| Title: | Structural and functional characterization of an agonistic anti-human EphA2 monoclonal antibody. |
| identifier: | 1974631 |
| description: |
epitope description:N57, M66, S68, C70, V72, M73, R103, S107, F108, P109, S153, F156, E157, R159, C188, V189, A190
antigen name:Ephrin type-A receptor 2
host organism:Homo sapiens
antibody name:1C1
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
21867711 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1025013 |
| landingPage: |
http://www.iedb.org/assay/1974631 |
| type: |
Literature
|
| publicationVenue: |
J Mol Biol
|
| dates: |
2011
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Li Peng
Vaheh Oganesyan
Melissa M Damschroder
Herren Wu
William F Dall'Acqua
|
| method: |
surface plasmon resonance (SPR)
|
| name: |
Structural and functional characterization of an agonistic anti-human EphA2 monoclonal antibody.
|
| description: |
The epitope residues were calculated from [PDB: 3SKJ] as the antigen residues at 4 Å
atomic distance from the antibody.
The binding affinity of epitope-specific 1C1 IgG for the EphA2 extracellular domain (ECD) was determined by surface plasmon resonance. Fab 1C1 bound with approximately 200-fold lower affinity, KD = 140 nM.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |