Anti-BIK antibody produced in rabbit

BIK (BCL2 interacting killer) is the founding member of the BH3 (BCL2 homology domain 3)-only pro-apoptotic protein family. This protein shows major localization to the ER (endoplasmic reticulum). It shares two domains with other BCL2 (B cell lymphoma) family proteins, namely BH3 domain and the trans-membrane domain. BIK is a 160-residue phosphoprotein and is highly conserved among primates. This gene is localized to human chromosome 22q13.2.

a 15 amino acid peptide from near the amino-terminus of human BIK.

BIK (BCL2 interacting killer) induces the release of calcium from ER (endoplasmic reticulum) to the mitochondria and mitochondrial cristae remodeling, thus, promoting apoptosis via the mitochondrial pathway. In certain types of cells, this protein also promotes non-apoptotic cell death through yet unknown mechanisms. It is critical in apoptosis induced by viral infections, cytokines and toxins. It is responsible for the selection of mature B cells in humans, and also functions as a pro-apoptotic tumor suppressor in various human tissues. Deletions in the BIK chromosomal locus or epigenetic silencing of BIK gene results in its inactivation in multiple types of cancers. BIK is up-regulated during hepatitis C virus (HCV), mediated by the viral protein NS5B (nonstructural protein 5B), and is crucial for HCV RNA replication and viral release. Studies have shown that BikDD, a constitutively active mutant of BIK, functions as a potent anti-tumor protein in preclinical pancreatic, lung and breast cancer models. Further mutation of BikDD produces BikDDA, which has a longer half-life and has potent pro-apoptotic activity in triple-negative breast cancer (TNBC).

The action of this antibody can be blocked using blocking peptide SBP3819.

Solution in phosphate buffered saline containing 0.02% sodium azide

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