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Titlebook: Lectin Purification and Analysis; Methods and Protocol Jun Hirabayashi Book 2020 Springer Science+Business Media, LLC, part of Springer Nat

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發(fā)表于 2025-3-21 17:19:50 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Lectin Purification and Analysis
副標(biāo)題Methods and Protocol
編輯Jun Hirabayashi
視頻videohttp://file.papertrans.cn/584/583390/583390.mp4
概述Includes cutting-edge methods and protocols.Provides step-by-step detail essential for reproducible results.Contains key notes and implementation advice from the experts
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Lectin Purification and Analysis; Methods and Protocol Jun Hirabayashi Book 2020 Springer Science+Business Media, LLC, part of Springer Nat
描述.This volume presents a series of experimental protocols for glycan analysis using lectins and the functional analysis of lectins. A key feature in this book are two comprehensive overview chapters on lectin structures and a list of the all the lectins—these chapters discuss the latest findings in the field. The remainder of the book covers topics such as lectins from mammals, non-mammalian animals; plants, algae, fungi, protists, bacteria, and viruses. Written in the highly successful .Methods in Molecular Biology. series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls..Cutting-edge and thorough, .Lectin Purification and Analysis: Methods and Protocols. is a valuable tool for any scientist interested in learning more about these life systems..
出版日期Book 2020
關(guān)鍵詞Galectin; Pentraxin; Botulinum neurotoxin; Knob domain; TgMIC4
版次1
doihttps://doi.org/10.1007/978-1-0716-0430-4
isbn_softcover978-1-0716-0432-8
isbn_ebook978-1-0716-0430-4Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media, LLC, part of Springer Nature 2020
The information of publication is updating

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發(fā)表于 2025-3-21 23:10:34 | 只看該作者
Recombinant Expression and Purification of Animal Intracellular L-Type Lectins,oproteins in the early secretory pathway. These lectins possess the carbohydrate recognition domain (CRD), which recognizes high-mannose-type glycans in a Ca.-dependent manner. Here we describe the procedures involved in bacterial overproduction and purification of the CRDs of the animal L-type lect
板凳
發(fā)表于 2025-3-22 03:24:44 | 只看該作者
Frontal Affinity Chromatography: A Highly Suitable Retardation Phenomenon-Based Research Tool for Ais renders FAC an extremely favorable analytical tool for weak interactions. In this short review, we propose a straightforward explanation of the underlying mechanism. When FAC is performed using analyte solutions at relatively high concentrations, concentration-dependent retardation is observed du
地板
發(fā)表于 2025-3-22 08:37:01 | 只看該作者
,Metazoan Soluble β-Galactoside-Binding Lectins, Galectins: Methods for Purification, Characterizatiticellular organisms and exert various biological functions by binding to the surface glycoconjugates as lectins. In this chapter, we describe the general methods of purification of galectins, quality control of purified galectins, some example methods of evaluating their carbohydrate-binding activi
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Expression and Purification of Full-Length and Domain-Fragment Recombinant Pentraxin 3 (PTX3) Protegregates of the protein of interest are sometimes encountered during the purification procedure. Pentraxin 3 (PTX3), a member of the pentraxin family that is classified as a carbohydrate-binding protein based on its structure, comprises one of the humoral arms of the pattern recognition receptors th
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發(fā)表于 2025-3-22 18:03:20 | 只看該作者
Identification of Siglec Cis-Ligands by Proximity Labeling,l (cis-ligands). Because of the low-affinity binding of Siglecs to the glycan ligands, conventional methods such as immunoprecipitation are not suitable for identification of Siglec cis-ligands. Here we describe efficient and specific labeling of cis-ligands of CD22 (also known as Siglec-2) on B lym
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Selectin-Binding Assay by Flow Cytometry, recruitment to inflammatory sites, lymphocyte homing, and extravasation of cancer cells. The interactions are enhanced at least partly through the upregulation of the selectin-ligand glycan expression, which is observed, for instance, during the activation of leukocytes or epithelial-mesenchymal tr
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