Mouse Monoclonal BID Antibody

BID (BH3-interacting domain death agonist) is a pro-apoptotic protein belonging to the Bcl-2 family, critical in regulating mitochondrial-dependent apoptosis. It exists as an inactive cytosolic monomer (full-length BID) until activated by proteolytic cleavage (e.g., by caspase-8 or granzyme B), generating truncated BID (tBID). This activated form translocates to mitochondria, where it induces oligomerization of BAX/BAK, triggering outer mitochondrial membrane permeabilization (MOMP) and cytochrome c release, ultimately activating caspases for apoptosis execution. BID serves as a molecular bridge connecting extrinsic (death receptor) and intrinsic (mitochondrial) apoptosis pathways. Dysregulation of BID is implicated in cancer, neurodegenerative diseases, and liver injury. Anti-BID antibodies are essential tools for detecting BID expression, activation status (via cleavage-specific epitopes), and subcellular localization in research. They enable studies on apoptosis mechanisms, drug responses, and disease pathogenesis. Commercial antibodies typically target specific regions (e.g., BH3 domain or cleavage sites) and require validation in applications like Western blotting, immunohistochemistry, and flow cytometry. Proper controls are crucial due to potential cross-reactivity with other Bcl-2 family proteins.