anti-VASP mAb (IE273)

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AdipoGen Life Sciences
Product Code: AG-20T-0002
Product Group: Primary Antibodies
CodeSizePrice
AG-20T-0002-C05050 ug£300.00
Quantity:
Prices exclude any Taxes / VAT

Overview

Antibody Clonality: Monoclonal
Regulatory Status: RUO
Target Species:
  • Bovine (Cattle)
  • Human
  • Porcine (pig)
  • Rabbit
Applications:
  • Enzyme-Linked Immunosorbent Assay (ELISA)
  • Immunocytochemistry (ICC)
  • Immunohistochemistry (IHC)
  • Immunoprecipitation (IP)
  • Western Blot (WB)
Shipping:
-20°C
Storage:
-20°C

Documents

Further Information

Alternate Names/Synonyms:
Vasodilator-stimulated Phosphoprotein
Concentration:
500µg/ml
EClass:
32160000
Form (Short):
liquid
Formulation:
Liquid. In PBS containing 2mg/ml BSA and 0.02% sodium azide.
Handling Advice:
Avoid freeze/thaw cycles.
Immunogen:
Purified human VASP.
Long Description:
Monoclonal Antibody. Recognizes both the 46kDa (Ser157 dephospho-) and 50kDa (Ser157 phospho-) form of human, porcine, bovine, sheep and rabbit VASP. Isotype: Mouse IgG1. Clone: IE273. Applications: ELISA, ICC, IHC, IP, WB. Liquid. In PBS containing 2mg/ml BSA and 0.02% sodium azide. VASP (vasodilator-stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. VASP is an actin-associated protein 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 proteins. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments and it plays a role in actin-based mobility of Listeria monocytogenes in host cells. It regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. VASP phosphorylation is used to monitor the effect of so-called antiplatelet drugs that reduce platelet reactivity and are used to prevent stent thrombosis, strokes and heart attacks in patients. Phosphorylation of VASP at Ser157 causes a mobility shift in SDS gel electrophoresis from 46 to 50kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity.
NCBI, Uniprot Number:
P50552
Package Type:
Plastic Vial
Product Description:
VASP (vasodilator-stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. VASP is an actin-associated protein 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 proteins. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments and it plays a role in actin-based mobility of Listeria monocytogenes in host cells. It regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. VASP phosphorylation is used to monitor the effect of so-called antiplatelet drugs that reduce platelet reactivity and are used to prevent stent thrombosis, strokes and heart attacks in patients. Phosphorylation of VASP at Ser157 causes a mobility shift in SDS gel electrophoresis from 46 to 50kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity.
Purity:
Protein A/G purified.
Specificity:
Recognizes both the 46kDa (Ser157 dephospho-) and 50kDa (Ser157 phospho-) form of human, porcine, bovine, sheep and rabbit VASP.
Transportation:
Non-hazardous
UNSPSC Category:
Primary Antibodies
UNSPSC Number:
12352203
Use & Stability:
Stable for at least 1 year after receipt when stored at -20°C.

References

The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences: A. Lambrechts, et al.; EMBO J. 16, 484 (1997) | A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family: K. Niebuhr, et al.; EMBO J. 16, 5433 (1997) | The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation: C. Bachmann, et al.; J. Biol. Chem. 274, 23549 (1999) | Vasodilator-Stimulated Phosphoprotein Serine 239 Phosphorylation as a Sensitive Monitor of Defective Nitric Oxide/cGMP Signaling and Endothelial Dysfunction: M. Oelze, et al.; Circ. Res. 87, 999 (2000) | Effects of In Vivo Nitroglycerin Treatment on Activity and Expression of the Guanylyl Cyclase and cGMP-Dependent Protein Kinase and Their Downstream Target Vasodilator-Stimulated Phosphoprotein in Aorta: A. Muelsch, et al.; Circulation 103, 2188 (2001) | Effects of angiotensin II infusion on the expression and function of NAD(P)H oxidase and components of nitric oxide/cGMP signaling: H. Mollnau, et al.; Circ. Res. 90, E58 (2002) | Phosphorylation of blood vessel vasodilator-stimulated phosphoprotein at serine 239 as a functional biochemical marker of endothelial nitric oxide/cyclic GMP signaling: C. Ibarra-Alvarado, et al.; Mol Pharmacol. 61, 312 (2002) | Changes of vasodilator-stimulated phosphoprotein (VASP) and its phosphorylation in endothelial cells exposed to laminar flow: L. Wei, et al.; Clin. Hemorheol. Microcirc. 28, 113 (2003) | Linked regulation of motility and integrin function in activated migrating neutrophils revealed by interference in remodelling of the cytoskeleton: S.I. Anderson, et al.; Cell Motil. Cytoskeleton 54, 135 (2003) | Monitoring of clopidogrel action: comparison of methods: J. Geiger, et al.; Clin. Chem. 51, 957 (2005) | VASP-dependent regulation of actin cytoskeleton rigidity, cell adhesion, and detachment: A.B. Galler, et al.; Histochem. Cell Biol. 125, 457 (2006) | AMP-activated protein kinase impairs endothelial actin cytoskeleton assembly by phosphorylating vasodilator-stimulated phosphoprotein: C. Blume, et al.; J. Biol. Chem. 282, 4601 (2007) | Cytoskeleton assembly at endothelial cell-cell contacts is regulated by alphaII-spectrin-VASP complexes: P.M. Benz, et al.; J. Cell. Biol. 180, 205 (2008) | Promotion of PDGF-induced endothelial cell migration by phosphorylated VASP depends on PKA anchoring via AKAP: D. Zhang, et al.; Mol. Cell. Biochem. 335, 1 (2010) | A protein phosphorylation-based assay for screening and monitoring of drugs modulating cyclic nucleotide pathways: J. Geiger, et al.; Anal. Biochem. 407, 261 (2010) | Apotential role for alpha-actinin in inside-out alphaIIbbeta3 signaling: S. Tadokoro, et al.; Blood 117, 250 (2011) | Proteomic signature of thrombin-activated platelets after in vivo nitric oxide-donor treatment: coordinated inhibition of signaling (phosphatidylinositol 3-kinase-gamma, 14-3-3zeta, and growth factor receptor-bound protein 2) and cytoskeleton protein translocation: E. Pena, et al.; Arterioscler. Thromb. Vasc. Biol. 31, 2560 (2011) | Monomeric C-reactive protein is prothrombotic and dissociates from circulating pentameric C-reactive protein on adhered activated platelets under flow: B. Molins, et al.; Cardiovasc. Res. 92, 328 (2011)