Epitope tagging: a monoclonal antibody specific for recombinant fusion proteins in plants

The easy identification of a recombinant protein in plant material becomes increasingly relevant as more transgenic plants are used for research and commercial applications. Tagging recombinant proteins with a small peptide (epitope) can perform such a task. However, available epitope antibodies wil...

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Main Authors: Susan D. Lawrence, Nicole G. Novak, Jeffrey M. Slack
Format: Article
Language:English
Published: Taylor & Francis Group 2003-09-01
Series:BioTechniques
Online Access:https://www.future-science.com/doi/10.2144/03353st01
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author Susan D. Lawrence
Nicole G. Novak
Jeffrey M. Slack
author_facet Susan D. Lawrence
Nicole G. Novak
Jeffrey M. Slack
author_sort Susan D. Lawrence
collection DOAJ
description The easy identification of a recombinant protein in plant material becomes increasingly relevant as more transgenic plants are used for research and commercial applications. Tagging recombinant proteins with a small peptide (epitope) can perform such a task. However, available epitope antibodies will also cross-react with endogenous plant proteins at a level that may be unacceptable. Here we describe the new epitope antibody AcV5. Whether it is attached to the carboxyl terminal end of enhanced green fluorescent protein (EGFP) or the Bacillus thuringiensis endotoxin Cry3A, these proteins remain functional. In addition, using less than 250 pg AcV5-tagged EGFP produces a strong signal on Western blots with no cross-reactivity of proteins from a broad range of plants of agronomic importance.
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1940-9818
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publishDate 2003-09-01
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series BioTechniques
spelling doaj-art-ecf27e656a5242ad841e033bfc0106802025-08-20T02:26:06ZengTaylor & Francis GroupBioTechniques0736-62051940-98182003-09-0135348849210.2144/03353st01Epitope tagging: a monoclonal antibody specific for recombinant fusion proteins in plantsSusan D. Lawrence0Nicole G. Novak1Jeffrey M. Slack21United States Department of Agriculture, Beltsville, MD, USA1United States Department of Agriculture, Beltsville, MD, USA1United States Department of Agriculture, Beltsville, MD, USAThe easy identification of a recombinant protein in plant material becomes increasingly relevant as more transgenic plants are used for research and commercial applications. Tagging recombinant proteins with a small peptide (epitope) can perform such a task. However, available epitope antibodies will also cross-react with endogenous plant proteins at a level that may be unacceptable. Here we describe the new epitope antibody AcV5. Whether it is attached to the carboxyl terminal end of enhanced green fluorescent protein (EGFP) or the Bacillus thuringiensis endotoxin Cry3A, these proteins remain functional. In addition, using less than 250 pg AcV5-tagged EGFP produces a strong signal on Western blots with no cross-reactivity of proteins from a broad range of plants of agronomic importance.https://www.future-science.com/doi/10.2144/03353st01
spellingShingle Susan D. Lawrence
Nicole G. Novak
Jeffrey M. Slack
Epitope tagging: a monoclonal antibody specific for recombinant fusion proteins in plants
BioTechniques
title Epitope tagging: a monoclonal antibody specific for recombinant fusion proteins in plants
title_full Epitope tagging: a monoclonal antibody specific for recombinant fusion proteins in plants
title_fullStr Epitope tagging: a monoclonal antibody specific for recombinant fusion proteins in plants
title_full_unstemmed Epitope tagging: a monoclonal antibody specific for recombinant fusion proteins in plants
title_short Epitope tagging: a monoclonal antibody specific for recombinant fusion proteins in plants
title_sort epitope tagging a monoclonal antibody specific for recombinant fusion proteins in plants
url https://www.future-science.com/doi/10.2144/03353st01
work_keys_str_mv AT susandlawrence epitopetaggingamonoclonalantibodyspecificforrecombinantfusionproteinsinplants
AT nicolegnovak epitopetaggingamonoclonalantibodyspecificforrecombinantfusionproteinsinplants
AT jeffreymslack epitopetaggingamonoclonalantibodyspecificforrecombinantfusionproteinsinplants