Mouse Clusterin DuoSet ELISA

An alternately spliced 50 kDa isoform of mouse Clusterin (nCLU) remains intracellular and is neither glycosylated nor cleaved into alpha and beta chains (4). Cellular exposure to ionizing radiation promotes the translocation of nCLU to the nucleus where it interacts with Ku70 and promotes apoptosis (4, 10). This function contrasts with the cytoprotective effect of secreted Clusterin (11). High µg/mL concentrations of Clusterin circulate predominantly as a component of high density lipoprotein particles, and these are internalized and degraded through interactions with LRP-2/Megalin (12, 13). The ability of Clusterin to bind and neutralize non-oxidatively modified LDL reduces cytotoxicity in atherosclerotic plaques (14). The chaperone function of Clusterin also helps to reduce the accumulation of beta-amyloid fibrils and damage due to amyloid plaques in Alzheimer's disease (15). Clusterin levels are elevated in the cerebrospinal fluid of patients with Alzheimer's disease, Parkinson's disease, and multiple sclerosis (9, 16, 17) and in the urine of patients with kidney injury or bladder cancer (18-20). Clusterin is released by activated platelets at sites of vascular injury and is found in the synovial fluid of rheumatoid arthritis and osteoarthritis patients (21, 22). During human tumor progression, nCLU is downregulated while the secreted form is upregulated and may be aberrantly glycosylated (10, 23-25). Increased circulating levels of Clusterin enhance tumor aggressiveness by inhibiting apoptosis and by promoting epithelial to mesenchymal transition (26-28).