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Key Documents

SAB4200280

Sigma-Aldrich

Anti-phospho-VASP [pSer157] 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

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

~50 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

western blot: 0.1-0.2 μg/mL using human platelets cell lysates

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

phosphorylation (pSer157)

Gene Information

human ... VASP(7408)

General description

VASP is localized at highly dynamic membrane regions, focal adhesion sites, lamellipodia protrusions, filopodia tips and along stress fibers. VASP is also localized at cell matrix and cell-cell contacts.
Vasodilator stimulated phosphoprotein (VASP) is encoded by the gene mapped to human chromosome 19q13.32. The encoded protein belongs to the Ena/VASP protein family. VASP is characterized with an N-terminal EVH1 domain, C-terminal EVH2 domain and proline-rich region.

Specificity

Anti-phospho-VASP [pSer157] specifically recognizes human VASP phosphorylated at Ser157.

Immunogen

synthetic peptide containing phosphorylated Ser157 of human VASP. The corresponding sequence is highly conserved (single amino acid substitution) in mouse and rat VASP.

Application

Anti-phospho-VASP [pSer157] antibody produced in rabbit is suitable for immunoblotting.

Biochem/physiol Actions

VASP plays an important role in the adherens junction formation and stabilization in epithelial cells. It is important for actin organization. VASP is a substrate for cyclic adenosine mono phosphate (cAMP) and cyclic guanosine mono phosphate (cGMP) dependent protein kinases. Ena/VASP proteins are required for neurite initiation and extension in the developing cortex. It is essential for the formation of filopodia, in a variety of cell types. 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 hemorrhaging during late embryonic development.
Vasodilator stimulated phosphoprotein (VASP) acts as an actin-polymerization regulator and plays a vital role in regulation of cell migration by interacting with Migfilin, a cell-extracellular matrix (ECM) adhesion protein. Elevated expression of VASP contributes to the development of breast cancer (BC). Hence, this protein can be used as a potential biomarker for BC metastasis. Phosphorylation of VASP by protein kinase A (PKA) at phosphorylation site S157 aids in localization of cell periphery into focal adhesions, but phosphorylation of VASP at S239 and T278 aids in regulation of F-actin assembly.

Physical form

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

Storage and Stability

Store at −20°C. For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

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

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


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Vasodilator-Stimulated Phosphoprotein Activity Is Required for Coxiella burnetii Growth in Human Macrophages
Colonne PM
PLoS Pathogens, 12 (2016)
Anita S Kris et al.
Biochemical and biophysical research communications, 375(1), 134-138 (2008-08-06)
Strengthening of cell-matrix adhesions in response to applied force has been well documented. However, while implied by various lines of evidence, the force-mediated strengthening of cell-cell adhesions has not been directly demonstrated. In the current study, we present results consistent
Genomic alterations identified by array comparative genomic hybridization as prognostic markers in tamoxifen-treated estrogen receptor-positive breast cancer
Han W
BMC Cancer (2006)
D W Lawrence et al.
Journal of immunology (Baltimore, Md. : 1950), 166(9), 5550-5556 (2001-04-21)
The expression and phosphorylation state of the vasodilator-stimulated phosphoprotein (VASP), a membrane-associated focal adhesion protein, was investigated in human neutrophils. Adhesion and spreading of neutrophils induced the rapid phosphorylation of VASP. The phosphorylation of VASP was dependent on cell spreading
J Victor Small et al.
Trends in cell biology, 12(3), 112-120 (2002-02-23)
Lamellipodia, filopodia and membrane ruffles are essential for cell motility, the organization of membrane domains, phagocytosis and the development of substrate adhesions. Their formation relies on the regulated recruitment of molecular scaffolds to their tips (to harness and localize actin

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