Abstract
An abnormal isoform of prion protein (PrPSc) was extracted from formalin-fixed paraffin-embedded (FFPE) tissues from sheep and analyzed by western blotting. PrPSc immunoreactivity against anti-PrP monoclonal antibody T2, which recognizes discontinuous PrP sequences, differed amongst individual scrapie sheep cases. This may reflect structural differences in PrPSc that have been formalin-fixed prior to their extraction. This study indicates that western blotting by using FFPE tissues is useful for the retrospective analysis of transmissible spongiform encephalopathies in which only formalin-fixed samples are available and in conducting transmissible spongiform encephalopathies surveillance where freezing system is insufficient. ©2012 The Japanese Society of Veterinary Science.
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CITATION STYLE
Dorj, G., Okada, H., Miyazawa, K., Masujin, K., Kimura, K., Mohri, S., & Yokoyama, T. (2012, September). Retrospective analysis of sheep scrapie by western blotting with formalin-fixed paraffin-embedded (FFPE) Tissues. Journal of Veterinary Medical Science. https://doi.org/10.1292/jvms.12-0037
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