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SAB4200555

Sigma-Aldrich

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

~1.0 mg/mL, affinity isolated antibody

Synonym(s):

Anti-Vasodilator-stimulated phosphoprotein

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.44

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~50 kDa

species reactivity

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

phosphorylation (pSer239)

Gene Information

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

Related Categories

General description

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.

Immunogen

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

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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