Reduced Immune Detection of the Pathogenic Prion Protein in Presenceof Triose Phosphate Isomerase
Copyright: (c) 2016 Moussa A. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. During performing electrophoresis for detecting the presence of recombinant prion protein (PrPrec) it was punctually planned to examine several expressed protein on the same polyacrylamide gel and the last empty well was used for depositing together the molecular weight marker (triose phosphate isomerase) and the pathogenic bovine prion protein PrPsc. After transfer and immune blotting with specific PrP monoclonal antibodies [1] no detectable PrPsc bands were observed. So we decided to explore these unexpected results.