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. 2010 Apr 20;10:40. doi: 10.1186/1471-213X-10-40

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Copyright ©2010 Fang et al; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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.