Determination of antibody affinity by surface plasmon resonance

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1007/978-3-7091-0870-3_17
AuthorSearch for: 1 ; Search for:
Name affiliation
  1. National Research Council Canada. Human Health Therapeutics
FormatText
TypeBook chapter
Book titleAnticarbohydrate Antibodies: From Molecular Basis to Clinical Application
ISBN9783709108703
3709108691
9783709108697
Pages403–429; # of pages: 27
Abstract
Over the past two decades surface plasmon resonance (SPR) has emerged as gold standard technology for the analysis of biomolecular interactions. In the monoclonal antibody (mAb) development area SPR is employed from the early screening stages to detailed characterization of binding kinetics and affinities to epitope mapping to final product testing. This label free technology provides high quality kinetic and affinity data and, in some instances, other unique information not obtained by alternative methods such as ELISA. SPR is well-suited to the study of protein-carbohydrate interactions which are often of low affinity and not easily characterized by other methods.
Publication date
PublisherSpringer International Publishing
Terms of use
LanguageEnglish
Peer reviewedYes
NPARC number21275592
Export citationExport as RIS
Report a correctionReport a correction
Record identifierf8fc3930-a093-4628-a8b9-5d649471ac64
Record created2015-07-14
Record modified2019-01-31
Date modified:
Report a problem on this page