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Merck

V3390

Sigma-Aldrich

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

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

别名:

Anti-Vasodilator-stimulated phosphoprotein

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About This Item

分類程式碼代碼:
12352203
NACRES:
NA.41

生物源

rabbit

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

形狀

buffered aqueous solution

分子量

antigen ~46 kDa

物種活性

canine, human, rat

濃度

~1.5 mg/mL

技術

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

UniProt登錄號

運輸包裝

dry ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

human ... VASP(7408)

一般說明

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.

應用

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

生化/生理作用

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.

外觀

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

免責聲明

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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儲存類別代碼

12 - Non Combustible Liquids

水污染物質分類(WGK)

nwg

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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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
Genomic alterations identified by array comparative genomic hybridization as prognostic markers in tamoxifen-treated estrogen receptor-positive breast cancer
Han W
BMC Cancer (2006)
Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions
Albiges-Rizo C, et al.
Journal of Cell Science, 122(17), 3037-3049 (2009)
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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