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Nucleic Acids Research Advance Access originally published online on February 10, 2009
Nucleic Acids Research 2009 37(5):e41; doi:10.1093/nar/gkp069
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Nucleic Acids Research, 2009, Vol. 37, No. 5 e41
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Methods Online

Selection of complementary single-variable domains for building monoclonal antibodies to native proteins

Tomoyuki Tanaka and Terence H. Rabbitts*

Leeds Institute of Molecular Medicine, University of Leeds, St. James's University Hospital, Leeds LS9 7TF, UK

*To whom correspondence should be addressed. Tel: +44 113 343 8518; Fax: +44 113 343 8601; Email: thr{at}leeds.ac.uk

Received November 30, 2008. Revised January 18, 2009. Accepted January 20, 2009.

Antibodies are now indispensable tools for all areas of cell biology and biotechnology as well as for diagnosis and therapy. Antigen-specific single immunoglobulin variable domains that bind to native antigens can be isolated and manipulated using yeast intracellular antibody capture technology but converting these to whole monoclonal antibody requires that complementary variable domains (VH or VL) bind to the same antigenic site. We describe a simple approach (CatcherAb) for specific isolation of such complementary single domains allowing the constitution of functional Fv, forming the basis of antigen-specific whole immunoglobulin and thus antibody production. We illustrate this approach by developing high-affinity Fv from single variable domains binding to RAS and LMO2 oncogenic proteins.


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