The aryl hydrocarbon receptor (AhR) carboxyl terminal transcriptional activation domain was cloned, purified in denatured conditions from bacteria, refolded via limited dialysis, and analyzed for proper refolding via co-immunoprecipitation with the known binding partner SRC-1. This AhR NΔ515 transactivation domain construct was used, along with amino terminal AhR deletion constructs AhR CΔ274 and AhR CΔ553, to attempt to elucidate the nature of the interaction between AhR and p23 in vitro.
| Identifer | oai:union.ndltd.org:pacific.edu/oai:scholarlycommons.pacific.edu:uop_etds-1175 |
| Date | 01 January 2015 |
| Creators | Thompson, John D. |
| Publisher | Scholarly Commons |
| Source Sets | University of the Pacific |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | University of the Pacific Theses and Dissertations |
| Rights | http://creativecommons.org/licenses/by-nc-nd/4.0/ |
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