CD230 (PrP) Monoclonal Antibody (4D5), eBioscience™, Invitrogen™

Description

• CD230 (prion protein; PrP^C) is a 35 kD glycoprotein, attached to the cell surface via a GPI-anchor
• While the function of CD230 is unclear, prion protein has been the focus of research based on its involvement in transmissible spongiform encephalopathies (TSE), including Creutzfeld-Jakob disease in humans
• CD230 undergoes a conformational change in which the cellular PrP^C form is converted to the scrapie PrP^Sc form
• This conversion is essential for the infectiousness of prion-based diseases
• CD230 is predominantly expressed on the surface of lymphocytes and monocytes, with weak expression on granulocytes and erythrocytes
• In platelets, CD230 is expressed primarily intracellularly, and is upregulated to the surface upon activation
• Human prion protein (PrP), also known as PRNP, is a ubiquitously expressed GPI-anchored cell surface glycoprotein associating with lipid raft components and functioning as a signaling molecule
• PrP plays a role in apoptosis in a cell context-dependent manner, is involved in proliferation of epithelial cells and in distribution of junction-associated proteins in human enterocytes
• Conversion of this normal cellular prion protein (PrPc) into an abnormal conformer (PrPSc) is the crucial step associated with triggering the pathogenesis of the prion neurodegenerative disorders, such as the Creutzfeld-Jakob disease (CJD)
• Whereas PrPc is rich in alpha-helices, the PrPSc form has higher content of beta-sheets and is resistant to proteinase K.