ArticleInternational journal of molecular sciences2017
Utilization of Multi-Immunization and Multiple Selection Strategies for Isolation of Hapten-Specific Antibodies from Recombinant Antibody Phage Display Libraries.
Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Recent Progress in Rapid Determination of Mycotoxins Based on Emerging Biorecognition Molecules: A Review.Toxins · 2022Review
- Recombinant antibodies and their use for food immunoanalysis.Analytical and bioanalytical chemistry · 2022Review
- Application of recombinant antibodies for treatment ofFrontiers in immunology · 2022Review
- Rapid-format recombinant antibody-based methods for the diagnosis ofFrontiers in microbiology · 2022Review
- Recombinant Peptide Mimetic NanoLuc Tracer for Sensitive Immunodetection of Mycophenolic Acid.Analytical chemistry · 2021Article
- Quantitation of Thyroid Hormone Binding to Anti-Thyroxine Antibody Fab Fragment by Native Mass Spectrometry.ACS omega · 2019Article
- Review
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Authors and funding
2 authors.
Funding
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Abstract
Phage display technology provides a powerful tool for the development of novel recombinant antibodies. In this work, we optimized and streamlined the recombinant antibody discovery process for haptens as an example. A multi-immunization approach was used in order to avoid the need for construction of multiple antibody libraries. Selection methods were developed to utilize the full potential of the recombinant antibody library by applying four different elution conditions simultaneously. High-throughput immunoassays were used to analyse the binding properties of the individual antibody clones. Different carrier proteins were used in the immunization, selection, and screening phases to avoid enrichment of the antibodies for the carrier protein epitopes. Novel recombinant antibodies against mycophenolic acid and ochratoxin A, with affinities up to 39 nM and 34 nM, respectively, were isolated from a multi-immunized fragment antigen-binding (Fab) library.
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