anti-cIAP 1and 2
The cellular inhibitor of apoptosis 1 and 2 (c-IAP1 and c-IAP2) proteins were identified based on their homology to a family of viral and cellular IAP proteins known to bind to caspases and inhibit their activity (1). Both cIAP1 and cIAP2 contain three characteristic baculovirus IAP repeat domains that facilitate binding to caspases and other proteins (2, 3). In addition, they contain a caspase recruitment domain of unknown function and a RING finger domain that functions as an E3 ubiquitin ligase (4). The precise biologic roles of c-IAP1 and c-IAP2 are currently not known. Biochemical data have indicated that c-IAP1 and c-IAP2, initially thought to be caspase inhibitors (2), can bind to caspases but do not directly inhibit them (5). Instead, recent studies show c-IAP1 and c-IAP2 regulate TNF alpha -mediated NF-kappa B signaling and are required to protect cells against and TNF alpha - and Interleukin-1 beta -induced apoptosis (6-9).
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