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Three Recombinant Engineered Antibodies against Recombinant Tags with High Affinity and Specificity

We describe three recombinant engineered antibodies against three recombinant epitope tags, constructed with divalent binding arms to recognize divalent epitopes and so achieve high affinity and specificity. In two versions, an epitope is inserted in tandem into a protein of interest, and a homodime...

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Detalles Bibliográficos
Autores principales: Zhao, Hongyu, Shen, Ao, Xiang, Yang K., Corey, David P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4778845/
https://www.ncbi.nlm.nih.gov/pubmed/26943906
http://dx.doi.org/10.1371/journal.pone.0150125
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author Zhao, Hongyu
Shen, Ao
Xiang, Yang K.
Corey, David P.
author_facet Zhao, Hongyu
Shen, Ao
Xiang, Yang K.
Corey, David P.
author_sort Zhao, Hongyu
collection PubMed
description We describe three recombinant engineered antibodies against three recombinant epitope tags, constructed with divalent binding arms to recognize divalent epitopes and so achieve high affinity and specificity. In two versions, an epitope is inserted in tandem into a protein of interest, and a homodimeric antibody is constructed by fusing a high-affinity epitope-binding domain to a human or mouse Fc domain. In a third, a heterodimeric antibody is constructed by fusing two different epitope-binding domains which target two different binding sites in GFP, to polarized Fc fragments. These antibody/epitope pairs have affinities in the low picomolar range and are useful tools for many antibody-based applications.
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spelling pubmed-47788452016-03-23 Three Recombinant Engineered Antibodies against Recombinant Tags with High Affinity and Specificity Zhao, Hongyu Shen, Ao Xiang, Yang K. Corey, David P. PLoS One Research Article We describe three recombinant engineered antibodies against three recombinant epitope tags, constructed with divalent binding arms to recognize divalent epitopes and so achieve high affinity and specificity. In two versions, an epitope is inserted in tandem into a protein of interest, and a homodimeric antibody is constructed by fusing a high-affinity epitope-binding domain to a human or mouse Fc domain. In a third, a heterodimeric antibody is constructed by fusing two different epitope-binding domains which target two different binding sites in GFP, to polarized Fc fragments. These antibody/epitope pairs have affinities in the low picomolar range and are useful tools for many antibody-based applications. Public Library of Science 2016-03-04 /pmc/articles/PMC4778845/ /pubmed/26943906 http://dx.doi.org/10.1371/journal.pone.0150125 Text en © 2016 Zhao et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Zhao, Hongyu
Shen, Ao
Xiang, Yang K.
Corey, David P.
Three Recombinant Engineered Antibodies against Recombinant Tags with High Affinity and Specificity
title Three Recombinant Engineered Antibodies against Recombinant Tags with High Affinity and Specificity
title_full Three Recombinant Engineered Antibodies against Recombinant Tags with High Affinity and Specificity
title_fullStr Three Recombinant Engineered Antibodies against Recombinant Tags with High Affinity and Specificity
title_full_unstemmed Three Recombinant Engineered Antibodies against Recombinant Tags with High Affinity and Specificity
title_short Three Recombinant Engineered Antibodies against Recombinant Tags with High Affinity and Specificity
title_sort three recombinant engineered antibodies against recombinant tags with high affinity and specificity
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4778845/
https://www.ncbi.nlm.nih.gov/pubmed/26943906
http://dx.doi.org/10.1371/journal.pone.0150125
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