Prion Proteins Research Antibody

Anti-prion antibody for use in research applications, clone 1E4:

Sanquin Reagents, in cooperation with the research division of Sanquin, has developed a monoclonal anti-prion antibody for use in research applications: clone 1E4. The antibody is available form Cell Sciences in unconjugated form as well as biotin conjugated or HRP conjugated (see below).

Item M1839: Anti-Prion, clone 1E4, Monoclonal Antibody
Item M1840: Biotinylated Anti-Prion, clone 1E4, Monoclonal Antibody
Item M1841: HRP Conjugated Anti-Prion, clone 1E4, Monoclonal Antibody

Background Information
The term “prion” was introduced by Stanley Prusiner in 1982 to describe the atypical infectious agent that causes transmissible spongiform encephalopathies, a group of infectious neurodegenerative diseases that include scrapie in sheep, Creutzfeldt-Jakob disease in humans, chronic wasting disease (CWD) in deer, and bovine spongiform encephalopathy (BSE) in cattle.

The ‘mad cow’ crisis has drawn a lot of attention to prion diseases. Significant progress has been made in prion disease research, and many aspects of prion pathogenesis are now understood. And yet the diagnostic procedures available for prion diseases are not nearly as sensitive as they ought to be, i.e. a diagnostic test to proof the presence of pathogenic prion in blood or serum.

Special Features of 1E4
In contrast to many other anti-prion antibodies, mAb 1E4 has a broad species reactivity. This enables the detection of prion proteins in biological samples of many species including mouse adapted BSE (301V)-infected mice, scrapie-infected sheep, scrapie infected hamster (263K), CWD infected deer, sCJD- and vCJD-infected human on Western blots.

Most of the currently available TSE tests are based on the fact that PrPC, normal prion protein, is digested by Protease K, whereas PrPSc, TSE specific prion, is relatively resistant to degradation by proteases. The special feature of mAb 1E4 is where the PrPSc epitope binds, PrP27-30, which is mostly hidden on non-digested prion proteins. After Proteinase K digestion the epitope becomes better available on proteinase resistant PrPSc, resulting in a significant signal increase. After digestion with Protease K , mAb 1E4 binds to PrPSc with a high affinity, whereas it has a low affinity for non-digested PrPSc. This makes mAb 1E4 a highly interesting antibody in current prion disease research.

Applications
1E4 has been tested in a broad variety of methods, such as Western blot, RIA, ELISA, EliBlot, FACS and immunohistochemistry. 1E4 allows prion research in many immunological techniques across a broad range of species.

REFERENCE:
Prusiner, S.B., Prions, Proc. Natl. Acad. Sci., Vol.95, pp 13363 - 13383, 1998.