Expression and purification of full-length recombinant PrP of high purity

Abstract

Summary: Certain applications in the prion field require recombinant prion protein (PrP) of high purity and quality. Here, we report an experimental procedure for expression and purification of full-length mammalian prion protein. This protocol has been proved to yield PrP of extremely high purity that lacks PrP adducts, which are normally generated as a result of spontaneous oxidation or degradation. © 2008 Humana Press, a part of Springer Science + Business Media, LLC.