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).
Immunogen
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.
Application
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide
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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.
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
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
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
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
Cells must divide strictly along a plane to form an epithelial layer parallel to the basal lamina. The axis of cell division is primarily governed by the orientation of the mitotic spindle and spindle misorientation pathways have been implicated in
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