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Purification of Recombinant Galectins Expressed in Bacteria

Galectins are soluble lectins that participate in many physiological and pathological functions. Since they can act extracellularly, the use of the recombinant protein is a recurrent strategy for studying their biological functions. Here, we provide a general protocol for the production of Galectins...

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Autores principales: Prato, Cecilia Arahí, Carabelli, Julieta, Cattaneo, Valentina, Campetella, Oscar, Tribulatti, María Virginia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7757657/
https://www.ncbi.nlm.nih.gov/pubmed/33377098
http://dx.doi.org/10.1016/j.xpro.2020.100204
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author Prato, Cecilia Arahí
Carabelli, Julieta
Cattaneo, Valentina
Campetella, Oscar
Tribulatti, María Virginia
author_facet Prato, Cecilia Arahí
Carabelli, Julieta
Cattaneo, Valentina
Campetella, Oscar
Tribulatti, María Virginia
author_sort Prato, Cecilia Arahí
collection PubMed
description Galectins are soluble lectins that participate in many physiological and pathological functions. Since they can act extracellularly, the use of the recombinant protein is a recurrent strategy for studying their biological functions. Here, we provide a general protocol for the production of Galectins and their isolated or chimeric domains. We take advantage of their lectin activity and the 6xHis-tag addition for purification, thus obtaining a highly pure and active Galectin to use in both in vitro and in vivo assays. For complete details on the use and execution of this protocol, please refer to Cattaneo et al. (2011), Tribulatti et al. (2012), and Prato et al. (2020).
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spelling pubmed-77576572020-12-28 Purification of Recombinant Galectins Expressed in Bacteria Prato, Cecilia Arahí Carabelli, Julieta Cattaneo, Valentina Campetella, Oscar Tribulatti, María Virginia STAR Protoc Protocol Galectins are soluble lectins that participate in many physiological and pathological functions. Since they can act extracellularly, the use of the recombinant protein is a recurrent strategy for studying their biological functions. Here, we provide a general protocol for the production of Galectins and their isolated or chimeric domains. We take advantage of their lectin activity and the 6xHis-tag addition for purification, thus obtaining a highly pure and active Galectin to use in both in vitro and in vivo assays. For complete details on the use and execution of this protocol, please refer to Cattaneo et al. (2011), Tribulatti et al. (2012), and Prato et al. (2020). Elsevier 2020-12-09 /pmc/articles/PMC7757657/ /pubmed/33377098 http://dx.doi.org/10.1016/j.xpro.2020.100204 Text en © 2020 The Author(s) http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Protocol
Prato, Cecilia Arahí
Carabelli, Julieta
Cattaneo, Valentina
Campetella, Oscar
Tribulatti, María Virginia
Purification of Recombinant Galectins Expressed in Bacteria
title Purification of Recombinant Galectins Expressed in Bacteria
title_full Purification of Recombinant Galectins Expressed in Bacteria
title_fullStr Purification of Recombinant Galectins Expressed in Bacteria
title_full_unstemmed Purification of Recombinant Galectins Expressed in Bacteria
title_short Purification of Recombinant Galectins Expressed in Bacteria
title_sort purification of recombinant galectins expressed in bacteria
topic Protocol
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7757657/
https://www.ncbi.nlm.nih.gov/pubmed/33377098
http://dx.doi.org/10.1016/j.xpro.2020.100204
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