Members in the Bcl-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. Bcl-2 homology 3 (BH3) domain containing pro-apoptotic proteins, such as Bax, Bid, and Bik, form a growing subclass of the Bcl-2 family. Another such protein is the Bcl-2-antagonist of cell death (Bad). Bad regulates apoptosis by forming heterodimers with anti-apoptotic proteins Bcl-2 and Bcl-xL, thereby preventing them from binding with Bax. Bad activity is regulated by its phosphorylation, it is inactivated by kinases such as Akt and MAP kinase and thus promotes cell survival, whereas JNK-induced phosphorylation promotes the apoptotic role of Bad.
Immunohistochemistry: Use at 2 µg/mL. Western blot: Recommend 0.5-1.0 µg/mL. The optimal dilution for a specific application should be determined by the researcher. Figure 1. Western blot analysis of Bad in T24 cell lysates with anti-Bad at (A) 0.5, (B) 1 and (C) 2 µg/mL. Figure 2. Immunohistochemical staining of rat thymus using anti-Bad at 2 µg/mL.