Tang, AA-S, Tiede, C orcid.org/0000-0003-0280-4005, Hughes, DJ et al. (2 more authors) (2017) Isolation of isoform-specific binding proteins (Affimers) by phage display using negative selection. Science Signaling, 10 (505). eaan0868. ISSN 1945-0877
Abstract
Some 30 years after its discovery, phage display remains one of the most widely used methods of in vitro selection. Initially developed to revolutionize the generation of therapeutic antibodies, phage display is now the first choice for screening artificial binding proteins. Artificial binding proteins can be used as reagents to study protein-protein interactions, target posttranslational modifications, and distinguish between homologous proteins. They can also be used as research and affinity reagents, for diagnostic purposes, and as therapeutics. However, the ability to identify isoform-specific reagents remains highly challenging. We describe an adapted phage display protocol using an artificial binding protein (Affimer) for the selection of isoform-selective binding proteins.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | (c) 2017, The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. This is the author's version of the work. It is posted here by permission of the AAAS for personal use, not for redistribution. The definitive version was published in Science Signaling vol. 10 on 14 November 2017, https://doi.org/10.1126/scisignal.aan0868 |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Synthetic Biology (Leed) |
Depositing User: | Symplectic Publications |
Date Deposited: | 11 Oct 2017 08:56 |
Last Modified: | 15 Jan 2018 19:01 |
Status: | Published |
Publisher: | American Association for the Advancement of Science |
Identification Number: | 10.1126/scisignal.aan0868 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:122205 |