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. 2021 Feb 11;42(4):650–662. doi: 10.1093/carcin/bgab009

Figure 1.

Figure 1.

In cells and in vitro binding of Pirh2 and AIP4. (A) In-cell binding of Pirh2 and AIP4 was assessed. H1299 cells were transfected with plasmids expressing Myc-Pirh2, or in combination with Flag-AIP4, and immunoprecipitated with M5 antibody for Flag-AIP4, and analyzed by western blotting with anti-Myc for Pirh2 and M2 for AIP4 (top panel). Direct western blots for Pirh2, AIP4 and Actin are shown in the lower panel. (B) Similar to (A), except that cell extracts were immunoprecipitated with anti-Myc and analyzed by immunoblotting with anti-Flag as indicated. (C) Cell lysates were prepared from H1299 cells, immunoprecipitated with the indicated antibodies and analyzed by western blotting with antibodies to detect Pirh2 or AIP4 (top panel). Direct western blots for AIP4, Pirh2 and Actin are shown in the lower panel. (D) In vitro interaction of Pirh2 and AIP4 was evaluated. GST-Pirh2 and GST-AIP4 fusion proteins were purified from E. coli. The ability of GST-Pirh2 to bind GST-AIP4 was analyzed by immunoprecipitating with an AIP4-specific antibody and immunoblotting with a Pirh2-specific antibody or with an AIP4-specific antibody, as indicated. (E) Similar to (D), except that protein lysates were immunoprecipitated with a Pirh2-specific antibody and immunoblotting with the indicated antibodies.