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Description
The monoclonal antibody 1.5D7 recognizes the disease associated isoform of the prion protein termed PrPSc. Prion diseases, also known as spongiform encephalopathies, are a group of neurodegenerative diseases that include BSE (bovine spongiform encephalopathy) in cattle, scrapie in sheep and CJD (Creutzfeldt-Jakob disease) in humans. The normal cellular form of the prion protein is denoted as PrPC and is a constitutively expressed glycosylphosphatidylinositol anchored protein that has been shown to play a role in myelin formation. PrPC has an unstructured N-terminal part and a C-terminal part consisting of three α -helices and two short β strands. Refolding of the normal prion protein results in PrPSc, which has a tightly packed C-terminal part enriched in beta sheets which is insoluble and resistant to digestion by proteases. Prion diseases are characterized by the deposition of highly structured aggregates of PrPSc, astrocytosis, neuronal cell death and spongiform structures in the brain. These diseases can be sporadically (unknown cause), be inherited due to polymorphisms or mutations in the prion protein gene or be transmitted by an infectious particle which is believed to consist of PrPSc only. In order to study prion diseases the detection of PrPSc and the ability to discriminate between the normal and disease associated PrP is of pivotal importance. The monoclonal antibody 1.5D7 can be used for the specific identification and characterization of PrPSc in tissue sections by immunohistochemistry and PET-blot.