Sna Lectin
Sna 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.
09:31
Visualization of Gut Microbiota-host Interactions via Fluorescence In Situ Hybridization, Lectin Staining, and Imaging
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Cited by 10 •
2021
This streamlined protocol details a workflow to detect and image bacteria in complex tissue samples, from fixing the tissue to staining microbes with fluorescent in situ hybridization.
FAQs
Binding depends primarily on the presence of terminal sialic acid residues attached to galactose through an α2,6 linkage. This structural preference allows SNA lectin to distinguish particular glycan arrangements rather than recognizing carbohydrates indiscriminately. Consequently, observed binding can provide evidence that this specific terminal motif occurs on a cell, tissue, or biomolecule.
The α2,6 linkage defines an important part of the carbohydrate pattern recognized by SNA lectin. Therefore, SNA-based detection should be interpreted as information about glycans containing this linkage, not as a general measurement of all sialic acid residues or total glycosylation. This distinction helps researchers make more precise comparisons among biological samples.
Applying the same SNA lectin-based analysis to different cells, tissues, or biomolecules allows researchers to compare the occurrence of its preferred glycan structure across samples. Differences in fluorescent staining, affinity-based detection, or lectin-profiling results can reveal altered glycosylation patterns. Such comparisons are useful when samples represent different biological states or conditions.
SNA lectin provides a way to examine how a defined cell-surface carbohydrate pattern varies in biological systems. Because glycosylation can influence cellular recognition and biological function, detecting changes in SNA-reactive structures helps connect carbohydrate composition with processes such as differentiation, infection, or disease-associated cellular changes.
In fluorescent staining, SNA lectin is applied as the carbohydrate-recognition reagent, and its binding is detected through fluorescence. The resulting staining pattern indicates where the preferred α2,6-linked sialic acid structures occur within the analyzed sample. This format supports visualization and comparison of glycan distribution across cells or tissue regions.
Affinity assays are useful when researchers want to evaluate interactions between SNA lectin and glycan-bearing biomolecules or biological samples. Because the assay focuses on preferential binding to a defined carbohydrate structure, it can support comparisons of glycan expression among samples. The approach complements imaging by emphasizing lectin-binding relationships rather than tissue localization.
Lectin-based profiling can compare SNA-reactive glycan patterns among samples associated with cancer or infection. Researchers may use these comparisons to identify changes in glycosylation linked to the biological state under investigation. The results do not by themselves explain the cause of a change, but they help characterize carbohydrate differences relevant to disease biology.
During differentiation studies, researchers can compare SNA-reactive glycan patterns between cells at different biological states. Changes detected through staining, affinity assays, or lectin profiling may indicate that cell-surface glycosylation changes alongside differentiation. This provides a carbohydrate-focused complement to broader analyses of cellular identity and helps investigate how glycan patterns relate to cell function.