Purification of Recombinant Galectins Expressed in Bacteria.

STAR Protoc

Laboratorio de Inmunología Molecular, Instituto de Investigaciones Biotecnológicas, Universidad Nacional de San Martín (UNSAM), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), San Martín, Buenos Aires B1650HMP, Argentina.

Published: December 2020

AI Article Synopsis

  • * Researchers often use recombinant Galectins to study their functions in the lab, which involves creating these proteins using specific methods.
  • * The provided protocol details how to produce and purify Galectins with added tags for easier extraction, ensuring they are of high quality for experimental use, referencing work from other studies for more information.

Article Abstract

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 and 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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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7757657PMC
http://dx.doi.org/10.1016/j.xpro.2020.100204DOI Listing

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