Concanavalin A
Concanavalin A - Related Videos
04:02
Ultrasound-Guided Concanavalin A Injection Into Inferior Lacrimal Gland: A Technique to Inoculate Inferior Lacrimal Gland With Concanavalin A to Induce Dry Eye Disease in Rabbit Model
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2025
In this video, we demonstrate the inoculation of Concanavalin A, a lymphocyte mitogen, into the inferior lacrimal gland of the eye of a rabbit to induce dry eye disease. Ultrasound or sonogram images are used to guide the precise location of the injection site and also to confirm the success of inoculation.
09:07
Concanavalin A-Based Sedimentation Assay to Measure Substrate Binding of Glucan Phosphatases
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2022
This method describes a lectin-based in vitro sedimentation assay to quantify the binding affinity of glucan phosphatase and amylopectin. This co-sedimentation assay is reliable for measuring glucan phosphatase substrate binding and can be applied to various solubilized glucan substrates.
08:04
A Rabbit Model of Aqueous-Deficient Dry Eye Disease Induced by Concanavalin A Injection into the Lacrimal Glands: Application to Drug Efficacy Studies
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Cited by 12 •
2020
This article describes the development of a method to induce acute or chronic dry eye disease in rabbits by injecting concanavalin A to all portions of the orbital lacrimal gland system. This method, superior to those already reported, generates a reproducible, stable model of dry eye suitable for the study of pharmacological agents.
11:09
Generating a "Humanized" Drosophila S2 Cell Line Sensitive to Pharmacological Inhibition of Kinesin-5
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Cited by 2 •
2016
This protocol describes how to generate a Drosophila S2 cell line that is sensitive to small molecule inhibitors of kinesin-5. The use of these cells in a cell-based error correction assay is also outlined.
02:50
An Assay to Study Bile-Salt Induced Biofilm Formation through EPS Matrix Detection
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2025
This video demonstrates a fluorescence-based method for quantifying bile salt-induced biofilm formation. Upon the addition of bile salts in the culture of a pathogenic enteric bacteria, biofilm production is detected using a fluorescent lectin that binds to the polysaccharides in the extracellular polymeric substance (EPS) matrix of the biofilm.
FAQs
Its carbohydrate-binding sites can attach to mannose and glucose residues on glycoproteins located on different neighboring cells. This multivalent binding links otherwise separate surface molecules and cells, creating visible agglutination. The effect provides a functional way to examine how carbohydrate distribution and accessibility influence cell-cell interactions and membrane organization.
Cells differ in the abundance, arrangement, and accessibility of surface glycoproteins carrying recognized sugars, so the same treatment can produce different outcomes. Concentration and exposure time also influence the extent of cross-linking or cellular stimulation. Controlling these variables is therefore essential when comparing agglutination or lymphocyte responses between experiments.
Binding to carbohydrate-bearing structures on immune-cell surfaces can trigger signaling associated with T-lymphocyte activation and proliferation. This response makes the lectin a controlled experimental stimulus rather than merely a cell-agglutinating reagent. Investigators can use the resulting change in lymphocyte growth or activation to examine cellular signaling and compare responses under defined treatment conditions.
Researchers can expose cells to the lectin and examine whether carbohydrate-dependent cross-linking produces agglutination. The observed response gives indirect information about the presence and accessibility of mannose- or glucose-containing structures on the cell surface. Comparing cell types or treatment conditions can help relate surface carbohydrate organization to differences in cell recognition and membrane behavior.
Because it recognizes particular sugar residues on glycoproteins, Concanavalin A can help isolate or characterize glycoprotein populations. Its binding provides a selective interaction for examining carbohydrate-bearing molecules rather than treating all proteins identically. In biology experiments, this supports analysis of glycoprotein composition and the relationship between carbohydrate structure and molecular recognition.
It is useful when researchers need to induce a controlled response from T lymphocytes and monitor activation or proliferation. Experimental designs should maintain consistent concentration and exposure conditions, since immune-cell responses can vary with treatment parameters. This application connects lectin-mediated surface recognition with measurable changes in lymphocyte behavior, supporting studies of cellular signaling and immune regulation.