell-autonomous manner. PMID: 24963131
    16. Serine phosphorylation of vasodilator-stimulated phosphoprotein (VASP) regulates colon cancer cell survival and apoptosis. PMID: 25543053
    17. VASP reconstitution of actin-based motility depends on the recruitment of F-actin seeds from the solution produced by cofilin PMID: 25246528
    18. low serum concentration of vaspin is a risk factor for the progression of T2DM PMID: 24732788
    19. palladin functions as a dynamic scaffolding protein that promotes the assembly of dorsal stress fibers by recruiting VASP to these structures. PMID: 24496446
    20. Overexpression of VASP in endothelial cells blocked inflammation and insulin resistance induced by palmitate. PMID: 25117404
    21. Results show that NPs, possibly through the clearance receptor (natriuretic peptide receptor-C) expressed on platelet membranes, increase VASP phosphorylation but only following PDE inhibition, indicating a small, localised cGMP synthesis. PMID: 23469931
    22. Binding of tetrameric VASP to interleukin-1 receptor-associated kinase (IRAK)1 is regulated by assembly of IRAK1 onto signaling complexes. PMID: 24857403
    23. Matrine modulates the structure, subcellular distribution, expression and phosphorylation of VASP in human gastric cancer cells, thus inhibiting cancer cell adhesion and migration. PMID: 23685951
    24. PKD1 directly phosphorylates VASP at two serine residues, Ser-157 and Ser-322. These phosphorylations occur in response to RhoA activation and mediate VASP re-localization from focal contacts to the leading edge region. PMID: 23846685
    25. Letter: In High on-treatment platelet reactivity assessed by various platelet function tests the consensus-defined cut-off of VASP-P platelet reactivity index too low. PMID: 22212857
    26. Active proteases in nephrotic plasma lead to a podocin-dependent phosphorylation of VASP in podocytes via protease activated receptor-1. PMID: 23436459
    27. VASP participates in the regulation of cell cytoskeleton reorganization and morphology modification induced by shear flow via a cAMP/cAK pathway. PMID: 21158099
    28. a novel TNF-alpha/HIF-1alpha/VASP axis in which HIF-1alpha acts downstream of TNF-alpha to inhibit VASP expression and modulate the adhesion and proliferation of breast cancer cells PMID: 22320863
    29. Membrane organelle disassembly reflected specific phosphorylation of VASP Ser239, the cGMP/PKG preferred site, and rapid VASP removal from tumor cell protrusions PMID: 21702043
    30. Prolonged treatment with albuterol prevents the agonist-induced phosphorylation of VASP at Ser157. PMID: 22210825
    31. The phosphorylation and dephosphorylation cycle of VASP by the Abi-1-bridged mechanism regulates association of VASP with focal adhesions, which may regulate adhesion of Bcr-Abl-transformed leukaemic cells. PMID: 22014333
    32. The Ser-239 phosphorylation level of VASP might be a useful protein marker for riboflavin and UV light-mediated PLT compromise. PMID: 21827504
    33. ENA/VASP-family proteins are functionally redundant in homologous recombination, and MENA, VASP and EVL may be involved in the DSB repair pathway in humans PMID: 21398369
    34. VASP protein regulates osteosarcoma cell migration and metastasis PMID: 21874265
    35. Studied generation of filopodia with regards to the dynamic interaction established by Eps8, IRSp53 and VASP with actin filaments. PMID: 21814501
    36. Data show that VASP and Mena interact with RSK1. PMID: 21423205
    37. Data show that VASP has different immunostaining patterns between cerebral cortical plates in prenatal and adult human brain samples, and suggest that VASP may play a crucial role in the regulation of human neonatal cerebral cortical development. PMID: 21163344
    38. VASP deficiency leads to a more profound endothelial barrier disruption and delayed recovery after activation of thrombin PAR-1 receptor. PMID: 20945373
    39. vasodilator-stimulated phosphoprotein is phosphorylated in patients with genetic defects of the platelet P2Y(12) receptor for ADP PMID: 20695985
    40. High VASP expression is associated with focal adhesion assembly in myofibroblasts fostering a microenvironment that promotes tumor growth. PMID: 20802179
    41. Results describe the impact of smoking on platelet reactivity and phosphorylation of vasodilator-stimulated phosphoprotein (VASP) in a group of 20 young smokers. PMID: 20822337
    42. Results suggest that actin polymerization and bundling by VASP are critical for spine formation, expansion, and modulating synaptic strength. PMID: 20826790
    43. peroxynitrite may inhibit platelet function by inducing the phosphorylation of VASP through a mechanism that requires the activation of PKC. PMID: 20624010
    44. presentation of a model for how VASP promotes actin filament assembly PMID: 21041447
    45. Letter: Report vasodilator-stimulated phosphoprotein (VASP) ELISA to evaluate P2Y12-ADP receptor activity in coronary artery disease patients taking antiplatelet agents. PMID: 20589315
    46. Platelet hyperreactivity in multiple electrode aggregometry might be a better risk predictor for stent thrombosis than the assessment of the specific clopidogrel effect with the VASP phosphorylation assay. PMID: 19943879
    47. Combination of experimental and computational interactome research was used for the analysis of protein-protein interactions between Abi-1 and VASP in human platelets. PMID: 20110575
    48. Compared clopidogrel effectiveness in unstable ST-elevation myocardial infarction (STEMI) patients on mechanical ventilation with stable STEMI patients using the VASP index. PMID: 19902490
    49. IRAK-1 forms a close complex with PKCepsilon as well as VASP, and participates in phorbol 12-myristate 13-acetate-induced phosphorylation of VASP. PMID: 20044140
    50. VASP phosphorylation controls remodeling of the actin cytoskeleton. PMID: 19825941

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  • 亚细胞定位：
    Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell junction, tight junction. Cell projection, lamellipodium membrane. Cell projection, filopodium membrane. Note=Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions. In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes).
  • 蛋白家族：
    Ena/VASP family
  • 组织特异性：
    Highly expressed in platelets.
  • 数据库链接：

    HGNC: 12652

    OMIM: 601703

    KEGG: hsa:7408

    STRING: 9606.ENSP00000245932

    UniGene: Hs.515469