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. 2017 Jun 7;8:661. doi: 10.3389/fimmu.2017.00661

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Copyright © 2017 Ng, Jennings, Wang, Molina, Nelson and Wang.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Gel mobility shift assay (GMSA). (A) Probe sequences. Sequences of the positive strand of Wt-GRE1, Mut-GRE1, Wt-GRE2, and Mut-GRE2 are displayed. (B) GR–GRE binding. Human recombinant GR protein (40 ng, Hu-GR) was incubated with each of the following double-stranded probes: wild-type GRE1 (Wt-GRE1), mutant GRE1 (Mut-GRE1), wild-type GRE2 (Wt-GRE2), or mutant GRE2 (mut-GRE2). After resolving in a 6% polyacrylamide non-denaturing gel, the GR–GRE complex was detected by X-ray film exposure. (C) Alcohol effect on GR-GRE binding. The GR protein (40 ng, Hu-GR) was incubated with the radio-labeled wild-type GRE1 or GRE2 probe in the presence of various concentrations of alcohol (0, 25, 50, or 100 mM). GR–GRE binding was similarly examined by GMSA.