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Aurora B kinase is a serine/threonine protein kinase involved in the regulation of mitosis.1 It is composed of an N-terminal regulatory domain containing KEN- and A-box motifs, which regulate degradation of Aurora B, and a C-terminal catalytic domain containing an activation loop and a D-box, which also regulates Aurora B degradation. Aurora B kinase is ubiquitously expressed with the highest expression at the G2/M phase of the cell cycle and the highest activity during mitosis.2 It localizes to the nucleus, where it is a component of the chromosome passenger complex (CPC).3 Aurora B kinase is involved in the modification of chromatin and centromeres by phosphorylating histone H3 and centromere protein A (CENP-A), respectively, during mitosis.1,3 It is also involved in chromatid separation, by phosphorylating mitotic centromere-associated kinesin (MCAK) to stabilize kinetochore-microtubule attachments, and in the regulation of cytokinesis.1 AURKB, the gene encoding aurora B kinase, is overexpressed in a variety of cancers and its expression levels are positively correlated with disease severity, poor prognosis, and lower overall survival.2 Cayman's Aurora B Kinase (N-Term) Rabbit Monoclonal Antibody (Clone RM278) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. Roles of Aurora kinases in mitosis and tumorigenesis. Mol. Cancer Res. 5(1), 1-10 (2007).
2. Aurora B: A new prognostic marker and therapeutic target in cancer. Curr. Med. Chem. 18(4), 482-496 (2011).
3. Aurora kinases. Curr. Biol. 18(4), R146-148 (2008).