WB
|
---|
mAb
|
Peptide ELISA
|
PrP
c
|
recPrP
c
|
if
|
RIPA
|
---|
14D3 | p4 | +/− | +/− |
+ +
| nd |
4F2 | P5 |
+ + +
|
+ + +
|
+ + +
|
+ +
|
13F10 | P5 |
+ +
|
+ +
|
+ + +
| nd |
8G8 | P7 |
+
|
+
|
+
a
|
+ +
|
11B9 | p10 |
+ +
|
+
|
+ +
| nd |
12F10 | p10 |
+ +
|
+
|
+ +
| nd |
7B4 | − | − | − |
+
|
+ +
|
11C6 | − | − | − |
+ +
| nd |
12E8 | − | − | − |
+ +
| nd |
- The binding specificity of some of the mAbs described in this paper are summarized. The entire cellular human prion protein or parts thereof were used as a target for antibody binding. Overlapping peptides were taken to characterize the epitopes relevant for mAb recognition in a peptide ELISA. mAbs were directed against peptides 4, 5, 7, and 10 (p4, p5, p7, and p10). Western blots (WB) were performed using PrPc from human brain tissue (PrPc) or recombinant human prion protein from overexpressing BHK cells (recPrPc). These prion protein-expressing cells also served as a target for immunofluorescence assays (IF) or as source of metabolically labeled prion protein for radioimmunoprecipitation (RIPA), nd, not done.
- amAb 8G8 showed a distinct binding pattern by exclusively staining a subset of prion protein expressing cells, as described in Results.