|Detection of Human CIDEA by Western Blot. Western blot shows lysates of human heart tissue. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human CIDEA Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7137) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for CIDEA at approximately 27 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
CIDEA (Cell death-Inducing DNA fragmentation factor-alpha -like Effector A) is a 24-27 kDa member of the CIDE family of molecules. It is expressed in human adipocytes and striated muscle, plus mouse brown adipocytes and hepatocytes, and appears to have at least two functions. In the cytoplasm of fat cells, CIDEA localizes to lipid droplets and ER, and promotes the formation of lipid droplets at the expense of lipolysis and AMPK activity. In the nucleus, CIDEA apparently binds to LXR, and is capable of inducing apoptosis. CIDEA undergoes O-linked glycosylation. When glycosylated, CIDEA is nuclear; when nonglycosylated, CIDEA is cytoplasmic. Human CIDEA is 219 amino acids (aa) in length, and contains one CIDE domain (aa 33-110) that potentially mediates dimerization. CIDEA reportedly homodimerizes, and heterodimerizes with CIDEB. There is one potential isoform variant that possesses a 46 aa substitution for aa 1-12. Over aa 61-162, human CIDEA shares 89% aa identity with mouse CIDEA.
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