Description: A rapid test for detection of antibodies (IgG and IgM) for 2019-nCoV, the novel Coronavirus from the Wuhan strain. The test is easy to perform, takes 10 minutes to provide reliable results and is higly specific to the 2019-nCoV Coronavirus.

Description: A quantitative ELISA kit for measuring Human in samples from biological fluids.

Description: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, GSG2/Haspin, and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). A positive feedback between GSG2 and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. [UniProt]

Description: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, GSG2/Haspin, and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). A positive feedback between GSG2 and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. [UniProt]

Description: Chromosomal segregation during mitosis as well as meiosis is regulated by kinases and phosphatases. The Aurora kinases associate with microtubules during chromosome movement and segregation. STK12 (Aurora kinase B) localizes to microtubules near kinetochores, specifically to the specialized microtubules called K-fibers, and Aurora kinase A localizes to centrosomes

Description: Chromosomal segregation during mitosis as well as meiosis is regulated by kinases and phosphatases. The Aurora kinases associate with microtubules during chromosome movement and segregation. STK12 (Aurora kinase B) localizes to microtubules near kinetochores, specifically to the specialized microtubules called K-fibers, and Aurora kinase A localizes to centrosomes

Description: Additional name(s) for this target protein: AURKB; aurora kinase B antibody; AIK2

Description: Aurora kinase A, also called ARK1, AURKA, AIK , AURORA2 ,BTAK, PPP1R47, STK7, STK15, and STK6, is a mitotic centrosomal protein kinase. The main role of AURKA in tumor development is in controlling chromosome segregation during mitosis. Aurora A is a member of a family of mitotic serine/threonine kinases. Cell cycle and Northern blot analyses showed that peak expression of the protein occurs during the G2/M phase and then decreases. By fluorescence in situ hybridization, the gene is represented by 2 signals in chromosome bands 20q13.2-q13.3 and 1q41-q42. It is overexpressed in many human cancers. Ectopic overexpression of Aurora A in mammalian cells induces centrosome amplification, chromosome instability, and oncogenic transformation, a phenotype characteristic of loss-of-function mutations of p53. Depletion of Ajuba prevented activation of AURKA at centrosomes in late G2 phase and inhibited mitotic entry. Activation of the kinase was independently sufficient to induce rapid ciliary resorption, and AURKA acted in this process through phosphorylation of HDAC6, leading to HDAC6-dependent tubulin deacetylation and destabilization of the ciliary axoneme.

Description: Aurora kinase B, also called Aik2, AIM-1, ARK2, AurB, STK12, IPL1, PPP1R48 or STK5, localizes to microtubules near kinetochores, specifically to the specialized microtubules called K-fibers. Cell cycle and Northern blot analyses showed that AURKB is expressed in the S phase and persistently thereafter. Western blot analysis indicated that it is localized in the midbodies during anaphase. Northern blot analysis detected strong expression of a 1.5-kb transcript in thymus, with weaker expression in small intestine, testis, colon, spleen, and brain. Examination of the role of both kinases in the phosphorylation of CENPA revealed that the reaction is mediated sequentially by AURKA and AURKB in early mitosis. EB1 overexpression enhanced AURKB kinase activity, and knockdown of EB1 with small interfering RNA impaired AURKB activity. EB1 protected Aurora B from dephosphorylation/inactivation by protein phosphatase-2A by blocking binding of PP2A.

Description: Chromosomal segregation during mitosis as well as meiosis is regulated by kinases and phosphatases. The Aurora kinases, members of the Ser/Thr protein kinase family, associate with microtubules during chromosome movement and segregation. Aurora kinase C may play a part in organizing microtubules in relation to the function of the centrosome/spindle pole during mitosis. This protein is localized to centrosome from anaphase to cytokinesis. Expression is limited to testis in normal cells. Elevated expression levels are seen only in a subset of cancer cells such as HepG2, HuH7 and HeLa cells. Aurora-C expression is maximum at M phase.

Description: Chromosomal segregation during mitosis as well as meiosis is regulated by kinases and phosphatases. The Aurora kinases, members of the Ser/Thr protein kinase family, associate with microtubules during chromosome movement and segregation. Aurora kinase C may play a part in organizing microtubules in relation to the function of the centrosome/spindle pole during mitosis. This protein is localized to centrosome from anaphase to cytokinesis. Expression is limited to testis in normal cells. Elevated expression levels are seen only in a subset of cancer cells such as HepG2, HuH7 and HeLa cells. Aurora-C expression is maximum at M phase.

Description: Chromosomal segregation during mitosis as well as meiosis is regulated by kinases and phosphatases. The Aurora kinases, members of the Ser/Thr protein kinase family, associate with microtubules during chromosome movement and segregation. Aurora kinase C may play a part in organizing microtubules in relation to the function of the centrosome/spindle pole during mitosis. This protein is localized to centrosome from anaphase to cytokinesis. Expression is limited to testis in normal cells. Elevated expression levels are seen only in a subset of cancer cells such as HepG2, HuH7 and HeLa cells. Aurora-C expression is maximum at M phase.

Description: Chromosomal segregation during mitosis as well as meiosis is regulated by kinases and phosphatases. The Aurora kinases, members of the Ser/Thr protein kinase family, associate with microtubules during chromosome movement and segregation. Aurora kinase C may play a part in organizing microtubules in relation to the function of the centrosome/spindle pole during mitosis. This protein is localized to centrosome from anaphase to cytokinesis. Expression is limited to testis in normal cells. Elevated expression levels are seen only in a subset of cancer cells such as HepG2, HuH7 and HeLa cells. Aurora-C expression is maximum at M phase.

Description: Chromosomal segregation during mitosis as well as meiosis is regulated by kinases and phosphatases. The Aurora kinases, members of the Ser/Thr protein kinase family, associate with microtubules during chromosome movement and segregation. Auroria kinase A may play a role in cell cycle regulation during anaphase and/or telophase, in relation to the function of the centrosome/spindle pole region during chromosome segregation. It may be involved in microtubule formation and/or stabilization. This protein has also been postulated to play a key role during tumor development and progression. Aurora kinase A localizes on centrosomes in interphase cells and at each spindle pole in mitosis. It is highly expressed in testis, weakly in skeletal muscle, thymus and spleen, and also highly expressed in colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines. Expression is cell-cycle regulated, low in G1/S, accumulates during G2/M, and decreases rapidly afterward. Defects in Aurora kinase A are responsible for numerical centrosome aberrations including aneuploidy.

Description: Rabbit polyclonal Aurora Kinase antibody

Description: This recombinant Aurora B antibody reacts to human Aurora kinase B.