Bad is an important regulatory protein involved in the control of cell survival and apoptosis, and is a member of the BH3-only family of proteins such as Bim and Bid that share homology with Bcl-2 only in the BH3 domain. Phosphorylated Bad is sequestered in the cytosol by 14-3-3 proteins under normal conditions, but is dephosphorylated and activated following apoptotic signals. Apoptotic stimuli induce Bad dephosphorylation by a number of phosphatases (e.g., calcineurin) and recruitment to the mitochondria, where Bad heterodimerizes with and inhibits prosurvival proteins of the Bcl family. In contrast, survival signals lead to phosphorylation of Bad at multiple serine residues, including phosphorylation at Ser112 and Ser136 which induce association with 14-3-3 proteins. Phosphorylation at Ser112 and Ser136 is required for a third phosphorylation event at Ser155, which induces dissociation of Bad/Bcl heterodimers to promote cell survival. This antibody specifically binds the Bad protein, but does not recognize Bad/Bcl-2 heterodimers in immunoprecipitation assays.

• For Immunohistochemistry, Western Blot

Recognizes mouse, rat, bovine, dog (weak), chicken (weak), Drosophila, hamster, monkey, pig, rabbit and sheep Bad. Detects a band of ~23kDa by Western blot.

Type: Primary
Antigen: BAD
Clonality: Polyclonal
Clone:
Conjugation:
Epitope:
Host: Rabbit
Isotype:
Reactivity: Mouse