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Isolation of isoform-specific binding proteins (Affimers) by phage display using negative selection

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Tang_2017_Isolation_of_isoform_SciSignal_AAM.pdf (619.2Kb)
Date
14/11/2017
Author
Tang, Anna Ah-San
Tiede, Christian
Hughes, David J
McPherson, Michael J
Tomlinson, Darren C
Keywords
QH301 Biology
QD Chemistry
RM Therapeutics. Pharmacology
T-NDAS
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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.
Citation
Tang , A A-S , Tiede , C , Hughes , D J , McPherson , M J & Tomlinson , D C 2017 , ' Isolation of isoform-specific binding proteins (Affimers) by phage display using negative selection ' , Science Signaling , vol. 10 , no. 505 , eaan0868 . https://doi.org/10.1126/scisignal.aan0868
Publication
Science Signaling
Status
Peer reviewed
DOI
https://doi.org/10.1126/scisignal.aan0868
ISSN
1945-0877
Type
Journal article
Rights
Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. This work has been made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at https://doi.org/10.1126/scisignal.aan0868
Description
This work was funded by the University of Leeds.
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  • University of St Andrews Research
URI
http://hdl.handle.net/10023/12214

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