Affimer proteins are versatile and renewable affinity reagents

Christian Tiede(University of Leeds), R. Bedford(University of Leeds), Sophie J. Heseltine(University of Leeds), Gina A. Smith(University of Leeds), Imeshi Wijetunga(University of Leeds), Rebecca L. Ross(University of Leeds), Danah AlQallaf(University of Leeds), Ashley P. E. Roberts(The Pirbright Institute), Alexander Balls(University of Leeds), Alistair Curd(University of Leeds), Ruth Hughes(University of Leeds), Heather L. Martin(University of Leeds), Sarah R. Needham(Rutherford Appleton Laboratory), Laura C. Zanetti-Domingues(Rutherford Appleton Laboratory), Yashar Sadigh(The Pirbright Institute), Thomas P. Peacock(The Pirbright Institute), Anna A. Tang(University of Leeds), Naomi Gibson(University of Leeds), Hannah F. Kyle(Avacta (United Kingdom)), Geoffrey W. Platt(Avacta (United Kingdom)), Nicola Ingram(University of Leeds), Thomas J. Taylor(University of Leeds), Louise Coletta(University of Leeds), Iain W. Manfield(University of Leeds), Margaret A. Knowles(University of Leeds), Sandra Bell(University of Leeds), Filomena Esteves(University of Leeds), Azhar Maqbool(University of Leeds), Rajendra Prasad(University of Leeds), Mark J. Drinkhill(University of Leeds), Robin S. Bon(University of Leeds), Vikesh Patel(Defence Science and Technology Laboratory), Sarah A. Goodchild(Defence Science and Technology Laboratory), Marisa L. Martin-Fernandez(Rutherford Appleton Laboratory), Raymond J. Owens(Rutherford Appleton Laboratory), Joanne E. Nettleship(Rutherford Appleton Laboratory), Michael E. Webb(University of Leeds), Michael A. Harrison(University of Leeds), Jonathan D. Lippiat(University of Leeds), Sreenivasan Ponnambalam(University of Leeds), Michelle Peckham(University of Leeds), Alastair Smith(Avacta (United Kingdom)), Paul Ko Ferrigno(Avacta (United Kingdom)), Matt Johnson(Avacta (United Kingdom)), Michael J. McPherson(University of Leeds), Darren C. Tomlinson(University of Leeds)
eLife
June 8, 2017
Cited by 208Open Access
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Abstract

Molecular recognition reagents are key tools for understanding biological processes and are used universally by scientists to study protein expression, localisation and interactions. Antibodies remain the most widely used of such reagents and many show excellent performance, although some are poorly characterised or have stability or batch variability issues, supporting the use of alternative binding proteins as complementary reagents for many applications. Here we report on the use of Affimer proteins as research reagents. We selected 12 diverse molecular targets for Affimer selection to exemplify their use in common molecular and cellular applications including the (a) selection against various target molecules; (b) modulation of protein function in vitro and in vivo; (c) labelling of tumour antigens in mouse models; and (d) use in affinity fluorescence and super-resolution microscopy. This work shows that Affimer proteins, as is the case for other alternative binding scaffolds, represent complementary affinity reagents to antibodies for various molecular and cell biology applications.


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