Peptides  >  Prion Protein (PrP) Fragments
Prion diseases are a group of transmissible neurodegenerative disorders that include kuru, Creutzfeld–Jakob disease, Gerstmann–Sträussler–Scheinker disease in humans, and scrapie and bovine spongiform encephalopathy in animals. Prion-related encephalopathies are characterized by the intracerebral accumulation of an abnormal isoform of the cellular prion protein (PrPC) named scrapie prion protein (PrPSc). Prion and nonprion (cellular) isoforms of one and the same protein can have identical amino acid sequences but differ from each other in conformation and ability to form aggregated multimolecular structures. The pathological forms of this protein and its cellular precursor are not only expressed in the brain but also, at lower concentrations in the peripheral tissues. Unlike Alzheimer’s Disease, prion disease is associated with a peripheral component in that the presumed causative agent, PrPSc, also accumulates in the spleen and other lymphoreticular organs.

Ref:Horonchik, L. et al. J. Biol. Chem. 280, 17062 (2005); Cunningham, C. et al. J. Virol. 79, 5174 (2005); Allen, K. et al. Genetics 169, 1227 (2005); Diomede, L. et al. Biochem. J. 320, 563 (1996); Cashman, NR. et al. Cell 61, 185 (1990); Meiner, Z. et al. Neurology 42, 1355 (1992).
 Product Size Catalog # US$  
PrP (106 - 126)
1 mg AS-61160 $176
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