Protocol for Monoclonal Antibody Epitope Mapping
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Epitopes consist of groups of amino acids that lie close together on the protein (antigen) surface and interact with an antibody; they therefore determine antigenicity. Epitopes of proteins are usually classified as either linear (continuous) or conformational (discontinuous). Conformational epitopes are thought to form the majority of epitopes on most proteins. However, many conformational epitopes may also be recognizable as linear epitopes.
A multitude of disciplines require detailed knowledge about epitopes. Not only immunologists who have an a priori interest depend on epitope mapping protocols, but also biologists using antibodies as research tools, structural biologists studying protein–protein interactions, clinicians investigating patients' immune responses, vaccine developers designing and testing immunogens, diagnostic labs developing and applying ELISAs, and last but not the least, biotech and pharmaceutical companies obliged to monitor the immunogenicity of novel therapeutic antibodies, proteins, and peptides, to mention only a few.
Staffed by dedicated scientists with combined expertise in antibody engineering and protein X-ray crystallography, Creative BioStructure has established an antibody epitope mapping platform this is based on protein crystallography. We have extensive experience in crystallizing antibody/antigen complexes and resolving their 3D structures. In particular, we are able to map the epitopes of a large variety of antibody forms, including intact IgG, Fab, scFv, F(ab')2, diabody, minibody, miniantibody, tandem scFv and nanobody as well as affibody. X-ray crystallography of antigen/antibody complexes allows mapping both conformational and linear epitopes.
We rely on our phage display based Bio-fishing Platform to offer linear epitope mapping service. Of note, we have two random phage display peptide libraries that were constructed in house using Trimer Codon technology.
In addition, linear epitope mapping can also be performed using NEB Ph.D.TM-7 and Ph.D.TM-12 Phage Display Peptide Libraries.
Compared with the commonly employed linear epitope mapping strategy of overlapping peptide arrays [chemically synthesized combinatorial peptide libraries], our phage display peptide libraries have a much greater diversity of the peptides and provide a method in which signals from individual peptides can be amplified for multiple rounds, thus significantly enhance the possibility of isolating the peptide of the perfect match.
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Protocol for: Monoclonal Antibody Epitope Mapping Abstract or Description:
Epitopes consist of groups of amino acids that lie close together on the protein (antigen) surface and interact with an antibody; they therefore determine antigenicity. Epitopes of proteins are usually classified as either linear (continuous) or conformational (discontinuous). Conformational epitopes are thought to form the majority of epitopes on most proteins. However, many conformational epitopes may also be recognizable as linear epitopes.
A multitude of disciplines require detailed knowledge about epitopes. Not only immunologists who have an a priori interest depend on epitope mapping protocols, but also biologists using antibodies as research tools, structural biologists studying protein–protein interactions, clinicians investigating patients' immune responses, vaccine developers designing and testing immunogens, diagnostic labs developing and applying ELISAs, and last but not the least, biotech and pharmaceutical companies obliged to monitor the immunogenicity of novel therapeutic antibodies, proteins, and peptides, to mention only a few.
Staffed by dedicated scientists with combined expertise in antibody engineering and protein X-ray crystallography, Creative BioStructure has established an antibody epitope mapping platform this is based on protein crystallography. We have extensive experience in crystallizing antibody/antigen complexes and resolving their 3D structures. In particular, we are able to map the epitopes of a large variety of antibody forms, including intact IgG, Fab, scFv, F(ab')2, diabody, minibody, miniantibody, tandem scFv and nanobody as well as affibody. X-ray crystallography of antigen/antibody complexes allows mapping both conformational and linear epitopes.
We rely on our phage display based Bio-fishing Platform to offer linear epitope mapping service. Of note, we have two random phage display peptide libraries that were constructed in house using Trimer Codon technology.
In addition, linear epitope mapping can also be performed using NEB Ph.D.TM-7 and Ph.D.TM-12 Phage Display Peptide Libraries.
Compared with the commonly employed linear epitope mapping strategy of overlapping peptide arrays [chemically synthesized combinatorial peptide libraries], our phage display peptide libraries have a much greater diversity of the peptides and provide a method in which signals from individual peptides can be amplified for multiple rounds, thus significantly enhance the possibility of isolating the peptide of the perfect match.
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