Gal Galnac Lectin
Gal Galnac Lectin - Related Videos
09:25
Lectin-based Isolation and Culture of Mouse Embryonic Motoneurons
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Cited by 21 •
2011
An alternative way of isolating mouse embryonic motoneurons from the spinal cord is described. The method takes into account the fact that lectin can bind to the low affinity nerve growth factor receptor p75NTR. This lectin-based preplating allows a purification similar to that with a specific antibody against the p75NTR.
20:23
A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
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Cited by 13 •
2009
Lectin-conjugated POROS beads were employed for HPLC. Glycopeptide standards served as positive and negative controls. MARS-14 depleted, trypsin-digested human plasma was chromatographed and flow-through (FT) and bound fractions collected for ESI-LC-MS/MS analyses. Glycopeptides were enriched in the bound fraction as compared to FT.
08:11
Measuring Influenza Neuraminidase Inhibition Antibody Titers by Enzyme-linked Lectin Assay
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Cited by 54 •
2016
We describe the enzyme-linked lectin assay (ELLA) for measuring influenza neuraminidase (NA)-inhibition antibody titers in sera. The assay uses peanut agglutinin to quantify galactose residues that become accessible when NA removes sialic acid from fetuin-coated, 96-well plates.
10:25
In Utero Intra-cardiac Tomato-lectin Injections on Mouse Embryos to Gauge Renal Blood Flow
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Cited by 2 •
2015
This manuscript describes a technique for visualization of the developing vasculature. Here we utilized in utero intra-cardiac FITC-labeled tomato lectin microinjections on mouse embryos. Using this technique, we delineate the perfused and unperfused vessels throughout the embryonic kidney.
08:47
Improved Visualization of Lung Metastases at Single Cell Resolution in Mice by Combined In-situ Perfusion of Lung Tissue and X-Gal Staining of lacZ-Tagged Tumor Cells
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Cited by 12 •
2012
The novel protocol reported in the present study allows selective detection of lung metastases at single cell resolution in mice by combined in-situ lung perfusion and fixation and X-Gal staining of lacZ-tagged tumor cells.
FAQs
Specificity arises from the fit between a carbohydrate-recognition domain and the spatial arrangement of sugars on a glycoconjugate. Galactose and GalNAc residues are contacted through noncovalent forces, particularly hydrogen bonding and hydrophobic contacts. Because recognition depends on residue arrangement, binding can provide information about glycan organization rather than indicating only the presence of an individual sugar.
Carbohydrate-recognition domains provide the contact surfaces that position galactose- or GalNAc-containing structures for selective binding. Their interactions are noncovalent, so recognition depends on the combined contribution of hydrogen bonds and hydrophobic contacts rather than a permanent chemical linkage. This molecular matching makes the lectin useful for examining glycan patterns in biological samples.
When multiple binding events connect neighboring glycoproteins or cells, the lectin can promote cross-linking or adhesion. The outcome depends on how recognizable sugar arrangements are presented across those surfaces, not merely on the presence of galactose or GalNAc in isolation. This links molecular recognition with larger biological effects involving cell association and glycoconjugate organization.
Mucin-associated carbohydrates are a useful application because mucins contain carbohydrate-rich structures whose galactose and GalNAc features can be examined through lectin recognition. Studying these interactions helps characterize sugar patterns on mucin-associated glycoconjugates, connecting molecular binding measurements with questions about cell-surface composition, molecular recognition, and biological communication.
To analyze glycan expression, researchers examine where and how the lectin recognizes glycoconjugates or cell surfaces. The resulting binding pattern provides information about the distribution of galactose- and GalNAc-containing structures, allowing comparisons among biological samples. This makes the lectin a molecular probe for studying cell-surface sugars without treating all glycans as equivalent.
Cell-cell and host-pathogen studies use the same recognition principle to ask whether complementary glycans participate in attachment or interaction. Lectin binding can connect sugar structures on one cell or organism with glycoconjugates on another, while its cross-linking capacity can make these associations apparent. The approach therefore relates glycan composition to biological contact and communication.
Selective recognition of galactose- and GalNAc-containing glycoconjugates makes the lectin a candidate tool for carbohydrate-targeted diagnostics. In that context, binding patterns could help identify or compare glycan features associated with biological samples. Its value comes from molecular specificity, while interpretation depends on relating the observed recognition to the relevant cell or glycoconjugate context.