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Human Polyclonal Aurora A Primary Antibody for ICC, IF - ABIN151704
Saskova, Solc, Baran, Kubelka, Schultz, Motlik: Aurora kinase A controls meiosis I progression in mouse oocytes. in Cell cycle (Georgetown, Tex.) 2008
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Human Polyclonal Aurora A Primary Antibody for FACS, IF - ABIN1882163
Strausberg, Feingold, Grouse, Derge, Klausner, Collins, Wagner, Shenmen, Schuler, Altschul, Zeeberg, Buetow, Schaefer, Bhat, Hopkins, Jordan, Moore, Max, Wang, Hsieh, Diatchenko, Marusina, Farmer et al.: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. ... in Proceedings of the National Academy of Sciences of the United States of America 2002
Show all 6 Pubmed References
Human Polyclonal Aurora A Primary Antibody for ICC, IF - ABIN4282417
Honma, Nakanishi, Nakanoko, Ando, Saeki, Oki, Iimori, Kitao, Kakeji, Maehara: Contribution of Aurora-A and -B expression to DNA aneuploidy in gastric cancers. in Surgery today 2014
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Human Polyclonal Aurora A Primary Antibody for ICC, IF - ABIN151735
Hontz, Li, Lingle, Negron, Bruzek, Salisbury, Li: Aurora a and B overexpression and centrosome amplification in early estrogen-induced tumor foci in the Syrian hamster kidney: implications for chromosomal instability, aneuploidy, and neoplasia. in Cancer research 2007
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Human Monoclonal Aurora A Primary Antibody for IF, IP - ABIN2477554
Quinn, Crane, Kocal, Best, Cameron, Rushmore, Farber, Hayes: Protective activity of different hepatic cytosolic glutathione S-transferases against DNA-binding metabolites of aflatoxin B1. in Toxicology and applied pharmacology 1990
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Human Monoclonal Aurora A Primary Antibody for IF, IHC (p) - ABIN563053
Lo Iacono, Monica, Saviozzi, Ceppi, Bracco, Papotti, Scagliotti: Aurora Kinase A expression is associated with lung cancer histological-subtypes and with tumor de-differentiation. in Journal of translational medicine 2011
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Human Monoclonal Aurora A Primary Antibody for FACS, IF - ABIN965625
De Luca, Brunetto, Asteriti, Giubettini, Lavia, Guarguaglini: Aurora-A and ch-TOG act in a common pathway in control of spindle pole integrity. in Oncogene 2008
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Human Monoclonal Aurora A Primary Antibody for ICC, FACS - ABIN968971
Veerakumarasivam, Goldstein, Saeb-Parsy, Scott, Warren, Thorne, Mills, Venkitaraman, Neal, Kelly: AURKA overexpression accompanies dysregulation of DNA-damage response genes in invasive urothelial cell carcinoma. in Cell cycle (Georgetown, Tex.) 2008
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Cow (Bovine) Monoclonal Aurora A Primary Antibody for ICC, IF - ABIN151177
Cremet, Descamps, Vérite, Martin, Prigent: Preparation and characterization of a human aurora-A kinase monoclonal antibody. in Molecular and cellular biochemistry 2003
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AURKA directly regulates mitochondrial functions and that AURKA over-expression promotes metabolic reprogramming by increasing mitochondrial interconnectivity.
WDR62 controls brain growth through lineage-specific interactions with master mitotic signaling kinase, aurora A kinase.
equatorial stimulation is mediated primarily by the delivery of factors to the cortex by noncentrosomal microtubules, as well as a midzone-derived phosphorylation gradient that is amplified by the concerted activities of mABK and a soluble pool of AAK.
Disrupting the spindle assembly checkpoint in the aurA mutant does not prevent neuroblast amplification, tumor formation or chromosome segregation.
Aurora A kinase activity contributes to phosphorylation of kinetochore substrates near poles and its inhibition results in chromosome misalignment and an increased incidence of erroneous kinetochore-MT attachments.
AurA and aPKC exert the spatiotemporal control of Lgl distribution to achieve unique cell polarity roles in distinct cell types.
Aurora A and B kinases directly phosphorylate Lgl to promote its mitotic relocalization.
Drosophila melanogaster aurora A phosphorylates the dynactin subunit p150(glued) on sites required for its association with the mitotic spindle.
One of the functions of Aurora A kinase is to direct centrosomal organization such that D-TACC complexed to the MSPS/XMAP215 microtubule-associated protein may be recruited, and thus modulate the behavior of astral microtubules.
Drosophila Aurora-A is required for centrosome maturation and actin-dependent asymmetric protein localization during mitosis.
Deletion mapping identifies a central domain of Aurora-A as essential for its centrosomal localization that is augmented by both the amino and the carboxyl terminal ends of the protein.
Results suggest that Aurora-A regulates centrosome assembly by controlling centrosomin's (CNN) ability to target and/or anchor gamma-tubulin to the centrosome and to organize microtubule-nucleating sites via interaction with CNN.
Aurora-A is essential for many crucial events during mitosis and phosphorylation of a series of substrates by Aurora-A at different stages of mitosis may promote diverse critical events in mitosis to maintain chromosome integrity in cells
identification of Bora, a conserved protein required for activation of Aurora-A at the onset of mitosis; model in which activation of Cdc2 initiates the release of Bora into the cytoplasm where it can bind and activate Aurora-A
Study shows that Aurora-A acts as a tumor suppressor by suppressing neuroblast self-renewal and promoting neuronal differentiation.
Study concludes that Aurora-A and Numb are novel inhibitors of neuroblast self-renewal and that spindle orientation regulates neuroblast self-renewal.
Study shows that a phosphorylation cascade triggered by the activation of Aurora-A is responsible for the asymmetric localization of Numb in mitosis.
Study identified a previously unrecognized evolutionarily conserved Pins domain (Pins(LINKER)) that requires Aurora-A phosphorylation to recruit Dlg and promote partial spindle orientation.
Zebrafish Aurora-A is critically required for embryonic proliferation during development.
Molecular dynamics simulations and electron paramagnetic resonance experiments show that phosphorylation triggers a switch from an autoinhibited substate to an active substate, leading to catalytic activation.
temporal and spatial Aurora kinase-mediated regulation of SPICE1 is important for correct chromosome segregation.
knockdown of AURKA suppressed cell proliferation, migration and invasion, and also induced apoptosis and reactive oxygen species generation in Oral squamous cell carcinoma.
residual disease and acquired resistance in response to EGFR inhibitors requires Aurora kinase A (AURKA) activity.
Aurora A phosphorylation of YY1 during mitosis inactivates its DNA binding activity.
These results suggest that Aurora A activity is involved in the maintenance of Golgi architecture and the relationship between the Golgi apparatus and centrosome.
AURKA and HDAC2 genes were significantly overexpressed in all groups compared to the control. overexpression of AURKA genes was detected in the presence of metastasis and was up regulated during Gastric Cancer development.
Study indicated that AURKA, CDC20 and TPX2 are over-expressed in smoking related lung adenocarcinoma tissues and their higher mRNA expression levels have a worse prognosis.
Results show that a fraction of cytoplasmic AURKA is associated with mitochondria, co-fractionating in cell extracts and interacting with mitochondrial proteins. Further data identify the mitochondrial fraction of AURKA as influencing mitochondrial morphology, because an N-terminally truncated version of the kinase that does not localize to mitochondria does not affect the mitochondrial network.
AurA is activated by the CXCL12-CXCR4 pathway in an ERK1/2-dependent manner. It contributes to glioblastoma cell survival, radio-resistance, self-renewal, and proliferation regardless of exogenous stimulation with CXCL12. It triggers the CXCL12-mediated migration of glioblastoma cells in vitro and the invasion of the subventricular zone in xenografts. It favors the pro-migratory activity of the Rho-GTPase CDC42 by CXCL12.
our results indicate that none of the AURKA polymorphisms are associated with neuroblastoma susceptibility in two distinct Chinese populations. Further studies with larger sample sizes and different ethnicities are warranted to validate our results.
findings reveal that BRCA2-deficient cancer cells show enhanced sensitivity to inactivation of TPX2 or its partner Aurora-A, which points at an actionable dependency of genomically unstable cancers.
Results found that PARP10 interacted with Aurora A, and inhibited its kinase activity, thereby regulating its downstream signaling.
MMSET is a regulator of p53 stability via methylation of AURKA in proliferating cells.
Cells lacking ARID1A show enhanced AURKA transcription, which leads to the persistent activation of CDC25C, a key protein for G2/M transition and mitotic entry.
AURKA protein was overexpressed in nearly all dermatofibrosarcoma protuberans tissues and AURKA protein levels significantly correlated with CD34 protein levels.
Aurora A-dependent phosphorylation of CENP-A at the inner centromere protects chromosomes against tension-induced cohesion fatigue until the last kinetochore is attached to spindle microtubules.
Aurora A kinase regulates kinetochore-microtubule dynamics of metaphase chromosomes, and Hec1 S69, a previously uncharacterized phosphorylation target site in the Hec1 tail, is a critical Aurora A substrate for this regulation.
Upon phorbol 12-myristate 13-acetate treatment, THP-1 cells differentiated into monocytes by down-regulating AURKA, resulting in a reduction in H3S10 phosphorylation. The AURKA inhibitor alisertib accelerates the expression of the H3K27 demethylase KDM6B, dissociating AURKA and YY1 from the KDM6B promoter region and inducing differentiation.
AURKA is expressed in several cell types in the testis. Spermatogonia and spermatocytes express AURKA as expected based on the known role of this kinase in cell division. Surprisingly, we also found AURKA localized to spermatids and the flagellum of spermatozoa.
ex vivo cells derived from teratomas exhibited high self-renewal capacity that was linked to Aurora-A kinase activity and gave rise to lung metastasis when injected into the tail vein of immunocompromised mice.
Aurora A and Plk4 are rate-limiting factors contributing to microtubule growth as the acentriolar oocyte resumes meiosis.
The high sequence similarity among the AURK family members has made discerning the individual kinase functions in meiosis challenging. Technical limitations in specifically targeting AURKB or AURKC using small-molecule inhibitors and compensatory abilities in single-knockout animals add to this challenge...proper regulation of AURKA expression is crucial for spindle formation in meiosis
Aurora kinase inhibitor CCT137690 induces necrosis-like death in pancreatic ductal adenocarcinoma cells, via RIPK1, RIPK3, and MLKL signaling.
CIP2A acts as a scaffold for CEP192-mediated microtubule organizing center assembly by recruiting Plk1 and aurora A during meiotic maturation in mouse oocytes
AURKA stabilizes MYC to promote tp53-altered liver tumor cell survival.
Bcl2l10, Tpx2, and Aurka co-localized on the meiotic spindles, and Bcl2l10 was present in the same complex with Tpx2.
Suppression of neuroendocrine and NEPC development by ICT was associated with dose-dependent inhibitory effects on abnormally elevated IL-6/STAT3 and Aurora kinase A in vitro and in vivo
Our findings demonstrate that prolonged overexpression of Aurora-A can be a driver somatic genetic event in mammary adenocarcinomas associated with deregulated tumor-relevant pathways in the Aurora-A subset of human breast cancer
Data show that aurora-A kinase (AURKA) supports effective spindle formation in zygote.
observations revealed that the alteration of PKB-GSK-3beta axis, Plk-1, and Aurora kinase-A expressions in HSPC compartment due to DNA damage response was associated with the proliferative impairment and apoptosis during aplastic anemia.
Augmented expression of Aurora kinase-A and Polo-like kinase-1 at the lactogenic switch likely mediates the formation of binucleated cells.
Aurora A inhibition causes delocalized clustering of Lck at the immunological synapses and decreases its phosphorylation levels thus indicating Aurora A is required for maintaining Lck active during T-cell activation.
Ndel1 acts as a novel upstream regulator of the trichoplein-Aurora A pathway to inhibit primary cilia assembly.
The Aurora kinase A and c-Myc expression and histone H3 phosphorylation level were comparatively higher in the cranial tumor than the caudal.
aurora kinase A (AURKA) represents a new therapeutic target in primary myelofibrosis.
A novel function was identified for Aurora-A in controlling the polarization of macrophages and inflammation.
Wdr62 interacts with Aurora A to control mitotic progression, and loss of these interactions leads to mitotic delay and cell death of NPCs, which could be a potential cause of human microcephaly.
Reduced levels of Aurora A protein immediately post-thaw may be associated with the impaired oocyte maturation manifested by the delayed progression through meiosis
Aurora A was the most abundant form in oocytes, both at mRNA and protein levels, in bovine oocytes during meiotic maturation.
Aurora kinase A is unlikely to be involved in CPEB1 activating phosphorylation and cyclin B1 mRNA polyadenylation during meiotic maturation of porcine oocytes.
Aurora-A may be a multifunctional kinase that plays pivotal regulatory roles in microtubule assembly during porcine oocyte meiotic maturation, fertilization and early embryonic mitosis
Aurora A stimulates the protein synthesis and promotes the meiotic resumption.
These results suggest a novel relationship between AurA and protein phosphatases during progression throughout the early embryonic cell cycle and shed new light on potential defects caused by AurA overexpression.
MCAK colocalized with NuMA and XMAP215 at the center of Ran asters where its activity is regulated by Aurora A-dependent phosphorylation of S196, which contributes to proper pole focusing
Plx1 promotes activation of Aurora A, most likely through TPX2.
Aurora-A kinase is required for astral microtubule polymerization and spindle microtubule flux during chromosome segregation.
Data show that Aurora A is a key regulator of microtubule assembly during M phase and therefore of bipolar spindle formation.
binding and elution properties of both the phosphopeptides and unphosphorylated peptides of His6-Aurora A
Results suggest that phosphorylation of maskin by Aurora-A prevents meiosis II proteins from being produced during meiosis I.
The N-terminal non-catalytic domain of Aurora-A can localize to the centrosome in Xenopus egg extracts, while GFP fusions of either the N-terminal or catalytic domains are targeted to the centrosome in Xenopus XL2 cells.
Here we identify G205 in Xenopus Aurora A as a key determinant of both intrinsic activity and regulation by TPX2
The catalytic domain alone of Aurora-A is sufficient to restore spindle bipolarity; additional N-terminal sequences function in mitotic timing.
The protein encoded by this gene is a cell cycle-regulated kinase that appears to be involved in microtubule formation and/or stabilization at the spindle pole during chromosome segregation. The encoded protein is found at the centrosome in interphase cells and at the spindle poles in mitosis. This gene may play a role in tumor development and progression. A processed pseudogene of this gene has been found on chromosome 1, and an unprocessed pseudogene has been found on chromosome 10. Multiple transcript variants encoding the same protein have been found for this gene.
A-type aurora kinase
, aurora A
, aurora A kinase
, aurora kinase
, Aurora A
, hypothetical protein
, aurora kinase A
, serine/threonine-protein kinase 6
, serine/threonine protein kinase 6
, aurora A kinase protein
, serine/threonine-protein kinase 6-like
, Aurora-A kinase
, IPL1-related kinase
, aurora 2
, aurora-related kinase 1
, aurora/IPL1-like kinase
, aurora/IPL1-related kinase 1
, breast tumor-amplified kinase
, breast-tumor-amplified kinase
, protein phosphatase 1, regulatory subunit 47
, serine/threonine kinase 6
, serine/threonine protein kinase 15
, serine/threonine-protein kinase 15
, serine/threonine-protein kinase aurora-A
, aurora family kinase 1
, ipl1- and aurora-related kinase 1
, serine/threonine-protein kinase Ayk1
, Serine/threonine-protein kinase 6
, aurora kinase A-A
, serine/threonine-protein kinase 6-A
, serine/threonine-protein kinase Eg2
, serine/threonine-protein kinase Eg2-A