| Title: | The role of CDR H3 in antibody recognition of a synthetic analog of a lipopolysaccharide antigen. |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1017762 |
| landingPage: |
http://www.iedb.org/assay/1786790 |
| type: |
Literature
|
| publicationVenue: |
Glycobiology
|
| dates: |
2010
|
| study type: | b cell assays |
| subject species: | Bacteria |
| fullName: |
Cory L Brooks
Ryan J Blackler
Georg Sixta
Paul Kosma
Sven Mü
ller-Loennies
Lore Brade
Tomoko Hirama
C Roger MacKenzie
Helmut Brade
Stephen V Evans
|
| method: |
surface plasmon resonance (SPR)
|
| name: |
The role of CDR H3 in antibody recognition of a synthetic analog of a lipopolysaccharide antigen.
|
| description: |
The solution affinity was determined by surface plasmon resonance from the inhibition of S67-27 Fab binding to immobilized Kdo(2->8) Kdo(2->4)Kdo-BSA. Fab S67-27 also bound to the epitope-BSA conjugate by ELISA.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |