ICAD (Q177) polyclonal antibody

The CED/ICE family of cysteine proteases plays a pivotal role in mediating apoptosis through the proteolysis of specific targets. Among the targets are poly (ADP-ribose) polymerase (PARP), gelsolin, DFF-45/ICAD and the nuclear lamins. PARP is a 112 kDa nuclear protein that is specifically cleaved by CPP32 and Mch2, but not by ICE, into a signature 85 kDa apoptotic fragment. Gelsolin is cleaved by CPP32 to an active form that severs actin filaments in a Ca++-independent manner. In addition to binding actin, gelsolin can form complexes with fibronectin, which may be important for localizing gelsolin to inflammatory sites. DFF-45/ICAD, the 45 kDa subunit of DNA fragmentation factor, is cleaved by CPP32 to generate an active factor that induces DNA fragmentation. The 70 kDa nuclear Lamin A is cleaved by Mch2, but not CPP32. Nuclear Lamin B is fragmented as a consequence of apoptosis by an unidentified member of the ICE family.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of IDCAD (Q177) polyclonal antibody at 1:500 dilution Lane1:C6 whole cell lysate (40ug) Lane2:CT26 whole cell lysate (40ug) Lane3:HCT116 whole cell lysate (40ug) Lane4:COS-7 whole cell lysate (40ug) Lane5:SGC7901 whole cell lysate (40ug)