Description
Product Characteristics:
Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing the inhibitory effect of growth factor on Bad-mediated apoptosis. Cdc2-induced phosphorylation of Bad serine 128 has an inhibitory effect on its interaction with 14-3-3 proteins. The latter interaction is critical for Bad phosphorylation at serine 155, a site within the BH3 domain that leads to the release of BclxL and the promotion of cell survival. Alternative splicing of this gene results in two transcript variants which encode the same isoform.
Subcellular location: Cytoplasm, Cell membrane
Synonyms: Bad phospho S99, Bad phospho Ser99, p-Bad S99,p- Bad Ser99, p-Bad phospho Ser99, BBC 2, BBC2, BBC6, Bcl 2 Antagonist of Cell Death, Bcl 2 Binding Component 6, BCL X / BCL 2 Binding Protein, BCL X Binding Protein, Bcl XL/Bcl 2 Associated Death Promoter, Bcl-2-like protein 8, Bcl2 antagonist of cell death, BCL2 antagonist of cell death protein, BCL2 associated agonist of cell death, Bcl2 Associated Death Promoter, BCL2 binding component 6, BCL2 binding protein, Bcl2 Like 8 Protein, Bcl2-L-8, BCL2L8, BclXL, Proapoptotic BH3 Only Protein, BAD_HUMAN, Bcl-2-binding component 6.
Target Information: The protein encoded by this gene is a member of the BCL-2 family. BCL-2 family members are known to be regulators of programmed cell death. This protein positively regulates cell apoptosis by forming heterodimers with BCL-xL and BCL-2, and reversing their death repressor activity. Proapoptotic activity of this protein is regulated through its phosphorylation. Protein kinases AKT and MAP kinase, as well as protein phosphatase calcineurin were found to be involved in the regulation of this protein. Alternative splicing of this gene results in two transcript variants which encode the same isoform. [provided by RefSeq, Jul 2008]