Polyclonal Antibody to FLIPγ/δ (CT)

Apoptosis is related to many diseases and can also be 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 caspase-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 c-FLIPs, respectively [1,2]. The human FLIPs were also cloned by several labs independently and termed Casper, I-FLICE, FLAME-1, CASH, CLARP and Usurpin, respectively [3-8]. FLIP contains two death effector domains (DEDs) and a caspase-like domain. FLIP interacts with adapter proteins FADD and caspase-8 and caspase-10, and potently inhibits apoptosis induced by death receptors CD95, DR3, TRAIL-R and TNF-R1. Four splice variants of c-FLIPs have been identified and termed FLIPα, β, γ, and δ, respectively [9].