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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

Synonym(s):

Anti-Vasodilator-stimulated phosphoprotein

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~46 kDa

species reactivity

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... VASP(7408)

General description

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.

Biochem/physiol Actions

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.

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

12 - Non Combustible Liquids

WGK

nwg

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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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)
Ena/VASP Is Required for neuritogenesis in the developing cortex
Kwiatkowski AV, et al.
Neuron, 56(3), 441-455 (2007)

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