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.
","abstract_html":"<p>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.</p>","abstract_has_math":false,"creators":["Thompson, John D."],"institution":null,"degree_name":"Master of Science (M.S.)","degree_level":"Thesis - Pacific Access Restricted","degree_discipline":"Biological Sciences","degree_department":null,"school":null,"contributors":["Lisa Wrischnik"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-01-01T08:00:00Z","date_published":"2015-01-01T08:00:00Z","updated_at":"2026-07-24T05:36:00Z","subjects":["Biology","Biological sciences","Ahr","Arnt","Aryl hydrocarbon receptor","P23"],"languages":[],"rights":[],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["9781339047355"],"render_values":[{"text":"9781339047355","href":null,"code":true}]}]},"links":{"outbound_url":"https://scholarlycommons.pacific.edu/uop_etds/176","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Lisa Wrischnik"]},{"key":"dc:creator","label":"Author","values":["Thompson, John D."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2018-06-29T09:05:01Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biological Sciences"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis - Pacific Access Restricted"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science (M.S.)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology","Biological sciences","Ahr","Arnt","Aryl hydrocarbon receptor","P23"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["http://rightsstatements.org/vocab/InC/1.0/"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["9781339047355","https://scholarlycommons.pacific.edu/uop_etds/176"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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.
"]},{"key":"dc:source","label":"Dc Source","values":["101"]},{"key":"dc:title","label":"Title","values":["Analysis of the interaction between the co-chaperone p23 and the aryl hydrocarbon receptor"]}]}],"canonical_facts":{"dc:contributor":["Lisa Wrischnik"],"dc:creator":["Thompson, John D."],"dc:date.available":["2018-06-29T09:05:01Z"],"dc:description.abstract":["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.
"],"dc:identifier":["9781339047355","https://scholarlycommons.pacific.edu/uop_etds/176"],"dc:rights":["http://rightsstatements.org/vocab/InC/1.0/"],"dc:source":["101"],"dc:subject":["Biology","Biological sciences","Ahr","Arnt","Aryl hydrocarbon receptor","P23"],"dc:title":["Analysis of the interaction between the co-chaperone p23 and the aryl hydrocarbon receptor"],"thesis:degree_discipline":["Biological Sciences"],"thesis:degree_level":["Thesis - Pacific Access Restricted"],"thesis:degree_name":["Master of Science (M.S.)"]},"updated_at":"2026-07-24T05:36:00Z"}