Clusterin / Apolipoprotein J (RM437), RMab

Summary and Explanation

The Clusterin protein, also known as Apolipoprotein J, is a 75-80 kDa disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid. It is a stress-induced cytoprotective chaperone protein regulated by HSF1 and functions similarly to a small heat-shock protein. Clusterin is distributed widely in human tissues and fluids, including normal epithelial cells, plasma, cerebrospinal fluid, breast milk, semen and urine. Clusterin has been implicated in a variety of activities including programmed cell death, regulation of complement mediated cell lysis, membrane recycling, cell-cell adhesion, and src induced transformation. As part of the attack complex of complement, it acts as a complement inhibitor. Clusterin is expressed in a wide variety of hematopoietic and non-hematopoietic tumors. Overexpression of Clusterin is associated with poor prognosis in breast cancer and chemosensitivity in cervical cancer.