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Key Documents

SAB4200555

Sigma-Aldrich

Anti-phospho-VASP [pSer239] antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonyme(s) :

Anti-Vasodilator-stimulated phosphoprotein

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.44

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~50 kDa

Espèces réactives

rat, human, mouse, dog

Concentration

~1.0 mg/mL

Technique(s)

indirect immunofluorescence: 1-2 μg/mL using MDCK cells
western blot: 1-2 μg/mL using HEK-293T, NIH-3T3 and Rat2 cell extracts

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

phosphorylation (pSer239)

Informations sur le gène

human ... VASP(7408)
mouse ... Vasp(22323)
rat ... Vasp(361517)

Description générale

Monoclonal Anti-WASH1 (mouse IgG1 isotype) is derived from the hybridoma WASH1-27 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to an internal region of human WASH1. VASP (vasodilator-stimulated phosphoprotein) belongs to the family of Ena/VASP actin-regulatory proteins. VASP is localized at highly dynamic membrane regions, focal adhesion sites, lamellipodia protrusions, filopodia tips and along stress fibers.

Immunogène

synthetic peptide containing phosphorylated Ser239 of human VASP conjugated to KLH. The corresponding sequence is identical in mouse and rat VASP.

Application

Anti-phospho-VASP [pSer239] antibody produced in rabbit has been used in:
  • immunoblotting
  • immunoprecipitation
  • immunofluorescence

Actions biochimiques/physiologiques

VASP (vasodilator-stimulated phosphoprotein) is implicated in cell motility and adhesion. VASP is localized at cell matrix and cell-cell contacts and plays an important role in adherens junction formation and stabilization in epithelial cells. VASP is a substrate for cAMP- and cGMP-dependent protein kinases. It is phosphorylated at multiple sites including Ser157, Ser239 and Thr278. cGMP-dependent protein kinase I (cGKI) phosphorylates VASP in a variety of cells, including platelets, fibroblasts and endothelial cells. In platelets, cGMP-mediated phosphorylation of VASP correlates with inhibition of agonist-induced platelet aggregation. Ena/VASP proteins are required for neurite initiation and extension in the developing cortex. VASP has been shown to be required for endothelial barrier function in vivo. Knockout of Ena/VASP proteins in mice leads to increased endothelial permeability causing fatal vascular leakage and haemorrhaging during late embryonic development. In contrast, overexpression of VASP enhances barrier function of endothelial cells in vitro and increases their force generation.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Ena/VASP is required for endothelial barrier function in vivo
Furman C, et al.
The Journal of Cell Biology, 179(4), 761-775 (2007)
Ena/VASP proteins: regulators of the actin cytoskeleton and cell migration
Krause M, et al.
Annual Review of Cell and Developmental Biology, 19(1), 541-564 (2003)
Ena/VASP Is Required for neuritogenesis in the developing cortex
Kwiatkowski AV, et al.
Neuron, 56(3), 441-455 (2007)
Relaxing the actin cytoskeleton for adhesion and movement with Ena/VASP
Trichet L, et al.
The Journal of Cell Biology, 181(1), 19-25 (2008)
The vasodilator-stimulated phosphoprotein is regulated by cyclic GMP-dependent protein kinase during neutrophil spreading
Lawrence DW and Pryzwansky KB
Journal of Immunology, 166(9), 5550-5556 (2001)

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