|Other Names||Aurora kinase A, Aurora 2, Aurora/IPL1-related kinase 1, ARK-1, Aurora-related kinase 1, hARK1, Breast tumor-amplified kinase, Serine/threonine-protein kinase 15, Serine/threonine-protein kinase 6, Serine/threonine-protein kinase aurora-A, AURKA|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7002c was selected from the C-term region of human Aurora-A. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis.|
|Cellular Location||Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Note=Detected at the neurite hillock in developing neurons (By similarity). Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase. Colocalized with SIRT2 at centrosome. Moves to the midbody during both telophase and cytokinesis. Associates with both the pericentriolar material (PCM) and centrioles.|
|Tissue Location||Highly expressed in testis and weakly in skeletal muscle, thymus and spleen. Also highly expressed in colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines|
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Provided below are standard protocols that you may find useful for product applications.
Chromosomal segregation during mitosis as well as meiosis is regulated by kinases and phosphatases. The Aurora kinases, members of the Ser/Thr protein kinase family, associate with microtubules during chromosome movement and segregation. Auroria kinase A may play a role in cell cycle regulation during anaphase and/or telophase, in relation to the function of the centrosome/spindle pole region during chromosome segregation. It may be involved in microtubule formation and/or stabilization. This protein has also been postulated to play a key role during tumor development and progression. Aurora kinase A localizes on centrosomes in interphase cells and at each spindle pole in mitosis. It is highly expressed in testis, weakly in skeletal muscle, thymus and spleen, and also highly expressed in colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines. Expression is cell-cycle regulated, low in G1/S, accumulates during G2/M, and decreases rapidly afterward. Defects in Aurora kinase A are responsible for numerical centrosome aberrations including aneuploidy.
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).Tanaka, M., et al., J. Biol. Chem. 277(12):10719-10726 (2002).Nigg, E.A., Nat. Rev. Mol. Cell Biol. 2(1):21-32 (2001).Deloukas, P., et al., Nature 414(6866):865-871 (2001).Shindo, M., et al., Biochem. Biophys. Res. Commun. 244(1):285-292 (1998).
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