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. 2010 Jan 4;38(7):2355–2368. doi: 10.1093/nar/gkp1188

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Electrophoretic mobility shift assay (EMSA) of ERα binding to nonconsensus repetitive element ERE sequences. EMSA was performed using HESC cell nuclear lysates plus recombinant ERα and labeled consensus ERE probe (lanes 1–3) or repetitive DNA element ERE sequences as probes: B68 (lanes 4–6) and D66 (lanes 7–9). An ERα-containing complex bound to all three ERE sequences (arrowhead, lanes 1, 4 and 7) and was confirmed by supershift (bracket) using a monoclonal antibody that recognizes ERα (lane 2). Specific ERα-containing complexes were similarly shown by loss of bands for B68 (lane 5) and D66 (lane 8) when anti-ERα antibody was added. The nonspecific antibody recognizing Sp1 had no effect on the ERα-containing complexes bound to the classical ERE (lane 3) and B68 (lane 6), but displayed moderate effects on complexes bound to D66 (lane 9), indicating that Sp1 may cooperate with ERα in binding to this sequence. Mismatches from the consensus ERE sequence are indicated by lower case letters and red font. Oligonucleotide sequences are presented in Supplementary Table S1.