Recombinant human NEK2 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >70% purity and suitable for Inhib.
>70% SDS-PAGE
Baculovirus infected Sf9 cells
Tag free
Inhib
Yes
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application Inhib | Reactivity Reacts | Dilution info - | Notes - |
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; SGO1; 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). Phosphorylates CCDC102B either directly or indirectly which causes CCDC102B to dissociate from the centrosome and allows for centrosome separation (PubMed:30404835).Isoform 1Phosphorylates and activates NEK11 in G1/S-arrested cells.Isoform 2Not present in the nucleolus and, in contrast to isoform 1, does not phosphorylate and activate NEK11 in G1/S-arrested cells.
NEK2A, NLK1, NLK1, NEK2A, NEK2, Serine/threonine-protein kinase Nek2, HSPK 21, Never in mitosis A-related kinase 2, NimA-like protein kinase 1, NimA-related protein kinase 2
Recombinant human NEK2 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >70% purity and suitable for Inhib.
>70% SDS-PAGE
Baculovirus infected Sf9 cells
Tag free
Inhib
Yes
100 U/mg. One unit is defined as the amount of enzyme that will phosphorylate 1 nmol of myelin basic protein (MBP) substrate per minute at pH 7.4 and 30C. Assay buffer: 50 mM HEPES, pH 7.4, 3 mM MgCl2, 3 mM MnCl2, 1 mM DTT, 3 uM Naorthovanadate, 0.5 mM ATP, 0.3 mg/ml MBPsubstrate, and 0.2 ug/ml NEK2.
No
Human
pH: 8
Constituents: 40% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.395% Tris HCl, 0.05% Sorbitan monolaurate, ethoxylated, 0.0462% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Liquid
Affinity purified.
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; SGO1; 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). Phosphorylates CCDC102B either directly or indirectly which causes CCDC102B to dissociate from the centrosome and allows for centrosome separation (PubMed:30404835).
Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.
Activated by autophosphorylation. Protein phosphatase 1 represses autophosphorylation and activation of isoform 1 by dephosphorylation. Phosphorylation by STK3/MST2 is necessary for its localization to the centrosome.
Nucleus, Nucleolus, Cytoskeleton, Microtubule organizing center, Centrosome, Spindle pole
Dry Ice
-80°C
-80°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Expressed in a Baculovirus infected Sf9 cell expression system.
This supplementary information is collated from multiple sources and compiled automatically.
The cell cycle serine/threonine-protein kinase Nek2 also known as Never in Mitosis Gene A (NIMA)-related kinase 2 has a molecular weight of approximately 56 kDa. Expressed mainly in proliferating cells with high expression in the testes it primarily localizes to the centrosome and nucleus. This protein regulates centrosome separation and spindle formation. Such functions are essential for proper cell division contributing to the accurate segregation of chromosomes.
Nek2 involves key roles in cell cycle progression especially from the G2 to the M phase. It integrates into a complex regulatory network interacting with various cell division controllers. Nek2 phosphorylates centrosomal proteins which ensures timely centrosome disjunction and bipolar spindle formation. This action establishes Nek2 as important for the maintenance of genomic stability preventing abnormal cell divisions.
Nek2 fits into critical pathways that control cell division and mitosis. It operates within the PI3K/AKT pathway influencing cell growth and survival. Additionally Nek2 relates to other kinases like Aurora A kinase sharing pathway intersections that modulate centrosome dynamics and stability. These interactions reflect the significance of Nek2 in orchestrating precise mitotic events contributing to orderly cell cycle transitions.
Nek2 shows connections to cancers particularly breast and prostate cancer. Overexpression of Nek2 correlates with the pathogenesis of these cancers indicating its role in aberrant cellular proliferation. It also interacts with proteins like MAD2 which is a spindle checkpoint protein. This connection highlights Nek2's involvement in tumorigenesis through mitotic checkpoint control failure contributing to cancer cell survival and progression.
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