| Title: | Functional intracellular antibody fragments do not require invariant intra-domain disulfide bonds. |
| identifier: | 1833692 |
| description: |
epitope description:S17, Q25, H27, V29, E31, Y32, D33, P34, T35, I36, E37, D38, S39, Y40, Q61, E63, Y64
antigen name:GTPase HRas
host organism:Homo sapiens
antibody name:HRAS-Fv, disulfide-free anti-RAS, VH#6(AV) and VL#204(VA)
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
18187153 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1018819 |
| landingPage: |
http://www.iedb.org/assay/1833692 |
| type: |
Literature
|
| publicationVenue: |
J Mol Biol
|
| dates: |
2008
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Tomoyuki Tanaka
Terence H Rabbitts
|
| method: |
immuno staining
|
| name: |
Functional intracellular antibody fragments do not require invariant intra-domain disulfide bonds.
|
| description: |
Epitope residues were calculated from the structure [PDB: 2VH5] as the antigen residues interacting with the antibody fragment at atomic distance of 4 Å
.
Binding of the epitope specific disulfide-free anti-RAS, VH#6(AV) and VL#204(VA) (designated HRAS-Fv SS-free) to RAS was demonstrated using a luciferase reporter assay in COS-7 cells co-transfected with VH or VL and HRAS(G12V).
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |