Cf cas3

Cells were lysed in the presence of protease and phosphatase inhibitors (Roche Diagnostics, Indianapolis, IN, USA). Whole-cell lysates were subjected to SDS-polyacrylamide gel electrophoresis, electrophoretically transferred onto polyvinylidene difluoride (PVDF) membranes (Thermo Fisher, Inc., Rockford, IL, USA), and immunoblotted with anti-Mcl-1 (4572), -PARP (9542), -Bim (2819), -Bak (3814), -Bax (2774), -c-Myc (5605s), -cleaved caspase-3 (9661, designated -cf-Cas3; Cell Signaling Technology, Danvers, MA, USA), or -β-actin (A2228; Sigma-Aldrich) antibody, as previously described.^{37 (link),38 (link)} Immunoreactive proteins were visualized using the Odyssey Infrared Imaging System (Li-Cor, Lincoln, NE, USA), as described by the manufacturer. Western blots were repeated at least three times, and one representative blot is shown. Densitometry measurements were made using Odyssey V3.0 (Li-Cor), normalized to β-actin, and calculated as the fold change compared to the corresponding no drug treatment control.

Cells were lysed in the presence of protease and phosphatase inhibitors (Roche Diagnostics, Indianapolis, IN, USA). Whole cell lysates were subjected to SDS‐polyacrylamide gel electrophoresis, electrophoretically transferred onto polyvinylidene difluoride membranes (Thermo Fisher Scientific, Waltham, MA, USA) and immunoblotted with anti‐Bcl‐2 (Abcam, Cambridge, MA, USA), ‐Bcl‐xL, ‐Mcl‐1, ‐PARP, ‐Bim, ‐Bak, ‐Bax, ‐cleaved caspase‐3 (designated ‐cf‐Cas3; Cell Signaling Technology, Danvers, MA, USA), or ‐β‐actin (Sigma‐Aldrich) antibody, as previously described.41, 42 Immunoreactive proteins were visualized using the Odyssey Infrared Imaging System (Li‐Cor, Lincoln, NE, USA), as described by the manufacturer. Western blots were repeated at least 2 times and one representative blot is shown. Densitometry measurements were made using Odyssey V3.0 (Li‐Cor), normalized to β‐actin, and calculated as the fold change compared to the corresponding no drug treatment control.