Figure 2
Figure 2. BCR-ABL1 interacts with RAD51 in a kinase-independent manner. BCR-ABL1 nonmutated (nm) and the kinase defective (KD) mutant were IVTT and analyzed by Western blotting with the use of anti-ABL1 (A, top left box) and antiphosphotyrosine (B, left box) antibodies to detect BCR-ABL1 and phosphotyrosine proteins (p-Tyr), respectively. IVTT products were incubated with GST-RAD51 in the kinase buffer supplemented with adenosine triphosphate. The presence of BCR-ABL1 in a GST-RAD51 pull-downs (A, top right box) and tyrosine phosphorylation of GST-RAD51 (B, top right box) was detected by Western analysis with the use of anti-ABL1 and antiphosphotyrosine antibodies, respectively. GST-fusion proteins were detected by Ponceau red staining (bottom boxes).

BCR-ABL1 interacts with RAD51 in a kinase-independent manner. BCR-ABL1 nonmutated (nm) and the kinase defective (KD) mutant were IVTT and analyzed by Western blotting with the use of anti-ABL1 (A, top left box) and antiphosphotyrosine (B, left box) antibodies to detect BCR-ABL1 and phosphotyrosine proteins (p-Tyr), respectively. IVTT products were incubated with GST-RAD51 in the kinase buffer supplemented with adenosine triphosphate. The presence of BCR-ABL1 in a GST-RAD51 pull-downs (A, top right box) and tyrosine phosphorylation of GST-RAD51 (B, top right box) was detected by Western analysis with the use of anti-ABL1 and antiphosphotyrosine antibodies, respectively. GST-fusion proteins were detected by Ponceau red staining (bottom boxes).

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