| identifier: | 1755178 |
| description: |
epitope description:E78, T79, K80, A81, Q82, R119, G123, A124, L125, Q126, S127, L128, L129, G130, T131, Q132, L133, P134, P135, R136;
antigen name:Thrombopoietin
host organism:Mus musculus
antibody name:TN1-neutralizing
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
14769915 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/401 |
| landingPage: |
http://www.iedb.org/assay/1755178 |
| type: |
Literature
|
| publicationVenue: |
Proc Natl Acad Sci U S A
|
| dates: |
2004
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Michael D Feese
Taro Tamada
Yoichi Kato
Yoshitake Maeda
Masako Hirose
Yasuko Matsukura
Hideki Shigematsu
Takanori Muto
Atsushi Matsumoto
Hiroshi Watarai
Kinya Ogami
Tomoyuki Tahara
Takashi Kato
Hiroshi Miyazaki
Ryota Kuroki
|
| method: |
calorimetry
|
| name: |
Structure of the receptor-binding domain of human thrombopoietin determined by complexation with a neutralizing antibody fragment.
|
| description: |
The binding of epitope-specific Fab TN1 to fragment hTPO 1-163 occluded the low affinity binding site on the c-Mpl receptor, as measured by isothermal titration calorimetry. The association constant of hTPO 163 and TN1 is about 1 nM, whereas, that of c-Mpl at the low affinity site is about 1 µM, explaining the strong neutralizing activity of TN1.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |