BID (Intermediate Domain) Blocking Peptide

BID (Intermediate Domain) Blocking Peptide

Product No.: B487

[product_table name="All Top" skus="B487"]

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Product Type
Blocking Peptide
Alternate Names

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Antibody Details

Product Details

Reactive Species
Product Concentration
0.2 mg/ml
Amino Acid Location
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.
Storage and Handling
Store this peptide in working aliquots at -20°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles.
Country of Origin
Next Day Ambient
Amino Acid Sequence
14 amino acids near the center of human Bid.
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.


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.

Antigen Details

References & Citations

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.
Disclaimer AlertProducts are for research use only. Not for use in diagnostic or therapeutic procedures.