| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1006970 |
| landingPage: |
http://www.iedb.org/assay/2007458 |
| type: |
Literature
|
| publicationVenue: |
Biochemistry
|
| dates: |
1996
|
| study type: | b cell assays |
| subject species: |
| fullName: |
P C Swanson
C Ackroyd
G D Glick
|
| method: |
radio immuno assay (RIA)
|
| name: |
Ligand recognition by anti-DNA autoantibodies. Affinity, specificity, and mode of binding.
|
| description: |
The epitope -specific mAb bound the epitope with the highest affinity, as shown by a gel shift assay. MAbs 15D8, 9F11, 15B10 are IgG2b, 8D8 is IgG2a, and 11F8 is IgG3. For the other mAbs, the KD for 11F8 was 940 nM, for 15D8 was 590 nM, for 15B10 was 230 nM, for 8D8 was 5700 nM. The epitope was the minimal DNA oligomer bound by the mAbs as shown by gel shift assay.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |