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. 2012 Nov 9;287(53):44151–44163. doi: 10.1074/jbc.M112.372540

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© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 2. — K_V10.1 is able to pull down CTTN in vitro. K_V10.1-BBS or K_V10.2-BBS were labeled with BTX-biotin (+Bb) in lysates of HEK293 cells expressing either K_V10.1-BBS or K_V10.2-BBS, pulled down, and washed rigorously using streptavidin-coated beads. The streptavidin-precipitated proteins were then used in pull-down experiments with various GST-CTTN fusion proteins that were then analyzed by SDS-PAGE followed by immunoblotting using an anti-GST antibody (Santa Cruz Biotechnology) (A, B, and D) or Coomassie staining (E). Unlabeled cell lysates served as a negative control (−Bb). Both K_V10.1 and K_V10.2 were able to precipitate the full-length GST-CTTN (A) but not GST alone (B). C, schematic representation of the various CTTN domain GST-tagged proteins using pull-down assays with K_V10.1-BBS. Of these CTTN-domain containing fusions only the HP region was precipitated by K_V10.1-BBS (D). Specific pull down of GST-HP-region of CTTN by K_V10.1 was also confirmed in Coomassie stained gels (E).