Prion Protein (PrP) and namely its abnormal isoform, partially resistant to proteinase K (PrPres), is the only specific molecular marker of the Transmissible Spongiform Encephalopathies (TSEs) such as Bovine Spongiform Encephalopathie (BSE) or its huma...More
|Antigen||This anti-prion protein (PrP) monoclonal antibody was raised against proteinase K treated and non-denatured scrapie-associated fibrils from Syrian hamster infected brain (263K).|
Reconstitute the content of the vial in 1 mL of water.
For EIA, the optimal working dilution must be determined empirically (currently be-tween 0.1 and 1 µg/mL). For western blot analysis of PrPc, dilute the antibody to a final concentration of 1 µg/mL.
|Application Media||Reconstitute the content of the vial in 1 mL of water.|
|Formulation||lyophilized IgG with BSA|
Vulin J, Biacabe AG, Cazeau G, Calavas D, and Baron T Molecular typing of protease-resistant prion protein in transmissible spongiform encephalopathies of small ruminants, France, 2002-2009. Emerg Infect Dis, Jan 2011; 17(1): 55-63.
Morel N., Simon S., Frobert Y., Volland H., Mourton-Gilles C., Negro A., Sorgato M.C., Creminon C., and Grassi J. Selective and efficient immunoprecipitation of the disease-associated form of the prion protein can be mediated by nonspecific interactions between monoclonal antibodies and scrapie-associated fibrils.
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Notari S., Capellari S., Langeveld J., Giese A., Strammiello R., Gambetti P., Kretzschmar H.A., and Parchi P. A refined method for molecular typing reveals that co-occurrence of PrP(Sc) types in Creutzfeldt-Jakob disease is not the rule.
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Feraudet C, Morel N, Simon S, Volland H., Frobert Y., Creminon C., Vilette D., Lehmann S., and Grassi J. Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells.
J Biol Chem 2005, 280:11247–11258