Phospho-Aurora A (Thr288)/Aurora B (Thr232)/Aurora C (Thr198) (CC12) rabbit mAb

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.