c-IAP2 (58C7) Rabbit mAb

The inhibitor of apoptosis protein (IAP) family consists of an evolutionarily conserved group of apoptosis inhibitors containing a conserved 70 amino acid BIR (baculovirus inhibitor repeat) domain (1,2). Human members of this family include c-IAP1, c-IAP2, XIAP, survivin, livin, and NAIP. Overexpression of IAP family members, particularly survivin and livin, in cancer cell lines and primary tumors suggests an important role for these proteins in cancer progression (3-5). In general, the IAP proteins function through direct interactions to inhibit the activity of several caspases, including caspase-3, caspase-7, and caspase-9 (5,6). In addition, binding of IAP family members to the mitochondrial protein Smac blocks their interaction with caspase-9, thereby allowing the processing and activation of the caspase (2). 1.Deveraux, Q.L. and Reed, J.C. (1999) Genes Dev 13, 239-52. 2.Deveraux, Q.L. et al. (1998) EMBO J 17, 2215-23. 3.Altieri, D.C. et al. (1999) Lab Invest 79, 1327-33. 4.Tamm, I. et al. (2000) Clin Cancer Res 6, 1796-803. 5.Kasof, G.M. and Gomes, B.C. (2001) J Biol Chem 276, 3238-46. 6.Deveraux, Q.L. et al. (1997) Nature 388, 300-4.