商品编号


AG-20T-0002-C050



品牌


Adipogen



公司


Adipogen



公司分类


Antibodies



Size

50 ?g


商品信息


More Information



Product Details



Synonyms

Vasodilator-stimulated Phosphoprotein



Product Type

Monoclonal Antibody



Properties



Clone

IE273



Isotype

Mouse IgG1



Immunogen/Antigen

Purified human VASP.



Application


ELISA
Immunocytochemistry:
(1-5μg/ml, 1:100-1:500)

Immunohistochemistry
Immunoprecipitation

Western Blot:
(0.01-0.25μg/ml, 1:2000-1:50'000)
Optimal conditions must be determined individually for each application.



Crossreactivity

Bovine
Human
Pig
Rabbit
Sheep



Specificity

Recognizes both the 46kDa (Ser
157
dephospho-) and 50kDa (Ser
157
phospho-) form of human, porcine, bovine, sheep and rabbit VASP.



Purity

Protein A/G purified.



Concentration

500μg/ml



Formulation

Liquid. In PBS containing 2mg/ml BSA and 0.02% sodium azide.



Other Product Data


Contains Positive Control:
Human platelet protein (500?g) (Prod. No. AG-35T-0001), supplied at 5mg/ml in SDS-stop solution (100mM NaCl, 73mM Tris/HCl pH 6.7, 10mM DTT, 8mM EDTA, 5% [v/v] glycerol, 2% [w/v] SDS, 10μg/ml bromophenol blue sodium salt). Use 5μl (25μg) per lane.



Accession Number

UniProt ID P50552: VASP



Shipping and Handling



Shipping

BLUE ICE



Short Term Storage

+4°C



Long Term Storage

-20°C



Handling Advice

Avoid freeze/thaw cycles.



Use/St
ABI
lity

Stable for at least 1 year after receipt when stored at -20°C.



Documents



MSD
S


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Product Specification Sheet



Datasheet


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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.


Product 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 αII-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 α-actinin in inside-out αIIbβ3 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-γ, 14-3-3ζ, 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)