Phospho-Aurora A (Thr288)/Aurora B (Thr232)/Aurora C (Thr198) (CC12) rabbit mAb APC conjugate
Aurora kinases (serine/threonine kinases) are essential requirement for the onset and progression of mitosis. These kinases share a similar protein structure as well as kinase activity, however each kinase display distinct cellular and subcellular localization. Each Aurora member is phosphorylated at specific residues upon co-factor binding during mitosis. Aurora kinases acquire active kinase conformations due to the activation loop. The active kinase conformation is acquired upon auto-phosphorylation through an intermolecular (trans)-reaction within Aurora kinase domain. Aurora Kinase A (Aurora A) is involved in G2/M transition. AuroraA promotes centrosome maturation and mitotic spindle assembly, whereas AuroraB and AuroraC act as chromosome-passenger complex proteins. They play a crucial role in chromosomal binding to kinetochores and segregation of chromosomes. Aurora B is widely distributed in the cell, while AuroraC is expressed mainly in the meiotically-active germ cells. Aurora kinases are auto-phosphorylated into active forms at conserved threonine residues (i.e. the Thr288 (AurA), Thr232 (AurB) and Thr195 (AurC) residues). AuroraA auto-phosphorylation is initiated by several co-factors acting at different steps of mitosis. AroraB and AruroaC auto-phosphorylation are mediated by survivin and Borealin proteins.
|Cross Reactivity||Predicted to work with mouse, rat and other homologues.|
|Immunogen||A synthetic phospho-peptide corresponding to residues surrounding human Aurora A (Thr288)/Aurora B (Thr232)/Aurora C (Thr198)|
|Formulation||1X PBS, 0.09% NaN3, 0.2% BSA|
|Recommended Usage||For flow cytometric staining, the suggested use of this reagent is 5 µL per million cells or 5 µL per 100 µL of staining volume. It is recommended that the reagent be titrated for optimal performance for each application. See product image legends for additional information.|
|Pseudonyms||Aurora kinase A/B/C, AURKA, AURKB, AURKC|
|Uniprot ID||O14965 Q96GD4 Q9UQB9|
|References||Hochegger H, et al., (2013) Open Biol. 3:120185.
Carmena M, et al., (2009) Curr Opin Cell Biol 21:796–805.
Bolanos-Garcia VM. (2005) Int J Biochem Cell Biol. 37:1572–1577.
Kimmins S, et al., (2007) Mol Endocrinol. 2007;21(3):726–739.
Vader G, and Lens SMA. (2008) Biochim Biophys Acta. 1786:60–72.
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