Prion protein PrP is a membrane glycosylphosphatidylinositol(GPI) anchored glycoprotein highly expressed in neuron and glia cells as well as immune and reproductive cells. Mutations in the octapeptide repeat regions as well as elsewhere in this gene have been associated with neurodegenerative diseases such as Creutzfeldt Jakob disease, fatal familial insomnia, Gerstmann Straussler disease, Huntington disease like 1, and kuru. The infectious isoform of PrPC, known as PrPSc, is able to convert normal PrPC proteins into the infectious isoform,which is insoluble amyloid aggregate, by changing their conformation (1)
Both PrP is encoded as a protein of ~ 250 amino acids and the mature protein consists of 209 amino acids. Several topological forms exist; one cell surface form anchored via glycolipid and two transmembrane forms, which is responsible for the formation multiple bands in SDS-PAGE.
1) Western blotting (~0.5 μg/ml)
2) ELISA (most suitable)
|Clone : 2C5-5
Clone : 7A1
1) Figure Identification of Prion protein in crude cell extract by western blotting with monoclonal antibody 2C5-5 or 7A1 Lane1. Extract of rabbit kidney cells RK13,overexpressing prion protein. Lane 2. Negative control; extract of the vector infected cells. Lane 3. Negative control; extract of RK13 cells.
1. Sakudo A, et al. J Vet. Med. Sci. 69, 329-337 (2007) Review
2. Inoue Y, et al. Jpn. J. Infect. Dis. 58, 78-82 (2005)
3. Grathwohl KU, et al. J Virol. Methods 64, 205-216 (1997)
To be used for research only. DO NOT use for human gene therapy or clinical diagnosis.