Anti-CIDE-A Antibody

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 containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. DFF45/ICAD has been identified as inhibitor of caspase activated DNase DFF40/CAD. DFF45 related proteins CIDE-A and CIDE-B (for cell death-inducing DFF-like effector A and B) were recently identified. CIDE contains a new type of domain termed CIDE-N, which has high homology with the regulatory domains of DFF45/ICAD and DFF40/CAD. Expression of CIDE-A induces DNA fragmentation and activates apoptosis, which is inhibited by DFF45. CIDE-A is a DFF45-inhibitable effector that promotes cell death and DNA fragmentation. CIDE-A is expressed in many tissues.

CIDE-A antibody was raised against an 18 amino acid peptide near the carboxy terminus of mouse CIDE-A. The immunogen is located within the last 50 amino acids of CIDE-A.

Acts as a CEBPB coactivator in mammary epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter (By similarity) . Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair and occurs at a lower rate than that promoted by CIDEC. When overexpressed, induces apoptosis. The physiological significance of its role in apoptosis is unclear.