experiments was shown. Electrophoretic mobility shift assay (EMSA) Nuclear extract was prepared from HepG2 cells according to the principle described by Dignam (25). Freshly prepared cell pellet (>1×10 7 cells) resuspended in 5× packed cell volume (PCV) of
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Wo-Shing Au, Liwei Lu, Chung-Man Yeung, Ching-Chiu Liu, Oscar G Wong, Lihui Lai, Hsiang-fu Kung, and Marie C Lin
Bassam El-Asmar, Xavier C Giner, and Jacques J Tremblay
Antisense: CTGCACTGGGGCTaaCCTGGCGAACCC EMSA C/EBPβ element (bold) at −110 bp Wild-type sense: CCCTTGT ATGGCCAAAG CTCGCCG Wild-type antisense: CGGCGAG CTTTGGCCAT ACAAGGG Mutated sense: CCCTTGT ATGGCCttAG CTCGCCG Mutated antisense: CGGCGAG CTaaGGCCAT ACAAGGG
Francis Bergeron, Edward T Bagu, and Jacques J Tremblay
′-TTTGAAGAGACCAGGtttGGGGGACTTCATTTCCTGACAG-3′ EMSA WT1 −157/−127 bp S: 5′-GAGCAAGGAGGAGTCCGAGGGAAACTTTTAT-3′ WT2 −144/−112 bp S: 5′-TCCGAGGGAAACTTTTATTTTGAAGAGACCAGG-3′ M2 −151/−149 bp S: 5′-GAGCAAaagGGAGTCCGAGGGAAACTTTTAT-3′ M3 −147/−145 bp S: 5′-GAGCAAGGAGtctTCCGAGGGAAACTTTTAT-3′ M4 −143
Weiming Zheng, Jingying Yang, Qiaorong Jiang, Zhibin He, and Lisa M Halvorson
, LRH-1 Ab2 was directed against rat amino acid positions #242–560 and was unsuccessful on Western but was effective on electrophoretic mobility shift assay (EMSA). Both antibodies are cross reactive with mouse. Transient
D T Furuya, A C Poletto, H S Freitas, and U F Machado
–Newman–Keuls). Chronic and acute CB1 antagonism decreases NF-κB binding activity To further investigate the mechanisms involved in Slc2a4 upregulation by the CB1 receptor, an electrophoretic mobility shift assay (EMSA) was performed. For the analysis of NF-κB binding
B Horard, A Castet, P-L Bardet, V Laudet, V Cavailles, and J-M Vanacker
A: GTCAAGCTTGCCGCTTCACC C: GTCTTCAGCTCACTGTCTGG B: TTGGACAAGTGACGACCTGT Electrophoretic mobility shift assays (EMSA) ERR proteins were translated in vitro by the transcription
Naama Reizner, Sharon Maor, Rive Sarfstein, Shirley Abramovitch, Wade V Welshons, Edward M Curran, Adrian V Lee, and Haim Werner
isoforms lacking KTS was associated with specific binding to cis -elements in the IGF-IR promoter region, as demonstrated using electrophoretic mobility shift assays (EMSAs) and DNaseI footprinting analysis. Isoforms including the KTS tripeptide were
M Udelhoven, U Leeser, S Freude, M M Hettich, M Laudes, J Schnitker, W Krone, and M Schubert
electromobility shift assay (EMSA) were annealed to yield double strands in 10 mM Tris–HCl pH 8, 50 mM NaCl and the binding reaction was performed using the LightShift Chemiluminescent EMSA Kit (Pierce Biotechnology Inc, Rockford, IL, USA). Oligonucleotides used
Julie Amyot, Isma Benterki, Ghislaine Fontés, Derek K Hagman, Mourad Ferdaoussi, Tracy Teodoro, Allen Volchuk, Érik Joly, and Vincent Poitout
(−327)Luc, and 4 μl of Lipofectamine 2000. Cells were harvested 48 h later for electrophoretic mobility shift assay (EMSA) or luciferase assay. Dual-Luciferase Reporter assays (Promega) were performed according to the manufacturer's instructions
Takanobu Sato, Kousuke Kitahara, Takao Susa, Takako Kato, and Yukio Kato
assay, followed by analyzing the Prop-1-binding site by electrophoretic mobility shift assay (EMSA) and DNase I footprinting. Our results show that the promoter of α GSU gene was activated by Prop-1, whereas that of LH β gene was not. EMSA and DNase I
