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Niamh Cosgrave, Arnold D K Hill, and Leonie S Young

Cycle Sequencing Kits (Amersham Biosciences) according to the manufacturers’ instructions. Electrophoretic mobility shift assays (EMSA) Nuclear protein was extracted using a NE-Per kit according to the manufacturer

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Yonghua Jiang and Stanko S Stojilkovic

assay (EMSA) and chromatin immunoprecipitation (ChIP), whereas the site-directed mutagenesis study indicated that this site regulates the expression of α 1-sGC gene in resting cells. Materials and methods Materials

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Tina Di Palma, Tiziana de Cristofaro, Chiara D'Ambrosio, Dolores Del Prete, Andrea Scaloni, and Mariastella Zannini

by adding 200 μM βNAD + (Sigma) and further incubated for another 15 min. The SDS sample buffer was added to stop the reaction that was diluted 10-fold in WCE buffer and then used in the pull down assay. Electrophoretic mobility shift assay (EMSA

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L Chen, J Zhu, G Sun, and A S Raikhel

mobility shift assays (EMSA) EMSAs were carried out as described previously ( Wang et al. 1998 ). Drosophila BR consensus binding sequences were used to determine the DNA-binding activities of the AaBR isoforms. The consensus sequences that we

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Tien-Chun Yang, Mei-Hua Lu, Wei-Jie Wang, and Jang-Yi Chen

( Fig. 3A ). Electrophoretic mobility shift assay (EMSA) results showed that the enhanced region could bind to nuclear extract proteins of SHR VSMCs ( Fig. 3B , lane 2) but not to WKY VSMCs ( Fig. 3B , lane 4). These results suggest that SHR VSMCs are

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Tomoko Kakizawa, Shin-ichi Nishio, Gerard Triqueneaux, Stephanie Bertrand, Juliette Rambaud, and Vincent Laudet

mean ± s.d . of at least three independent experiments. Electrophoretic mobility shift assays (EMSA) Synthetic oligonucleotides representing each strand of sequences were radiolabeled with 32-P-γATP using

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Hitoshi Iida, Takeshi Ogihara, Mun-kyeong Min, Akemi Hara, Yeong Gi Kim, Kyoko Fujimaki, Motoyuki Tamaki, Yoshio Fujitani, Hail Kim, and Hirotaka Watada

dishes, and isolated nuclear extracts were subjected to electrophoretic mobility shift assay (EMSA) according to the procedure described previously ( Sadowski et al . 1993 ). The GAS-A oligonucleotides (5′-GATCTGTCCCCAGCTC TTCCCAGAA AGCCCTGAGGTG-3′) and

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Yueting Dong, Zhiye Xu, Ziyi Zhang, Xueyao Yin, Xihua Lin, Hong Li, and Fenping Zheng

3 μM pioglitazone or co-treated with 10 μM T0901317 and 3 μM pioglitazone for 24 h, and nuclear protein was extracted and quantified. Electrophoretic mobility shift assay (EMSA) was performed using double-stranded biotin-labelled oligo probes of PPRE

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M L Panno, L Mauro, S Marsico, D Bellizzi, P Rizza, C Morelli, M Salerno, F Giordano, and S Ando’

the Sp1 site (5′-AGGTCA(N) 12 CCGCCC-3′) within nt −1500 to −1477, is responsible for the E 2 -induced activation of the whole IRS-1 promoter. Both electrophoretic mobility shift assay (EMSA) and chromatin immunoprecipitation (ChIP) assay confirmed

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Pulak R Manna and Douglas M Stocco

quantified using a computer-assisted image analyzer (Visage 2000, BioImage, Ann Arbor, MI, USA). All western blotting experiments were repeated three to five times. Electrophoretic mobility shift assay (EMSA) EMSA experiments were carried out with MA-10