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P aurora a

Manufactured by Cell Signaling Technology
Sourced in United States

P∼Aurora-A is a laboratory reagent that detects the phosphorylated form of the Aurora-A protein kinase. Aurora-A is a key regulator of mitotic cell division. The P∼Aurora-A product allows for the specific detection of the active, phosphorylated state of Aurora-A in cellular samples.

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3 protocols using p aurora a

1

Evaluating Aurora A and Histone H3

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Expression levels and phosphorylation of Aurora A and histone H3 were evaluated by performing immunoblotting analysis as described previously (14 (link)). Antibodies against Aurora A (p-Aurora A) and PARP were purchased from Cell Signaling Technology (Danvers, MA, USA). Anti-histone H3 antibody and anti-phosphorylated histone H3 (anti-p-H3; Ser10) antibody were obtained from Abcam (Cambridge, MA, USA) and Millipore (Billerica, MA, USA), respectively. The monoclonal antibody against β-actin (Sigma-Aldrich, St. Louis, MO, USA) was used for a loading control.
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2

Immunoblot, Immunofluorescence, and FACS Assays

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Immunoblot, Immunofluorescence and FACS assays were performed as previously described [26 (link)]. Antibodies employed to perform these studies were the followings: p53 (D07 DAKO), p21 (Oncogene), Centrin 20h5 (Mayo Clinic, Rochester, Minnesota, USA), H2AX, Aurora-A, p∼Aurora-A, SMAD5, PLK1, cleaved-PARP, CD44 (Cell Signaling, Danvers, Massachusetts, USA), CD44, CD24 (BD Pharmigen, San Jose, California, USA), PROCR and Beta-actin (Sigma, St. Louis, Missouri, USA). Results are derived from three independent experiments with comparable outcomes.
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3

NanoPro 1000 Phosphoprotein Assay

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Lysates were analyzed using a NanoPro 1000 system (ProteinSimple Inc.) with an optimized protocol. Primary antibodies were used at 1:50 dilution for 2 hours. Antibodies employed to perform the NIA assay were the followings: p∼Aurora-A (Cell Signaling, Danvers, Massachusetts, USA) and p∼SMAD5 (Abcam, Cambridge, Massachusetts, USA). Results are derived from three independent experiments with comparable outcomes.
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