| identifier: | 1694020 |
| description: |
epitope description:E22, H23, E24, T25, R26, L27, V28, A29, K30, L31, F32, K33, D34, W105, V106, D107, Y108, N109, L110, K111, W112, N113, P114, D115, D116, Y117, G118, G119, V120, K121, K122, I123, H124, I125, P126
antigen name:Acetylcholine receptor subunit alpha (UniProt:P02708)
host organism:Rattus norvegicus Lewis
antibody name:35
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
18567851 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1017012 |
| landingPage: |
http://www.iedb.org/assay/1694020 |
| type: |
Literature
|
| publicationVenue: |
Ann N Y Acad Sci
|
| dates: |
2008
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Jon Lindstrom
Jie Luo
Alexander Kuryatov
|
| method: |
immunoprecipitation
|
| name: |
Myasthenia gravis and the tops and bottoms of AChRs: antigenic structure of the MIR and specific immunosuppression of EAMG using AChR cytoplasmic domains.
|
| description: |
The epitope sequence is from the reference cited: Tzartos (1998) Immunol Rev 163: 89-120 [PMID: 9700504].
Conformation-dependent rat mAb 35 immunoprecipitated human alpha1/alpha7chimera containing residues 2-14 and 60-81, demonstrating that these residues form part of the conformational epitope recognized by the mAb. Shortening the length of the alpha1 insert to residues 66-76 reduced the binding of the mAb.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |