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Several human degenerative diseases resulted from misfolding and aggregation of proteins. The prototype central nervous system protein pathology is CJD, in which neuronal prion protein (PrP) with high α-helical content switches into a stable structure rich in β-pleated sheets in a self-catalyzing process that eventually causes a plethora of neurologic and psychiatric symptoms.
Anti-bovine prion protein mab 3B8 specifically binds to the conformational epitope of bovine prion protein containing sequences GSDYEDRY and YRPVDQ.
Purified, in PBS w/o additives, frozen at -20°C, 12 months shelf life. ELISA, WB, IHC, IF