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rabbit
Mono-/polyclonal:
polyclonal (pAB) | anti-(full-length protein)
Purity:
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Quantity (mass):
n/a
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polyclonal (pAB) | anti-(full-length protein)
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rabbit
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polyclonal (pAB) | anti-(full-length protein)
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250 µl
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Article #:
0010-10
Antigen/Product:
VASP, vasodilator stimulated phosphoprotein
Synonym(s):
VASP, vasodilator-stimulated phosphoprotein
Uni-/SwissProt #:

P50552, B2RBT9, Q6PIZ1, Q93035

Clone / Name:
M4
Host Species:
rabbit
Mono-/polyclonal:
polyclonal (pAB) | anti-(full-length protein)
Purity:
serum
Quantity (mass):
n/a
Quantity (vol.):
100 µl
Price (net):
sold out, replaced by affinity purified antibody IG-731
Cross-reactivity:
human, mouse, rat, dog, pig, chicken, marsupial (PtK2)
included:
free positive control: human platelet protein (lysate)
Applications:
WB - Western blot / immunoblot, IF - immunofluorescence, IP - immunoprecipitation
Sugg. dilutions:
WB: 1:3,000; IF: 1:500; IP: 1:125
Fixatives tested:
formaldehyde, acetone
Remarks:

The antibody recognizes both the 46 kDa (Ser-157 dephospho) and 50 kDa (Ser-157 phospho) form of VASP.

immunoGlobe VASP Antibodies in Basic and Clinical Research

Form:
sterile filtered liquid, with sodium azide
Immunization:
natural protein
Storage:
-20°C
Shipping:
RT - ambient temperature
Availability:
sold out
Data sheet:
Figure(s):
Vasp blotVasp fibroblast<p>(Modified from EMBO J. 11:2063-2070; by permission of Oxford University Press)</p>Vasp shiftVasp zzk
Publications referring to this product:
  • Reinhard et al. (1997) VASP. Guidebook to the cytoskeleton and motor proteins. Kreis T. & Vale R. (eds.), p.168-171.
  • Dutartre et al. (1996) Cytokinesis arrest and redistribution of actin cytoskeleton regulatory components in cells expressing the Rho GTPase CDC42HS. J. Cell Sci. 109:367-377.
  • Gerstel et al. (1996) The ActA polypeptides of Listeria ivanovii and Listeria monocytogenes harbor related
    binding sites for host microfilament proteins. Infect. Immunit. 64:1929-1936.
  • Gertler et al. (1996) Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics. Cell 87:227-239.
  • Reinhard et al. (1996) VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs. FEBS Lett. 399:103-107.
  • Markert et al. (1996) High expression of the focal adhesion and microfilament associated protein VASP in vascular smooth muscle and endothelial cells of the intact human vessel wall. Basic Res. Cardiol. 91:337-343.
    Abel et al. (1995) Dephosphorylation of the focal adhesion protein VASP in vitro and in intact human platelets. FEBS Lett. 370:184-188.
  • Chakraborty et al. (1995) A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells. EMBO J. 14,1314-1321.
  • Draijer et al. (1995) Expression of cGMP-dependent protein kinase I and phosphorylation of its substrate, vasodilator-stimulated phosphoprotein, in human endothelial cells of different origin. Circ. Res. 77:897-905.
  • Haffner et al. (1995) Molecular cloning, structural analysis, and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP. EMBO J. 14:19-27.
  • Pistor et al. (1995) The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins. Curr. Biol. 5:517-525.
  • Reinhard et al. (1995) The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. EMBO J. 14:1583-1589.
  • Reinhard et al. (1995) Identification, purification, and characterization of a zyxin-related protein which binds the focal adhesion and microfilament protein VASP. Proc. Natl. Acad. Sci. USA 92:7956-7960.
  • Butt et al. (1994) cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets. J. Biol. Chem. 269:14509-14517.
  • Horstrup et al. (1994) Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition. Eur. J. Biochem. 225:21-27.
  • Nolte et al. (1994) Synergistic phosphorylation of the focal adhesion-associated Vasodilator-stimulated phospho-protein in intact human platelets in response to cGMP- and cAMP-elevating platelet inhibitors. Biochem. Pharmacol. 48:1569-1575.
  • Pohl et al. (1994) Endothelium-dependent phosphorylation of vasodilator-stimulated protein in platelets during coronary passage. Am. J. Physiol. 266:H606-612.
  • Eigenthaler et al. (1993) Defective nitrovasodilatorstimulated protein phosphorylation and calcium regulation in cGMP-dependent protein kinase-deficient human platelets of chronic myelocytic leukemia. J. Biol. Chem. 268:13526-31.
  • Walter et al. (1993) Role of cyclic nucleotide-dependent protein kinases and their common substrate VASP in
    the regulation of human platelets. Adv. Exp. Med. Biol. 344:237-249.
  • Eigenthaler et al.(1992) Concentration and regulation of cyclic nucleotides, cyclic-nucleotide-dependent protein kinases and one of their major substrates in human platelets. Estimating the rate of cAMP-regulated and cGMP-regulated protein phosphorylation in intact cells. Eur. J. Biochem. 205:471-481.
  • Geiger et al. (1992) Role of cGMP and cGMPdependent protein kinases in nitrovasodilator inhibition of agonist-evoked calcium elevation in human platelets. Proc. Natl. Acad. Sci. USA 89:1031-1035.
  • Halbrügge et al. (1992) Protein phosphorylation regulated by cyclic nucleotide-dependent protein kinases in cell extracts and in intact human lymphocytes. Cell. Signalling 4:189-199.
  • Reinhard et al. (1992) The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. EMBO J. 11:2063-2070.
  • Nolte et al. (1991) Comparison of vasodilatory prostaglandins with respect to cAMP-mediated phosphorylation of a target substrate in intact human platelets. Biochem. Pharmacol. 42:253-262.
  • Nolte et al. (1991) Endothelial cell-dependent phosphorylation of a platelet protein mediated by cAMP and cGMP-elevating factors. J. Biol. Chem. 266:14808-14812.
  • Sandberg et al. (1991) Characterization of Sp-5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole-3´,5´-monophosphorothioate (Sp-5,6-DCl-cBiMPS) as a potent and specific activator of cyclic-AMP-dependent protein kinase in cell extracts and intact cells. Biochem. J. 279:521-527.
  • Halbrügge et al. (1990) Stoichiometric and reversible phosphorylation of a 46 kDa protein in human platelets
    in response to cGMP- and cAMP-elevating vasodilators. J. Biol. Chem. 265:3088-3093.
  • Halbrügge & Walter (1990) Analysis, purification and properties of a 50,000-dalton membrane-associated phosphoprotein from human platelets. J. Chromatogr. 521:335-343.
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