ArticleMethods in molecular biology (Clifton, N.J.)2022
Purification of Recombinant Galectins from Different Species Using Distinct Affinity Chromatography Methods.
Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Tools for investigating host-microbe crosstalk using glycan analysis probes inspired by human lectins.Glycobiology · 2025Article
- Whole microbe arrays accurately predict interactions and overall antimicrobial activity of galectin-8 toward distinct strains of Streptococcus pneumoniae.Scientific reports · 2023Article
- Characterization of Galectin Fusion Proteins with Glycoprotein Affinity Columns and Binding Assays.Molecules (Basel, Switzerland) · 2023Article
- Innate immune Galectin-7 specifically targets microbes that decorate themselves in blood group-like antigens.iScience · 2022Article
- An Automated Approach to Assess Relative Galectin-Glycan Affinity Following Glycan Microarray Analysis.Frontiers in molecular biosciences · 2022Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Galectins are lectins having the capacity to recognize β-galactose-containing glycan structures and are widely distributed among various taxa. However, the exact physiological and biochemical functions mediated by galectins that necessitate their wide occurrence among diverse species have not yet been delineated in a precise manner. Purification of recombinant galectins in active form is a fundamental requirement to elucidate their biological function. In this chapter, we are describing methods to recombinantly express and purify galectins using three different methods of affinity purification, i.e., lactosyl-Sepharose chromatography for fungal galectin Coprinopsis cinerea galectin 2 (CGL2), nickel-chromatography for histidine-tagged human galectin-7, and glutathione-Sepharose chromatography for Glutathione S-transferase-tagged (GST-tagged) human galectin-7. Step-by-step instructions are provided for obtaining the above-mentioned recombinant galectins that retain carbohydrate-binding activity and are suitable for conducting biochemical experiments.
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Registered trials
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