Aurka

Manufactured by Santa Cruz Biotechnology

Sourced in United States

AURKA is a laboratory product offered by Santa Cruz Biotechnology. It is an enzyme that plays a key role in the regulation of cell division. AURKA is essential for the proper progression of mitosis and is involved in the formation of the mitotic spindle. This product is intended for research use only.

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7 protocols using aurka

Cell line authentication and antibody validation

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C4-2, HEK293, Phoenix and 22Rv1 cell lines were purchased from ATCC. AURKA, Actin and YBX1 antibodies were bought from Santa Cruz Biotech (Santa Cruz, CA, USA). N-cadherin, CD44, Slug and Snail antibodies were bought from One World Lab (San Diego, CA, USA). E-cadherin, MMP-2 and Vimentin antibodies were obtained from Bioss (Woburn, MA, USA). All validated antibodies were used at 1-1000 dilution. Details of antibodies are provided in Supplementary Table S1.

Nikhil K., Raza A., Haymour H.S., Flueckiger B.V., Chu J, & Shah K. (2020). Aurora Kinase A-YBX1 Synergy Fuels Aggressive Oncogenic Phenotypes and Chemoresistance in Castration-Resistant Prostate Cancer. Cancers, 12(3), 660.

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Elucidating BMP-2 Signaling Pathways

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Recombinant human BMP-2 was obtained from Dae Woong Pharmaceuticals (Seoul, South Korea). The BMP-2 antibody was aquired from Abcam (Cambridge, UK) and p-Smad1/5/8, β-catenin, p-β-catenin, ERK1/2, and p-ERK1/2 antibodies were purchased from Cell Signaling Technology (Danvers, MA, USA). Antibodies for BMPRII, c-Myc, AURKA, AURKB, and GAPDH were from Santa Cruz Biotechnology (Santa Cruz, CA, USA). β-catenin small interfering RNA (siRNA) was purchased from Santa Cruz Biotechnology (Dallas, TX, USA) and the aurora kinase A and B inhibitor (AURK inhibitor) was obtained from TOCRIS Bioscience (Bristol, UK).

Lee K.B., Jin H., Ye S., Park B.H, & Kim S.M. (2016). Recombinant human bone morphogenetic protein-2 inhibits gastric cancer cell proliferation by inactivating Wnt signaling pathway via c-Myc with aurora kinases. Oncotarget, 7(45), 73473-73485.

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Protein Expression Analysis in Cells

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Cells were collected and lysed. The protein concentration was then determined, and lysates were resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred onto polyvinylidene difluoride membranes (EMD Millipore, Billerica, MA, USA). Blots were blocked with 5% milk/Tris-Buffered Saline and Tween 20 and then incubated with primary monoclonal antibodies (AURKA, 1:500; c-myc, 1:1,000; sox2, 1:200; V E-cadherin, 1:400; β-catenin, 1:500; and E-cadherin, 1:500 [Santa Cruz Biotechnology Inc., Dallas, TX, USA]) at 4°C overnight and then with secondary antibodies (1:2,000; Santa Cruz Biotechnology Inc., Dallas, TX, USA). Blots were developed using a chemiluminescence detection kit (Amersham Pharmacia Biotech, Piscataway, NJ, USA). Monoclonal β-actin antibody (1:2,000; Santa Cruz Biotechnology Inc.) was used as a control treatment. All the experiments were repeated thrice and provided reproducible results.

Liu Y., Sun B., Liu T., Zhao X., Wang X., Li Y., Meng J., Gu Q., Liu F., Dong X., Liu P., Sun R, & Zhao N. (2016). Function of AURKA protein kinase in the formation of vasculogenic mimicry in triple-negative breast cancer stem cells. OncoTargets and therapy, 9, 3473-3484.

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Antibodies for Western Blotting Analysis

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Antibodies for western blotting were purchased from Cell Signaling (Danvers, MA): p-EGFR (Tyr1068) (2234, 1:1000), EGFR (4267, 1:1000), p-MEK1/2 (Ser217/221) (9154, 1:1000), MEK1/2 (8727, 1:1000), p-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (9101, 1:1000), p44/42 MAPK (Erk1/2) (9102, 1:1000), p-p38 MAPK (Thr180/Tyr182) (9211, 1:1000), p38 MAPK (9212, 1:1000), α-tubulin (2144, 1:2000), vimentin (3390, 1:1000), TACE (3976, 1:1000), Snail (3879, 1:1000), E-cadherin (3195, 1:1000), p-FAK (Tyr397) (3283, 1:1000), FAK (3285, 1:1000), p-STAT3 (Tyr705) (9131, 1:1000), STAT3 (9139, 1:1000), GAPDH (2118, 1:2000), β-actin (3700, 1:2000), p-DNA-PK (68716, 1:1000), DNA-PK (38168, 1:1000), PARP (9532, 1:1000), p-Histone H2A.X (Ser139) (9718, 1:1000), Histone H2A.X (2595, 1:1000), p-Chk2 (Thr68) (2197, 1:1000), Chk2 (2662, 1:1000), p53 (2524, 1:1000), caspase-7 (9492, 1:1000), caspase-3 (14220, 1:1000), AURK-A (14475, 1:1000); Santa Cruz Biotechnology (Dallas, TX): integrin β1/ITGB1 (sc-374429, 1:1000). Selumetinib (AZD6244, MEK1/2 inhibitor), osimertinib (AZD9291, EGFR^T790M), M3814 (DNA-PK inhibitor, DNA-PK-I) and ZM-447439 (AURK-A inhibitor, AURK-A-I), MK-4827 (PARP inhibitor, PARP-I), M4076 (ATM inhibitor, ATM-I), M6620 (ATM/ATR inhibitor, benzosertib) and M4344 (ATR inhibitor, ATR-I) were purchased from Selleck Chemicals (Selleckchem).

De Rosa C., De Rosa V., Tuccillo C., Tirino V., Amato L., Papaccio F., Ciardiello D., Napolitano S., Martini G., Ciardiello F., Morgillo F., Iommelli F, & Della Corte C.M. (2024). ITGB1 and DDR activation as novel mediators in acquired resistance to osimertinib and MEK inhibitors in EGFR-mutant NSCLC. Scientific Reports, 14, 500.

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Immunohistochemical Analysis of Aurora Kinases

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Three millimeters tumor sections were incubated with commercial rabbit polyclonal antibodies against AURKA, AURKB, and AURKC (all from Santa Cruz Biotechnology, Santa Cruz, CA, USA) at 1/100 dilution overnight at 4°C. Then, the sections were conjugated with horseradish peroxidase antibody (1:500 dilution; Santa Cruz Biotechnology) at room temperature for 2 h, then covered by 3, 3-diaminobenzidine (Vector Laboratories, Burlingame, CA, USA), and slides were mounted with Vectashield mounting medium (Vector Laboratories). Subsequently, all fields were observed under light microscopy (Olympus 600 auto-biochemical analyzer, Tokyo, Japan). Control experiments without primary antibody demonstrated that the signals observed were specific.

Hu T., Wang X., Xia Y., Wu L., Ma Y., Zhou R, & Zhao Y. (2022). Comprehensive analysis identifies as a critical prognostic prediction gene in breast cancer. Chinese Medical Journal, 135(18), 2218-2231.

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SDS-PAGE and Western Blot Analysis

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SDS-PAGE was performed as previously described in37 (link). Primary antibodies were: mouse monoclonal β-actin (1:400, Sc-47778 Santa Cruz Biotechnology), β-catenin (1:100, Sc-7963 Santa Cruz Biotechnology), MMP9 (1:200, Sc-21733 Santa Cruz Biotechnology), Wnt3a (1:200, sc-136163 Santa Cruz Biotechnology), rabbit polyclonal AurkA (1:400, sc-25425, Santa Cruz Biotechnology), Snail (1:100, PA5-11923 Pierce), Stat3 (1:200, sc-482 Santa Cruz Biotechnology). A representative picture of three independent experiments was reported.

Eterno V., Zambelli A., Villani L., Tuscano A., Manera S., Spitaleri A., Pavesi L, & Amato A. (2016). AurkA controls self-renewal of breast cancer-initiating cells promoting wnt3a stabilization through suppression of miR-128. Scientific Reports, 6, 28436.

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Immunohistochemical Analysis of Breast Cancer

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For immunohistochemistry on human breast cancer tissues and tumor xenografts, FFPE tumor specimens were processed to obtain 5 μm-thick slides. Epitope retrieval was performed in Citrate Buffer pH6 (DAKO) in a pre-warmed bath at 98 °C for 45 minutes. Primary antibody incubation was carried out at 4 °C ON. Primary mouse antibodies: AurkA (1:100, sc-25425, Santa Cruz Biotechnology) β-catenin (1:50, Sc-7963 Santa Cruz Biotechnology), MMP9 (1:100, Sc-21733 Santa Cruz Biotechnology). Normal breast tissues were used as control of staining.
Samples were analyzed on Leica DM1000 Microscope (Leica) equipped with LAS Software for image capture and analysis. For each slide a least 50 fields were analyzed.
For Ki67 counting, at least ten randomly selected regions for slides were analyzed and a minimum of 500 nuclei was counted for each sample. Representative images at 200X magnification has been shown.

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