|Application ||WB, IF|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||42330 Da|
|Other Names||Alpha-parvin, Actopaxin, Parva, Actp|
|Target/Specificity||A phospho specific peptide corresponding to residues surrounding serine 8 of human Parvin was used as an immunogen. This antibody detects Actopaxin phosphorylated on serine 8.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Actopaxin/Parvin Antibody Phospho (pS8) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development.|
|Cellular Location||Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line Note=Constituent of focal adhesions|
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Provided below are standard protocols that you may find useful for product applications.
Actopaxin (also named Parvin, Parva) is a member of the alpha actinin superfamily containing a single alpha-actinin-like actin-binding domain. The Parvin family plays a role in cell adhesion and cytoskeleton organization. Analysis of Actopaxin and its para- and orthologues suggest, that the parvins represent a new family of alpha-actinin-related proteins that mediate cell-matrix adhesion (1). Actopaxin is a widely expressed protein that binds directly to both F-actin and paxillin LD1 and LD4 motifs. It exhibits robust focal adhesion localization in several cultured cell types, but it is not found along the length of the associated actin-rich stress fibers. Actopaxin colocalizes with paxillin to rudimentary focal complexes at the leading edge of migrating cells. Results suggest an important role for actopaxin in integrin-dependent remodeling of the actin cytoskeleton during cell motility and cell adhesion (2).
1. Olski TM et al. J Cell Sci 114(Pt.3):525-38, 2001
2. Nikolopoulos SN et al. J Cell Biol 151(7) :1435-48, 2000
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