Development of RAP Tag, a Novel Tagging System for Protein Detection and Purification

Affinity tag systems, possessing high affinity and specificity, are useful for protein detection and purification. The most suitable tag for a particular purpose should be selected from many available affinity tag systems. In this study, we developed a novel affinity tag called the “RAP tag” system,...

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Autores principales: Fujii, Yuki, Kaneko, Mika K., Ogasawara, Satoshi, Yamada, Shinji, Yanaka, Miyuki, Nakamura, Takuro, Saidoh, Noriko, Yoshida, Kanae, Honma, Ryusuke, Kato, Yukinari
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Mary Ann Liebert, Inc. 2017
Materias:
Short Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5404252/
https://www.ncbi.nlm.nih.gov/pubmed/28339303
http://dx.doi.org/10.1089/mab.2016.0052
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author Fujii, Yuki
Kaneko, Mika K.
Ogasawara, Satoshi
Yamada, Shinji
Yanaka, Miyuki
Nakamura, Takuro
Saidoh, Noriko
Yoshida, Kanae
Honma, Ryusuke
Kato, Yukinari
author_facet Fujii, Yuki
Kaneko, Mika K.
Ogasawara, Satoshi
Yamada, Shinji
Yanaka, Miyuki
Nakamura, Takuro
Saidoh, Noriko
Yoshida, Kanae
Honma, Ryusuke
Kato, Yukinari
author_sort Fujii, Yuki
collection PubMed
description Affinity tag systems, possessing high affinity and specificity, are useful for protein detection and purification. The most suitable tag for a particular purpose should be selected from many available affinity tag systems. In this study, we developed a novel affinity tag called the “RAP tag” system, which comprises a mouse antirat podoplanin monoclonal antibody (clone PMab-2) and the RAP tag (DMVNPGLEDRIE). This system is useful not only for protein detection in Western blotting, flow cytometry, and sandwich enzyme-linked immunosorbent assay, but also for protein purification.
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spelling pubmed-54042522017-05-02 Development of RAP Tag, a Novel Tagging System for Protein Detection and Purification Fujii, Yuki Kaneko, Mika K. Ogasawara, Satoshi Yamada, Shinji Yanaka, Miyuki Nakamura, Takuro Saidoh, Noriko Yoshida, Kanae Honma, Ryusuke Kato, Yukinari Monoclon Antib Immunodiagn Immunother Short Communications Affinity tag systems, possessing high affinity and specificity, are useful for protein detection and purification. The most suitable tag for a particular purpose should be selected from many available affinity tag systems. In this study, we developed a novel affinity tag called the “RAP tag” system, which comprises a mouse antirat podoplanin monoclonal antibody (clone PMab-2) and the RAP tag (DMVNPGLEDRIE). This system is useful not only for protein detection in Western blotting, flow cytometry, and sandwich enzyme-linked immunosorbent assay, but also for protein purification. Mary Ann Liebert, Inc. 2017-04-01 2017-04-01 /pmc/articles/PMC5404252/ /pubmed/28339303 http://dx.doi.org/10.1089/mab.2016.0052 Text en © Yuki Fujii et al., 2017; Published by Mary Ann Liebert, Inc. This Open Access article is distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited.
spellingShingle Short Communications
Fujii, Yuki
Kaneko, Mika K.
Ogasawara, Satoshi
Yamada, Shinji
Yanaka, Miyuki
Nakamura, Takuro
Saidoh, Noriko
Yoshida, Kanae
Honma, Ryusuke
Kato, Yukinari
Development of RAP Tag, a Novel Tagging System for Protein Detection and Purification
title Development of RAP Tag, a Novel Tagging System for Protein Detection and Purification
title_full Development of RAP Tag, a Novel Tagging System for Protein Detection and Purification
title_fullStr Development of RAP Tag, a Novel Tagging System for Protein Detection and Purification
title_full_unstemmed Development of RAP Tag, a Novel Tagging System for Protein Detection and Purification
title_short Development of RAP Tag, a Novel Tagging System for Protein Detection and Purification
title_sort development of rap tag, a novel tagging system for protein detection and purification
topic Short Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5404252/
https://www.ncbi.nlm.nih.gov/pubmed/28339303
http://dx.doi.org/10.1089/mab.2016.0052
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