The function of Bad, a proapoptotic member of the Bcl-2 family, is regulated primarily by rapid changes in phosphorylation that modulate its protein-protein interactions and subcellular localization. Human Bad, which is 43 amino acids shorter than its mouse counterpart, is cleaved by a caspase upon exposure of Jurkat T cells to anti-FAS antibody, tumor necrosis factor alpha (TNF-alpha), or TRAIL. Moreover, a truncated form of human Bad lacking the N-terminal 28 amino acids is more potent than wild-type Bad in inducing apoptosis. Bad plays a novel and important role in maintaining the apoptotic phenotype in response to various apoptosis inducers.
|Product By Gene ID
- BCL-X/BCL-2 binding protein
- Bcl-XL/Bcl-2-associated death promoter
- BCL2-binding protein
- Bcl-2-like protein 8
- BCL2-binding component 6
- Bcl-2-binding component 6
- BCL2-antagonist of cell death protein
- bcl2 antagonist of cell death
- BCL2-associated agonist of cell death
Research Areas for cleaved BAD
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