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V3390

Sigma-Aldrich

Anti-VASP (C-terminal) antibody produced in rabbit

~1.5 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-Vasodilator-stimulated phosphoprotein

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

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 ~46 kDa

Espèces réactives

canine, human, rat

Concentration

~1.5 mg/mL

Technique(s)

indirect immunofluorescence: 5-10 μg/mL using MDCK cells
western blot: 0.5-1 μg/mL using K562, Rat2 and MDCK cell lysates

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... VASP(7408)

Description générale

VASP (vasodilator stimulated phosphoprotein) 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.

Application

Anti-VASP (C-terminal) antibody produced in rabbit has been used in immunoblotting and immunofluorescence.

Actions biochimiques/physiologiques

VASP (vasodilator stimulated phosphoprotein) 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.
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.

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

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Laura E McCormick et al.
Journal of cell science, 137(2) (2024-01-26)
The actin cytoskeleton performs multiple cellular functions, and as such, actin polymerization must be tightly regulated. We previously demonstrated that reversible, non-degradative ubiquitylation regulates the function of the actin polymerase VASP in developing neurons. However, the underlying mechanism of how
Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions
Albiges-Rizo C, et al.
Journal of Cell Science, 122(17), 3037-3049 (2009)
Genomic alterations identified by array comparative genomic hybridization as prognostic markers in tamoxifen-treated estrogen receptor-positive breast cancer
Han W
BMC Cancer (2006)
Vasodilator-stimulated phosphoprotein: crucial for activation of Rac1 in endothelial barrier maintenance
Schlegel N and Waschke J
Cardiovascular Research (2010)
Punsiri M Colonne et al.
PLoS pathogens, 12(10), e1005915-e1005915 (2016-10-07)
Coxiella burnetii is an intracellular bacterial pathogen that causes human Q fever, an acute flu-like illness that can progress to chronic endocarditis and liver and bone infections. Humans are typically infected by aerosol-mediated transmission, and C. burnetii initially targets alveolar

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