Goat Anti-Human PRNP (N-terminal) polyclonal antibody for ELISA, IHC, WB. The prion protein is a large membrane protein that occurs normally in neurons of the human brain and is thought to be involved in synaptic transmission. In prion diseases, such as Creutzfeld-Jakob disease (CJD), Gerstmann-Straussler-Scheinker syndrome (GSS), Fatal Familial Insomnia (FFI), Alpers Syndrome and Kuru, the normal cellular form of this protein (PrPc) is transformed into an altered protein when it comes into contact with an infectious prion protein (PrPsc) from another host. This altered PrPsc accumulates in cytoplasmic vesicles of diseased individuals forming lesions, vacuoles and amyloid deposits. PrPsc is a proteolytic-resistant form of PrPc, although no major chemical differences between the two have been found. The major difference between the two is that the infectious form has assumed a different conformational 3-D structure. The PrPc protein is highly conserved across many species, including humans, sheep, mice, hamsters, Drosophila and bovine. The prion protein has received considerable attention in the last few years because it is the same protein that is responsible for bovine spongiform encephalopathy or "Mad Cow disease" and also scrapie in sheep. Prion disease can either occur spontaneously by means of coming in contact with the infectious agent, such as the outbreak in England with the infection of several people who consumed contaminated beef, or it can occur as a rare hereditary form. Currently, there is no cure for prion diseases and death usually occurs within one year of the onset of symptoms, which usually include dementia.
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