Lectin Microarray
Lectin Microarray - 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.
08:29
Expression Profiling with Microarrays
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2023
Microarrays are important tools for profiling gene expression, and are based on complementary binding between probes that are attached to glass chips and nucleic acids derived from samples. Using these arrays, scientists can simultaneously evaluate the expression of thousands of genes. In addition, the expression profiles of different cells or tissue types can be compared, allowing researchers to deduce how the expression of different genes change during biological processes, and thus gain...
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.
13:21
Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
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Cited by 6 •
2012
In this study, we describe an improved protocol for a multiplexed high-throughput antibody microarray with lectin detection method that can be used in glycosylation profiling of specific proteins. This protocol features new reliable reagents and significantly reduces the time, cost, and lab equipment requirements as compared to the previous procedure.
09:13
Profiling Anti-Neu5Gc IgG in Human Sera with a Sialoglycan Microarray Assay
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Cited by 35 •
2017
A sialoglycan microarray assay can be used to evaluate anti-Neu5Gc antibodies in human sera, making it a potential high-throughput diagnostic assay for cancer and other chronic inflammation-mediated human diseases.
FAQs
Interpretation relies on the pattern formed across many lectin spots rather than on a single binding event. Each lectin interacts with carbohydrate structures on glycoproteins, cells, or other samples, so differences in spot responses can reflect changes in monosaccharide composition, terminal residues, or branching. The combined profile therefore provides a biochemical signature of glycosylation.
The lectin set determines which glycan features the assay can reveal. Because different carbohydrate-binding proteins interact with sugars in distinct ways, using multiple immobilized lectins produces a broader binding profile than relying on one lectin. Consequently, the selected panel influences whether comparisons emphasize composition, terminal residues, branching, or other detectable glycan differences.
A lectin microarray offers a rapid, high-throughput profile of glycan-related binding patterns, making it useful for screening and comparison. It does not replace more detailed structural glycan analysis; instead, the two approaches are complementary. Microarray results can indicate differences in glycosylation and help identify samples or proteins that merit deeper structural characterization.
Separate immobilized spots organize many carbohydrate-binding probes within one assay format. When the labeled sample contacts the surface, each spot records interactions associated with its particular lectin, allowing the resulting pattern to be compared across samples. This arrangement supports rapid profiling of glycan features on glycoproteins, cells, or other biological materials.
The workflow begins with immobilizing different lectins as discrete spots on a solid surface. A biological sample, labeled with a fluorescent marker, is then applied so its glycan-containing components can interact with the lectins. Measuring the resulting fluorescence across the spots generates a binding profile that can be compared among samples or biological states.
Researchers can use the approach to compare glycosylation between biological states, characterize proteins, and search for candidate biomarkers. Samples may include glycoproteins, cells, or other biological materials, depending on the experimental question. In biochemistry, the resulting profiles provide a rapid way to examine glycan-related differences before or alongside more detailed structural analysis.