I-FLICE (inhibitor of FLICE) is a catalytically inactive form FLICE (Caspase 8) and Mch4/FLICE2 (Caspase 10). I-FLICE shares sequence homologies to FLICE and Mch4/FLICE2 and binds to these two molecules as demonstrated by co-immunoprecipitation anlalysis. However, unlike the effector proteases FLICE and Mch4/FLICE2, I-FLICE does not bind to the adaptor molecule FADD. I-FLICE inhibits both TNFR-1 and CD-95 induced apoptosis. Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain (DD)- containing adapter molecules and members of the ICE/CED-3 protease family. Caspases-8 (FLICE) and -10 (FLICE2) are two pivotal members in the ICE/CED-3 protease family. FLICE-inhibitory proteins were identified in virus and human and designated v-FLIPs and FLIP, respectively. The human FLIP was also cloned by several labs independently and termed Casper, I-FLICE, FLAME-1, CASH and CLARP. FLIP contains two death effector domains (DEDs) and a caspase-like domain. FLIP interacts with adapter protein FADD and caspase-8 and -10, and potently inhibits apoptosis induced by all known death receptors. Four splice variants of c-FLIPs have been identified and termed FLIPa, b, g, and d, respectively.
CFLAR antibody can be used in ELISA, Western Blot, and immunohistochemistry starting at 5 μg/mL.
Protein G Column
PBS, 0.05% BSA, 0.05% sodium azide.
Aliquot and store at -20°C or below. Avoid multiple freeze-thaw cycles.