Bid is a pro-apoptotic ''BH3 domain-only member of the Bcl-2 family originally discovered to interact with both the anti-apoptotic family member Bcl-2 and the pro-apoptotic protein Bax. Bid is normally localized in the cytosolic fraction of cells as an inactive precursor and is cleaved at Asp60 by caspase-8 during Fas signaling, leading to translocation of the carboxyl terminal p15 fragment (tBid) to the mitochondrial outer membrane. Translocation of Bid is associated with release of cytochrome c from the mitochondria, leading to complex formation with Apaf-1 and caspase-9 and resulting in caspase-9 activation. Thus, Bid relays an apoptotic signal from the cell surface to the mitochondria triggering caspase activation.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.4.
Application Dilute:
WB: 1:2000~1:5000 IP:1:2000~1:8000 IHC:1:50~1:100
Application Notes:
BID polyclonal antibody detects endogenous levels of BID protein.
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