BID (Intermediate Domain) Blocking Peptide

14 amino acids near the center of human Bid.

This peptide is formulated in PBS pH 7.2 (0.01 M Sodium Phosphate, 0.13 M NaCl) containing 0.1% bovine serum albumin and 0.02% sodium azide.

Store this peptide in working aliquots at -20°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles.

Next Day Ambient

14 amino acids near the center of human Bid.

Bid is a member of the Bcl-2 family of proteins that regulates outer mitochondrial membrane permeability. Bid is a pro-apoptotic member that causes cytochrome c to be released from the mitochondria intermembrane space into the cytosol. In healthy cells Bid is cytosolic. In response to Fas ligand or TNF Bid is cleaved by caspase-8 and it then relocates to the mitochondria outer membrane. Cleavage of Bid by caspase-8 generates a new N-terminal that contains a terminal glycine. It appears that the glycine is myristoylated and myristoylation serves to target Bid to the mitochondria. Bid may then interact with another pro-apoptotic Bcl-2 family member Bak. Interaction of Bid with Bak causes altered mitochondrial membrane permeability. A 9 - 13 amino acid stretch called the BH3 region (Bcl-2 homology region) appears to mediate the Bid interaction with other Bcl-2 family members. Bid is neutralized by binding to the anti-apoptotic member Bcl-x.

1. Jaffer ZM and Chernoff J. p21-activated kinases: three more join the Pak. Int. J. Biochem. Cell Biol. 2002; 34:713-7. 2. Rudel T and Bokoch GM. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 1997; 276:1571-4. 3. Vilas GL, Corvi MM, Plummer GJ, et al. Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events. Proc. Natl. Acad. Sci. USA 2006; 103:6542-7.