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. Author manuscript; available in PMC: 2019 Jun 1.

Published in final edited form as: Biochem Pharmacol. 2018 Mar 17;152:34–44. doi: 10.1016/j.bcp.2018.03.015

Fig. 7 — p23 interacted with AHR at the N-terminal 216 amino acids of AHR. (A) GST-p23 wild type (WT) (left panel) but not GST (right panel) co-precipitated AHR aa1-295 (TH553) but not AHR aa217-549 (TH217-549) or aa516-848 (TH515). TH, thioredoxin. Arrows indicate the location of the expected band. (B) All transfected p23 mutants were able to interact with TH553 similar to GST-p23 WT. All images are representative of triplicate data that are plotted with means ± SD (n = 3). (C) The above Western images showing that addition of affinity purified Pichia ARNT (5μL) did not interfere with the interaction between affinity purified GST-p23 (0.35 μl) and TH553 (5 μl). All images are representative of triplicate data that are plotted below with means ± SD (n=3).

Fig. 7 — p23 interacted with AHR at the N-terminal 216 amino acids of AHR. (A) GST-p23 wild type (WT) (left panel) but not GST (right panel) co-precipitated AHR aa1-295 (TH553) but not AHR aa217-549 (TH217-549) or aa516-848 (TH515). TH, thioredoxin. Arrows indicate the location of the expected band. (B) All transfected p23 mutants were able to interact with TH553 similar to GST-p23 WT. All images are representative of triplicate data that are plotted with means ± SD (n = 3). (C) The above Western images showing that addition of affinity purified Pichia ARNT (5μL) did not interfere with the interaction between affinity purified GST-p23 (0.35 μl) and TH553 (5 μl). All images are representative of triplicate data that are plotted below with means ± SD (n=3).