Polyclonal Antibody to Caspase-10 (CT)

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. A novel ICE/CED-3 protease was identified recently, designated FLICE2 and Mch4 [1,2] and renamed as caspase-10. Caspase-10 has two death effector domains (DEDs) that bind to the DED in the adapter molecule FADD and recruits both TNFR1 and CD95 to form complexes with these receptors. Caspase-10 is therefore involved in the CD95 and TNFR1 induced apoptosis [1]. Caspase-10 cleaves and activates caspase-3, -4, -6, -7, -8 and -9, which causes the proteolytic cleavage of many key proteins such as PARP. Cleavage of PARP occurs in many different systems during apoptosis and is the hallmark of programmed cell death [3]. Caspase-10 is expressed in many tissues and cell lines [1,2].