Recombinant Human BID Protein

The BH3 interacting domain death agonist (BID) is a pro-apoptotic member of the Bcl-2 protein family; which contains only the BH3 domain; and is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. BID is important to cell death mediated by these proteases and thus is the sentinel to protease-mediated death signals. Recent studies further indicate that Bid may be more than just a killer molecule; it could be also involved in the maintenance of genomic stability by engaging at mitosis checkpoint. BID is an integrating key regulator of the intrinsic death pathway that amplifies caspase-dependent and caspase-independent execution of neuronal apoptosis. Therefore pharmacological inhibition of BID provides a promising therapeutic strategy in neurological diseases where programmed cell death is prominent. BID is activated by Caspase 8 in response to Fas/TNF-R1 death receptor activation. Activated BID is translocated to mitochondria and induces cytochrome c release; which in turn activates downstream caspases. BID action has been proposed to involve the mitochondrial re-location of its truncated form; tBid; to facilitate the release of apoptogenic proteins like cytochrome c.