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Purified anti-Phospho-Aurora A (Aurora 2) (Thr288) Antibody
Purified anti-Phospho-Aurora A (Aurora 2) (Thr288) Antibody
Each lot of this antibody is quality control tested by Western blotting. For Western blotting, the suggested antibody concentration is 1-4 μg/ml. It is strongly recommended that immunoprecipitation with a pan-specific Aurora antibody be carried out before Western blotting with the phospho-specific antibody to increase signal.
COA:
Cell extract from untransfected HEK293T cells (Lane 1), HEK293T cells transfected with human AIK cDNA without nocodazole treatment (Lane 2) or overnight nocodazole-treated (Lane 3) were resolved by electrophoresis, transferred to nitrocellulose, and probed with monoclonal antibody against Thr288 phosphorylated Aurora A (clone AIK137). Proteins were visualized using a goat anti-mouse secondary conjugated to HRP and a chemiluminescence detection system.
Aurora A (also known as Aurora 2) is a serine/threonine kinase with a molecular weight of approximately 46 kD. This kinase is highly expressed in the thymus and some tumors and is also expressed in other tissues including the lung, testis, colon, placenta, and fetal liver. Aurora A localizes in the midzone or central spindle in late anaphase and is concentrated in the midbody in telophase and during cytokinesis. This kinase is believed to act in cell cycle regulation during anaphase and/or telophase at centrosome/spindle pole during chromosome segregation. Aurora A has been shown to regulate cleavage of polar spindle microtubules at the onset of cytokinesis during mitosis. Defects in Aurora A cause numerous centrosome aberrations including aneuploidy (genetic variant with amino acid substitution F31I). Aurora A expression is cell cycle regulated, low in G1/S, and accumulating in G2/M. Expression is upregulated in cancer cells during M phase. Phosphorylation by PKA has been shown to regulate function. Aurora A phosphorylation has been reported on Thr 288. This kinase associates with the centrosome and mitotic spindles, NM23-H1, protein phosphatase type I, and co-localizes with γ-tubulin. The Phe 31 variant has been shown to interact with the E2 ubiquitin-conjugating enzyme, UBE2N. The AIK137 mouse monoclonal antibody has been shown to react with phosphorylated human Aurora A.
Serine/threonine kinase, Aurora subfamily, molecular weight approximately 46 kD
Distribution:
High expression in thymus and some tumors. Also expressed in lung, testis, colon, placenta, and fetal liver. Localized in the midzone or central spindle in late anaphase; concentrated in the midbody in telophase and during cytokinesis.
Function:
Cell cycle regulation during anaphase and/or telophase at centrosome/spindle pole during chromosome segregation. Defects in Aurora A cause numerous centrosome aberrations including aneuploidy (genetic variant with amino acid substitution F31I). Regulates
Regulation:
Cell cycle regulated, low in G1/S, accumulates in G2/M. Expression is upregulated in cancer cells during M phase. Phosphorylation by PKA regulates function.
Modification:
Phosphorylation (Thr 288)
Interaction:
E2 ubiquitin-conjugating enzyme UBE2N with Phe 31 variant. Associates with centrosome and mitotic spindles, NM23-H1, protein phosphatase type I and localizes with γ-tubulin.
Antigen References:
1. Shindo M, et al. 1998. Biochem. Biophys. Res. Commun. 244:285. 2. Tatsuka M, et al. 1998. Cancer Res. 58:4811. 3. Nigg EA. 2001. Nat. Rev. Mol. Cell. Biol. 2:21.
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Purified anti-Phospho-Aurora A (Aurora 2) (Thr288)
Cell extract from untransfected HEK293T cells (Lane 1), HEK293T cells transfected with human AIK cDNA without nocodazole treatment (Lane 2) or overnight nocodazole-treated (Lane 3) were resolved by electrophoresis, transferred to nitrocellulose, and probed with monoclonal antibody against Thr288 phosphorylated Aurora A (clone AIK137). Proteins were visualized using a goat anti-mouse secondary conjugated to HRP and a chemiluminescence detection system.
