c-IAP2 Recombinant Rabbit mAb (S-3395)

Cellular inhibitor of apoptosis protein 2 (c-IAP2, gene BIRC3) is a 618-residue member of the IAP family containing three N-terminal baculoviral IAP repeat (BIR) domains that bind caspases, a central caspase-recruitment domain (CARD) that auto-inhibits its own ubiquitin-ligase activity, and a C-terminal RING domain that endows potent E3 ubiquitin-ligase activity; through this enzymatic function c-IAP2 polyubiquitinates receptor-interacting protein 1 (RIP1) and NF-κB-inducing kinase (NIK), thereby driving canonical NF-κB prosurvival signaling while suppressing non-canonical NF-κB activation, controls TNF-α-mediated apoptosis, regulates innate immunity downstream of Toll-like and NOD-like receptors, and is frequently amplified or over-expressed in multiple cancers where its anti-apoptotic activity contributes to chemoresistance, making it a prime target for small-molecule Smac mimetics that induce its autoubiquitination and proteasomal degradation.