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Mouse Anti-AURKA Recombinant Antibody (5F8) (CBMAB-A4186-YC)

Provided herein is a Mouse monoclonal antibody against Human Aurora Kinase A. The antibody can be used for immunoassay techniques, such as ELISA, IF, WB.
See all AURKA antibodies
Published Data
Mouse Anti-AURKA Recombinant Antibody (5F8) in WB
HeLa cells were transfected with control siRNA (ctrl) or siRNA against Aurora-A and -B (A/B). At 2 days after transfection, cells were treated with DMSO or Taxol, and VX680 was added to the cells for 2 h before harvesting as indicated. The samples were analyzed by Western blotting with the indicated antibodies. ...View More
Xiao, L., Chen, Y., Ji, M., Volle, D. J., Lewis, R. E., Tsai, M. Y., & Dong, J. (2011). KIBRA protein phosphorylation is regulated by mitotic kinase aurora and protein phosphatase 1. Journal of Biological Chemistry, 286(42), 36304-36315.
Mouse Anti-AURKA Recombinant Antibody (5F8) in IHC
Immunohistochemical detection of AURKA protein in lung cancer. AURKA was predominantly expresses in nuclear compartment of BAC, ADC and SQC (A, B, C, respectively). Original Magnification 200×. ). ...View More
Lo Iacono, M., Monica, V., Saviozzi, S., Ceppi, P., Bracco, E., Papotti, M., & Scagliotti, G. V. (2011). Aurora Kinase A expression is associated with lung cancer histological-subtypes and with tumor de-differentiation. Journal of translational medicine, 9, 1-6.

Summary

Host Animal
Mouse
Specificity
Human
Clone
5F8
Antibody Isotype
IgG2a, κ
Application
ELISA, IF, WB, IHC-P

Basic Information

Immunogen
AURKA (NP_940835, 1 a.a. ~ 110 a.a) partial recombinant protein with GST tag.
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
IF(ICC)10 µg/ml
IHC-P3 µg/ml

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4
Preservative
None
Concentration
Batch dependent
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Aurora Kinase A
Introduction
AURKA 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
Entrez Gene ID
6790
UniProt ID
O14965
Alternative Names
Aurora Kinase A; Protein Phosphatase 1, Regulatory Subunit 47; Serine/Threonine-Protein Kinase Aurora-A; Serine/Threonine-Protein Kinase 6; Breast Tumor-Amplified Kinase; Aurora/IPL1-Related Kinase 1; Aurora 2; STK15; STK6; ARK1; AURA; BTAK; AIK; Serine/T
Function
Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (PubMed:26246606, PubMed:12390251, PubMed:18615013, PubMed:11039908, PubMed:17125279, PubMed:17360485).
Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (PubMed:26246606, PubMed:14523000).
Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (PubMed:27335426).
Required for initial activation of CDK1 at centrosomes (PubMed:13678582, PubMed:15128871).
Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (PubMed:18056443, PubMed:15128871, PubMed:14702041, PubMed:11551964, PubMed:15147269, PubMed:15987997, PubMed:17604723, PubMed:18615013).
Regulates KIF2A tubulin depolymerase activity (PubMed:19351716).
Important for microtubule formation and/or stabilization (PubMed:18056443).
Required for normal axon formation (PubMed:19812038).
Plays a role in microtubule remodeling during neurite extension (PubMed:19668197).
Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (PubMed:14702041).
Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (PubMed:11551964).
Necessary for proper cilia disassembly prior to mitosis (PubMed:17604723, PubMed:20643351).
Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (PubMed:28218735).
Biological Process
Anaphase-promoting complex-dependent catabolic process Source: Reactome
Anterior/posterior axis specification Source: Ensembl
Cell division Source: UniProtKB-KW
Centrosome localization Source: Ensembl
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
G2/M transition of mitotic cell cycle Source: Reactome
Liver regeneration Source: MGI
Mitotic cell cycle Source: ProtInc
Mitotic centrosome separation Source: Ensembl
Mitotic spindle organization Source: GO_Central
Negative regulation of apoptotic process Source: Ensembl
Negative regulation of G2/M transition of mitotic cell cycle Source: Reactome
Negative regulation of gene expression Source: UniProtKB
Negative regulation of protein binding Source: UniProtKB
Neuron projection extension Source: Ensembl
Peptidyl-serine phosphorylation Source: UniProtKB
Positive regulation of mitotic nuclear division Source: UniProtKB
Positive regulation of oocyte maturation Source: Ensembl
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
Protein autophosphorylation Source: UniProtKB
Protein localization to centrosome Source: Ensembl
Protein phosphorylation Source: UniProtKB
Regulation of centrosome cycle Source: UniProtKB
Regulation of cytokinesis Source: GO_Central
Regulation of G2/M transition of mitotic cell cycle Source: Reactome
Regulation of protein stability Source: UniProtKB
Regulation of signal transduction by p53 class mediator Source: Reactome
Response to wounding Source: MGI
Spindle assembly involved in female meiosis I Source: Ensembl
Spindle organization Source: UniProtKB
Ubiquitin-dependent protein catabolic process Source: Reactome
Cellular Location
Centrosome; Spindle pole; Cilium basal body; Centriole; Neuron projection. Detected at the neurite hillock in developing neurons (By similarity). Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase (PubMed:9606188, PubMed:17229885, PubMed:21225229). Colocalized with SIRT2 at centrosome (PubMed:22014574). Moves to the midbody during both telophase and cytokinesis (PubMed:17726514). Associates with both the pericentriolar material (PCM) and centrioles (PubMed:22014574). The localization to the spindle poles is regulated by AAAS (PubMed:26246606).
PTM
Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-288 upon TPX2 binding. Thr-288 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-288 during mitosis. Phosphorylation at Ser-342 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-51 at the end of mitosis.
Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome (By similarity). Ubiquitinated by CHFR, leading to its degradation by the proteasome (By similarity). Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome (PubMed:10851084, PubMed:11039908). Ubiquitinated by the CUL3-KLHL18 ligase leading to its activation at the centrosome which is required for initiating mitotic entry (PubMed:23213400). Ubiquitination mediated by CUL3-KLHL18 ligase does not lead to its degradation by the proteasome (PubMed:23213400).

Cheng, X., Wang, J., Lu, S., Fan, W., & Wang, W. (2021). Aurora kinase A (AURKA) promotes the progression and imatinib resistance of advanced gastrointestinal stromal tumors. Cancer cell international, 21(1), 1-13.

Mou, P. K., Yang, E. J., Shi, C., Ren, G., Tao, S., & Shim, J. S. (2021). Aurora kinase A, a synthetic lethal target for precision cancer medicine. Experimental & Molecular Medicine, 53(5), 835-847.

Al-Sanea, M. M., Elkamhawy, A., Paik, S., Lee, K., El Kerdawy, A. M., Abbas, B. S. N., ... & Abdelgawad, M. A. (2020). Sulfonamide-based 4-anilinoquinoline derivatives as novel dual Aurora kinase (AURKA/B) inhibitors: Synthesis, biological evaluation and in silico insights. Bioorganic & medicinal chemistry, 28(13), 115525.

Zhang, H., Bao, J., Zhao, S., Huo, Z., & Li, B. (2020). MicroRNA-490-3p suppresses hepatocellular carcinoma cell proliferation and migration by targeting the aurora kinase A gene (AURKA). Archives of medical science: AMS, 16(2), 395.

Lee, J. W., Parameswaran, J., Sandoval-Schaefer, T., Eoh, K. J., Yang, D. H., Zhu, F., ... & Burtness, B. (2019). Combined aurora kinase A (AURKA) and WEE1 inhibition demonstrates synergistic antitumor effect in squamous cell carcinoma of the head and neck. Clinical Cancer Research, 25(11), 3430-3442.

Jacobsen, A., Bosch, L. J., Martens-de Kemp, S. R., Carvalho, B., Sillars-Hardebol, A. H., Dobson, R. J., ... & Feenstra, K. A. (2018). Aurora kinase A (AURKA) interaction with Wnt and Ras-MAPK signalling pathways in colorectal cancer. Scientific reports, 8(1), 1-11.

Kong, Y., Bender, A., & Yan, A. (2018). Identification of novel aurora kinase A (AURKA) inhibitors via hierarchical ligand-based virtual screening. Journal of chemical information and modeling, 58(1), 36-47.

Bertolin, G., Bulteau, A. L., Alves-Guerra, M. C., Burel, A., Lavault, M. T., Gavard, O., ... & Tramier, M. (2018). Aurora kinase A localises to mitochondria to control organelle dynamics and energy production. Elife, 7, e38111.

Lopez-Cortes, A., Cabrera-Andrade, A., Ona-Cisneros, F., Rosales, F., Ortiz, M., Tejera, E., & Paz-y-Mino, C. (2018). Breast cancer risk associated with genotype polymorphisms of the aurora kinase a gene (AURKA): a case-control study in a high altitude ecuadorian mestizo population. Pathology & Oncology Research, 24(3), 457-465.

Wang, L., Arras, J., Katsha, A., Hamdan, S., Belkhiri, A., Ecsedy, J., & El‐Rifai, W. (2017). Cisplatin‐resistant cancer cells are sensitive to Aurora kinase A inhibition by alisertib. Molecular oncology, 11(8), 981-995.

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