Prion proteins

Prion proteins (PrPs) play an important role in a family of neurological disorders called transmissible spongiform encephalopathies (TSEs). These diseases involve aggregation of specific proteins in the brain. In order to study these diseases, researchers need a source of high quality non-aggregated PrPs that will aggregate in the presence of seed aggregates. To fill this need, Impact Biologicals has established itself as a leading commercial source for non-aggregated recombinant PrPs that can be used for studying TSEs.

Impact Biologicals’ PrPs are expressed in E. coli, then purified and refolded. Two forms of purified PrP are available and almost always in stock. These include full-length versions of both hamster and bank vole PrP sequences. Both proteins are highly active in seeded conversion assays.

Hamster PrP (full-length, 23-231)   Bank vole PrP (full-length, 23-230)
Catalog # 201-01
1 x 0.5 mgs – $370
  Catalog # 211-01
1 x 0.5 mgs – $370
Catalog # 201-05
5 x 0.5 mgs – $1,595
  Catalog # 211-05
5 x 0.5 mgs – $1,595
Prices are in US dollars and do not include local taxes or shipping charges. These proteins are for research purposes only. Products may be ordered by phone +1-610-543-6320 or email. Please inquire about volume discounts.

Prion Proteins in RT-QuIC

Impact Biologicals’ prion proteins are widely used as substrates in real-time quaking induced conversion assays (RT-QuIC), the fastest and most sensitive method for detecting infectious prions and for confirming prion disease in animals. Below are links to YouTube videos related to RT-QuIC. [No endorsement relationship is implied between Impact Biologicals and the creators of these videos].

BMG RT-QuIC image

Scientists from BMG and the University of Colorado describe how to establish RT-QuIC methods in your own lab.

Christina OrrĂº (Caughey lab, NIH) discusses ongoing efforts to improve speed and sensitivity of RT-QuIC as a diagnostic test for vCJD, sCJD and other prion diseases.

Other Applications

Impact Biologicals’ prion proteins are also ideal for structural and biochemical studies. Examples include work on fibrillation, including studies on formation of amyloid-like structures and protein-rich deposits related to neurodegeneration. A further application of these proteins is in comparative studies on prionopathies/TSEs such as Bovine Spongiform Encephalopathy (BSE, or “Mad Cow Disease”), Chronic Wasting Disease (CWD), Creutzfeld-Jakob Disease (CJD, vCJD, sCJD), Fatal Familial Insomnia (FFI), and Gerstmann-Sträussler-Scheinker Syndrome (GSS).

References

Please visit our list of open-source journal articles that describe use of recombinant substrate PrP for detection of prionopathies.