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. 2008 May 5;105(19):6936–6941. doi: 10.1073/pnas.0710831105

Fig. 6.

Fig. 6.

Interaction between Osx and Tcf1. (A) Coimmunoprecipitation (CoIP) of Osx and Tcf1 in transfected HEK293 cells. Here, 1 μg of pEX-HA-Osx and pCDNA-Tcf1 were cotransfected or transfected alone into HEK293 cells. Whole-cell lysates (WCL) were immunoprecipitated with anti-HA (10 μl) and the precipitate was immunoblotted with anti-Tcf1. (B) No disruption of β-catenin interaction with Tcf1 by Osx. (Upper) GST-β-catenin was used to pull down 35S labeled Osx. Ten percent of the synthesized Osx was used as an input, and GST was used as a control. (Lower) GST-β-catenin was used to pull down 35S-labeled Tcf1. Baculovirus-expressed Osx was used as Osx protein source. (C) Disruption of Tcf1 binding to DNA by Osx. Osx and Tcf1 proteins were synthesized by TNT IVTT systems. Tcf1 bound to Tcf 1 binding probe in EMSA. TNT lysates containing pEX-Osx and control TNT lysates with pEX were added to the DNA binding reaction.