Prion related neurodegenerative diseases, called transmissible spongiform encephalopathies, are observed in many animal species. These diseases involve conversion of prion protein (PrPc) into a form that is insoluble and resistant to proteases (PrPSc). The protease resistant form can polymerize into fibrils which accumulate in infected tissues and cause cell death and tissue damage. PrPs have an N-terminal signal sequence and a C-terminal linkage to glycosylphosphatidylinositol anchor. Phosphorylation of PrPC at Ser-43 by Cdk5 promotes proteinase K resistance, prion aggregation, and fibril formation in vitro. In addition, Ser-43 phosphorylation is upregulated in scrapie-infected mouse brain relative to controls.
Human recombinant Prion protein includes the full length protein along with an N-terminal GST fusion protein. This Prion protein was phosphorylated with active Cdk5/p25 in an in vitro kinase assay. The phosphorylated Prion protein is detected by anti-Prion Protein (a.a. 109-112) (Cat.#PM3971) and anti-Prion Protein (Ser-43) (Cat.#PP3951).
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: