Anti-NEK2

In 1X PBS, pH 7.4, with 0.09% sodium azide. NEK2 is closely related in its catalytic domain to the serine/threonine protein kinase NIMA of Aspergillus nidulans which is required for entry into mitosis and may function in parallel to the universal mitotic inducer p34cdc2. Like NIMA, the Nek2 protein is almost undetectable during G1 but accumulates progressively throughout S, reaching maximal levels in late G2. These observations demonstrate that NEK2 resembles Aspergillus NIMA, both in its catalytic domain, and cell cycle-dependent expression. Recombinant NEK2 is active as a serine/threonine-specific protein kinase and may undergo autophosphorylation. Both human NEK2 and fungal NIMA phosphorylate a similar, but not identical, set of proteins and synthetic peptides. NEK2 is shown to be expressed most abundantly in adult testis and there is increasing evidence that NEK2 is abnormally expressed in a wide variety of human cancers. This antibody is specific to isoform 2 of NEK2. Protein function: Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC, SGOL1, NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (PubMed:24554434). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (PubMed:25704143). Involved in the regulation of centrosome disjunction (PubMed:26220856). [The UniProt Consortium]