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Merck
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重要文件

A1226

Sigma-Aldrich

Anti-Actopaxin antibody produced in rabbit

IgG fraction of antiserum, PBS solution

同義詞:

Anti-α-Parvin, Anti-CH-ILKBP

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About This Item

MDL號碼:
分類程式碼代碼:
12352203
NACRES:
NA.46

生物源

rabbit

品質等級

共軛

unconjugated

抗體表格

IgG fraction of antiserum

抗體產品種類

primary antibodies

無性繁殖

polyclonal

形狀

PBS solution

分子量

antigen 42 kDa

物種活性

human, mouse

技術

microarray: suitable
western blot: 1:3,000 using whole cell extract of the human endothelial ECV304 cell line.

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 ... PARVA(55742)
mouse ... Parva(57342)

相關類別

一般說明

Actopaxin is a member of actin binding proteins that include beta-parvin/affixin and gamma-parvin. Actopaxin is known to associate with F-actin and paxillin LD motifs LD1 and LD4. This protein also directly binds to serine/threonine integrin-linked kinase (ILK). Studies have reported that actopaxin may be involved in integrin-dependent remodeling of the actin cytoskeleton during cell adhesion, motility and division.
Rabbit anti-actopaxin recognizes actopaxin (42 kDa). Staining of actopaxin in immunoblotting is specifically inhibited with actopaxin immunizing peptide (mouse, amino acids 35-53).

免疫原

synthetic peptide corresponding to the N-terminal region of mouse actopaxin (amino acids 35-53). The sequence is identical in human actopaxin and has considerable homology (~70%) with β-parvin/affixin, but no homology with γ-parvin.

應用

Actopaxin was detected in HEK 293 cell lysates at 42 kDa by western blot using rabbit anti-actopaxin antibody at a 1:1000 dilution. In these cells, actopaxin associated with an ILK complex.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Rabbit anti-actopaxin can also be used for protein microaarays.

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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S Yamaji et al.
The Journal of cell biology, 153(6), 1251-1264 (2001-06-13)
Focal adhesions (FAs) are essential structures for cell adhesion, migration, and morphogenesis. Integrin-linked kinase (ILK), which is capable of interacting with the cytoplasmic domain of beta1 integrin, seems to be a key component of FAs, but its exact role in
Thitima Keskanokwong et al.
The Journal of biological chemistry, 282(32), 23205-23218 (2007-06-08)
Kidney anion exchanger 1 (kAE1) mediates chloride/bicarbonate exchange at the basolateral membrane of kidney alpha-intercalated cells, thereby facilitating bicarbonate reabsorption into the blood. Human kAE1 lacks the N-terminal 65 residues of the erythroid form (AE1, band 3), which are essential
Sotiris N Nikolopoulos et al.
The Journal of biological chemistry, 277(2), 1568-1575 (2001-11-06)
Paxillin is a focal adhesion adapter protein involved in integrin signaling. We have recently reported that the paxillin LD1 motif acts as a binding interface for both the actin-binding protein actopaxin and the serine/threonine integrin-linked kinase (ILK). In this report
Iveta Dobreva et al.
Journal of proteome research, 7(4), 1740-1749 (2008-03-11)
Protein-protein interactions play an essential role in the regulation of vital biological functions. Through a network of interactions, integrin-linked kinase (ILK) functions downstream of integrin receptors to control cell spreading, migration, growth, survival, and cell cycle progression. Despite many reports
T M Olski et al.
Journal of cell science, 114(Pt 3), 525-538 (2001-02-15)
We have identified and cloned a novel 42-kDa protein termed alpha-parvin, which has a single alpha-actinin-like actin-binding domain. Unlike other members of the alpha-actinin superfamily, which are large multidomain proteins, alpha-parvin lacks a rod domain or any other C-terminal structural

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