Figure 9
From: The Drosophila Fry protein interacts with Trc and is highly mobile in vivo
Fry and N-Fry co-immunoprecipitate with Trc-FLAG. A. Shows the detection by mouse anti-Flag of the proteins pulled down by rabbit-anti-FLAG antibody. The Trc-FLAG fusion protein is approximately 52 kDa, and is only detected when both UAS-trc-FLAG and actin-GAL4 are present. B. Full-length Fry co-immunoprecipitated with Trc-FLAG. Trc-FLAG was pulled down using rabbit-anti-FLAG antibody and the Western Blot was probed using mouse-anti-GFP antibody. Full-length Fry-GFP (418 kDa) is detected only from extracts made from discs that expressed UAS-trc-FLAG and UAS-myc-fry-GFP together by actin-GAL4. C. Myc-N-Fry co-immunoprecipitated with Trc-FLAG (pulled down by rabbit-anti-FLAG antibody and detected by mouse-anti-Myc antibody) (size of the protein detected by the anti-myc antibody was smaller than the predicted size of Myc-N-Fry, which should be ~180 kDa. A band of the same size was also detected in western blots of extracts of discs that expressed Myc-N-Fry and it is likely to be a degradation product.