Prion protein (PrP) is a membrane glycosylphosphatidylinositol (GPI)-anchored glycoprotein that is encoded by the PRNP gene and is highly conserved among mammals. PrP contains an unstable region consisting of five octapeptide repeats; mutations in this region are associated with Creutzfeldt-Jakob disease (CJD), fatal familial insomnia, Gerstmann-Straussler disease, Huntington disease-like 1, and kuru (a type of transmissible spongiform encephalopathy, TSE). The function of PrP is not clear, although it is known to bind copper ions. PrP exists as a normal cellular isoform (PrPC) that can undergo refolding to a conformational isoform known as scrapie isoform (PrPSc). PrPSc forms compact aggregates that are highly resistant to proteolysis. The conversion of PrPC to PrPSc is postulated to be the mechanism involved in transmission of TSEs. PrP is also known as prion protein (p27-30); major prion protein, prion-related protein, CJD, GSS, ASCR, KURU, PRIP, PrPc, CD230, AltPrP, p27-30, PrP27-30, and PrP33-35C.
These products are affinity-purified IgG antibodies that recognize human PrP protein. The antibodies were raised in rabbit using synthetic peptides and can be used for Western blot (WB) detection or immunohistochemical (IHC) detection of human PrP protein.