Anti-BID antibody produced in rabbit

synthetic peptide corresponding to N-terminal of cleavage site [59/60] of mouse BID.

Polyclonal anti-BID antibody produced in rabbit is suitable for western blotting by using mouse L929 cells treated with TNF-α. It is also suitable for microarray.

The protein encoded by this gene is a member of the BCL-2 family of cell death regulators and is localized on to chromosome 22q11.2. BID is activated by caspase 8 in response to Fas/TNF-R1 receptor activation. Activated BID then translocated to mitochondria where it induces cytochrome c release, which in turn activates downstream caspases. It is a BH3 interacting death domain that heterodimerizes with either agonist BAX or antagonist BCL2. BID initiates apoptosis by binding to regulatory sites on prosurvival BCL2 proteins to directly neutralize their function. Additionally, BID interacts with cathepsins play an important role in the actions of Camptothecin on breast cancer cells.

Supplied as a solution in Dulbecco′s phosphate buffered saline (without Mg²⁺ and Ca²⁺), pH 7.3, with 50% glycerol, 1.0 mg/ml BSA (IgG and protease free) and 0.05% sodium azide.

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