|Bax (D2E11) Rabbit mAb 5023||20 µl||
|Bak (D4E4) Rabbit mAb 12105||20 µl||
||H M R Mk||25||Rabbit IgG|
|Bok (D7V2N) Rabbit mAb 86875||20 µl||
|Bim (C34C5) Rabbit mAb 2933||20 µl||
||H M R||12, 15, 23||Rabbit IgG|
|Bad (D24A9) Rabbit mAb 9239||20 µl||
||H M R Mk||23||Rabbit IgG|
|BID Antibody 2002||20 µl||
|Puma (D30C10) Rabbit mAb 12450||20 µl||
|Noxa (D8L7U) Rabbit mAb 14766||20 µl||
|Bik Antibody 4592||20 µl||
|Anti-rabbit IgG, HRP-linked Antibody 7074||100 µl||
Monoclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to residues surrounding Leu45 of human Bax, Gly75 of human Bak, Val88 of human Bok, Pro25 of human Bim, Pro102 of human Bad, Leu45 of human Bax, Pro25 of human Bim, residues near the carboxy terminus of human Puma, and residues near the amino terminus of human Noxa. Polyclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to the amino-terminus of human Bik or residues surrounding the cleavage site of human BID. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
The Bcl-2 family consists of a number of evolutionarily conserved proteins containing Bcl-2 homology domains (BH) that regulate apoptosis through control of mitochondrial membrane permeability and release of cytochrome c (1-3). Four BH domains have been identified (BH1-4) that mediate protein interactions. The family can be separated into three groups based upon function and sequence homology: pro-survival members include Bcl-2, Bcl-xL, Mcl-1, A1 and Bcl-w; pro-apoptotic proteins include Bax, Bak and Bok; and "BH3 only" proteins Bad, Bik, Bid, Puma, Bim, Bmf, Noxa and Hrk. Interactions between death-promoting and death-suppressing Bcl-2 family members has led to a rheostat model in which the ratio of pro-apoptotic and anti-apoptotic proteins controls cell fate (4). Thus, pro-survival members exert their behavior by binding to and antagonizing death-promoting members. In general, the "BH3-only members" can bind to and antagonize the pro-survival proteins leading to increased apoptosis (5). While some redundancy of this system likely exists, tissue specificity, transcriptional and post-translational regulation of many of these family members can account for distinct physiological roles.
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