Biotinylated Lectin Detection
Biotinylated Lectin Detection - Related Videos
06:15
Biotinylated Cell-Penetrating Peptide Probe to Detect Protein-Protein Interactions
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2025
This video demonstrates a technique that uses biotinylated cell-penetrating peptides to detect intracellular protein-protein interactions. The cell-penetrating peptides facilitate the conjugated peptide to enter a cell and specifically bind to its interacting proteins. The biotin, after binding to avidin, allows purification of the interacting proteins’ complex from a cell lysate.
09:13
Cell-surface Biotinylation Assay
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2023
A cell can regulate the amount of particular proteins on its cell membrane through endocytosis, following which cell surface proteins are effectively sequestered in the cytoplasm. Once within a cell, these surface proteins can be either destroyed or “recycled” back to the membrane. The cell surface biotinylation assay provides researchers with a way to study these phenomena. The technique makes use of a derivative of the small molecule biotin, which can label surface proteins and then be...
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.
11:32
Mapping RNA-RNA Interactions Globally Using Biotinylated Psoralen
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Cited by 20 •
2017
Here, we detail the method of Sequencing of Psoralen crosslinked, Ligated, and Selected Hybrids (SPLASH), which enables genome-wide mapping of intramolecular and intermolecular RNA-RNA interactions in vivo. SPLASH can be applied to study RNA interactomes of organisms including yeast, bacteria and humans.
FAQs
Lectin selectivity determines which glycan features become visible. Each lectin recognizes particular sugar residues, so the observed pattern reflects locations where those residues are present on glycoproteins, glycolipids, or cell surfaces. This molecular preference allows researchers to compare glycan distribution among samples rather than treating all carbohydrate-containing structures as equivalent.
The biotin tag functions as the capture point for signal generation. Avidin or streptavidin binds the attached biotin and carries either an enzyme or fluorescent label, converting lectin binding into a detectable output. This two-part arrangement separates carbohydrate recognition from signal production while preserving the ability to visualize or measure where recognition occurred.
Each lectin reports only the carbohydrate features within its recognition preference. Consequently, a positive signal should be interpreted as evidence of binding to the relevant sugar residues, not as a complete inventory of every glycan in the sample. This distinction matters when comparing samples because differences in signal reflect the lectin-selected glycan patterns being examined.
An assay first exposes the biological sample to the lectin so selective carbohydrate recognition can occur. The biotin attached to that lectin is then captured by avidin or streptavidin coupled to an enzyme or fluorescent label. Researchers finally examine the resulting signal using microscopy, blotting, or tissue analysis, depending on the comparison required.
These formats emphasize different kinds of information. Microscopy and tissue analysis preserve spatial context, making the distribution of lectin binding visible across cells or tissue. Blotting supports analysis of glycoprotein-associated patterns in a sample. Selecting among them depends on whether the biological question centers on location, tissue organization, or comparison of glycosylation patterns.
Biotinylated lectin detection is useful when researchers need to compare glycan patterns between biological states. Applications include studying development, disease, and cellular differentiation, where glycosylation may change. By applying the same recognition-and-labeling logic across samples, investigators can examine whether lectin-binding distributions differ in association with those biological processes.