c-IAP2抗体(F-20): sc-1957

The baculovirus protein p35 inhibits virally induced apoptosis of invertebrate and mammalian cells and may function to impair the clearing of virally infected cells by the immune system of the host. This is accomplished at least in part by the ability of p35 to block both TNF- and FAS-mediated apoptosis through the inhibition of the ICE family of serine proteases. Three mammalian homologs of baculovirus p35, designated MIHA (mammalian IAP homolog A), MIHB and MIHC have been described. These three mammalian inhibitor of apoptosis proteins (IAPs) are designated XIAP, c-IAP1 and c-IAP2, respectively. XIAP, c-IAP1 and c-IAP2 share an N-terminal baculovirus IAP repeat (BIR) motif and a C-terminal RING finger. Although c-IAP1 and c-IAP2 do not directly associate with the TNF receptor (TNF-R), they efficiently block TNF-mediated apoptosis through their interaction with the downstream TNF-R effectors, TRAF1 and TRAF2. The interaction between the TRAF1/TRAF2 heterocomplexes and c-IAPs is dependent on a functional BIR motif.