A VL single-domain antibody library shows a high-propensity to yield non-aggregating binders

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1093/protein/gzs014
AuthorSearch for: 1; Search for: ; Search for: 1; Search for: 1; Search for: 1; Search for: 1; Search for: 1; Search for: 1; Search for: 1; Search for: 1
Affiliation
  1. National Research Council of Canada. NRC Institute for Biological Sciences
FormatText, Article
SubjectAntibody library; Complementarity-determining regions; non-aggregating; Phage display libraries; Single domains; Antibodies; Antigens; Scaffolds; Binders; antibody; bacterial antigen; bacterial protein; bacterial toxin; immunoglobulin light chain; single chain fragment variable antibody; toxB protein, Clostridium difficile; antibody library; antigen expression; codon; dissociation; enzyme linked immunosorbent assay; polyacrylamide gel electrophoresis; scanning electron microscopy; solubility; amino acid sequence; antibody affinity; chemistry; genetics; metabolism; molecular cloning; molecular genetics; nucleotide sequence; peptide library; protein binding; Amino Acid Sequence; Antibody Affinity; Antigens, Bacterial; Bacterial Proteins; Bacterial Toxins; Base Sequence; Cloning, Molecular; Enzyme-Linked Immunosorbent Assay; Immunoglobulin Light Chains; Molecular Sequence Data; Peptide Library; Protein Binding; Single-Chain Antibodies
Abstract
Publication date
In
LanguageEnglish
Peer reviewedYes
NPARC number21269535
Export citationExport as RIS
Report a correctionReport a correction (opens in a new tab)
Record identifier3cce1590-8dbb-4117-8281-e32f3e6de1f7
Record created2013-12-12
Record modified2020-04-21
Date modified: