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 (ADphospho-ribose) polymerase (PARP), gelsolin, DFF-45/ICAD and the nuclear lamins. PARP is a nuclear protein that is specifically cleaved by CPP32 and Mch2, but not by ICE, into a signature apoptotic fragment. Gelsolin is cleaved by CPP32 to an active form that severs actin filaments in a Ca2+-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 subunit of DNA fragmentation factor, is cleaved by CPP32 to generate an active factor that induces DNA fragmentation. The 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

Endonuclease 8-like 3; DNA glycosylase FPG2; DNA glycosylase/AP lyase Neil3; Endonuclease VIII-like 3; Nei-like protein 3; NEIL3

o00273

Human,Mouse,Rat

WB

WB 1:500-1:1000

~ 35, 45 kDa

Rabbit

This antibody detects endogenous levels of Cleaved-DFF45 (D224) protein.

Synthetic peptide, corresponding Human NEIL3.

Polyclonal

Rabbit IgG

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

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.