| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1001856 |
| landingPage: |
http://www.iedb.org/assay/1293914 |
| type: |
Literature
|
| publicationVenue: |
J Virol
|
| dates: |
1998
|
| study type: | b cell assays |
| subject species: | Mus musculus |
| fullName: |
R A Williamson
D Peretz
C Pinilla
H Ball
R B Bastidas
R Rozenshteyn
R A Houghten
S B Prusiner
D R Burton
|
| method: |
ELISA
|
| name: |
Mapping the prion protein using recombinant antibodies.
|
| description: |
The peptide sequence is invariant in hamster, human and bovine PrP.
Reactivity of Fab R72 to the epitope was determined by binding to overlapping 15-mer peptides representing Syrian hamster (SHa) PrP 90-231 or phage displayed protein fragment libraries of mouse PrP. Fab R72 reacts strongly with either mouse or hamster PrP. Binding of R72 to PrP 90-231 is inhibited 50% by 1.9 µM PrP (152-163) or 7.8 µM PrP (154-163), but is not inhibited by ShaPrP 90-231 in solution. Fab R72 reacts with prion rods containing mouse PrP 27-30 after treatment with denaturant and with cryostat sections of scrapie-infected mouse or hamster brains treated with denaturant.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |