Titlebook: Galectins; Methods and Protocol Sean R. Stowell,Connie M. Arthur,Richard D. Cummin Book 2022Latest edition Springer Science+Business Media,

Demonstrate

Examination of Whole-Cell Galectin Binding by Solid Phase and Flow Cytometric Analysis,rface glycoconjugates. These methods utilize commonly employed flow cytometry techniques and commercially available streptavidin-coated microplates to immobilize various biotinylated ligands, such as glycopeptides, oligosaccharides, and whole cells. Using this approach, fluorescently labeled GBPs, i

Shuttle

Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries,ying β-galactoside-containing glycans. To understand the diversity of functions governed by galectins, it is essential to define the binding specificity of the carbohydrate recognition domain (CRDs) of the individual galectins. The binding specificity of galectins has primarily been examined with gl

lesion

Method for Identifying Galectin Ligands on Lymphocyte Membrane Glycoproteins,an structures, and functional studies have indicated that a family of glycan-binding proteins, galectins, can significantly modulate lymphocyte development and function by interacting with these glycans. Several galectins have a varying degree of affinity for the .acetyllactosamine (LacNAc) disaccha

糾纏,纏繞

,Transformation of , Galectin into αGalNAc-Specific Lectin,cted mutagenesis of the hydrophilic residues His, Asn, Arg, and Glu, involved in carbohydrate recognition, abolished the binding affinity of the derived mutants to β-galactosides, whereas only N46A caused increased affinity to GalNAcα1-3Gal-containing oligosaccharides and loss of β-galactoside-bindi

商議

What Happens If a Human Galectin Enters the Endoplasmic Reticulum?,rresponding engineering of galectin-specific cDNA will answer questions on the fate of a signal peptide-bearing protein variant after its entry into the endoplasmic reticulum (ER). Affinity chromatography and mass-spectrometric analysis of occupancy of potential N-glycosylation sites for the galecti

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perpetual

Exploring the Galectin Network by Light and Fluorescence Microscopy,atus of glycan branching or chain length (e.g., core 1 vs core 2 mucin-type O-glycans and polyLacNAc additions) as well as of sialylation/sulfation has been delineated to convey signals. They are “read” by galectins, for example regulating lattice formation on the membrane and cell growth. Owing to

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怒目而視

Visualization of Cytosolic Galectin Accumulation Around Damaged Vesicles and Organelles,ally exposed glycans and accumulate around endocytic vesicles or organelles damaged by various disruptive substances. Accumulated galectins engage other cytosolic proteins toward damaged vesicles, leading to cellular responses, such as autophagy. Disruptive substances include bacteria, viruses, part

臨時抱佛腳

https://doi.org/10.1007/978-3-662-04240-3enome duplications, over 15 known vertebrate galectins likely evolved from a single common ancestor extant in pre-chordate lineages. While galectins have divergently evolved numerous functions, some of which do not involve carbohydrate recognition, the vast majority of the galectins have retained th