Introduction
Working with EY Laboratories we are able to supply the world's largest selection of Lectins, isolated from plant and animal components. Lectins are proteins that bind to specific carbohydrate groups on proteins or on cell membranes. In glycobiology, Lectins can be used to study glycoproteins due to their specific binding to the carbohydrate (or glycosylated) section.
It is believed that most Lectins consist of non-covalently associated subunits. This multimeric structure gives Lectins their ability to form precipitates with glycoconjugates or to agglutinate cells. However, it can be difficult to detect Lectins in nature as many do not agglutinate cells at all.
Uses of Lectins
Despite a lack of understanding of these proteins in nature, Lectins are powerful tools allowing researchers to study a wide variety of biological structures and processes. Even oligosaccharides with identical sugar compositions can be separated. Lectins vary in their binding requirements, some will only bind to mannose or glucose residues, others bind only to galactose residues. Similarly, some Lectins require that the sugar residue is in a particular position in the oligosaccharide, either at a specific end, or in a terminal position.
Lectins are presently used in the clinical laboratory to type blood cells. Additionally, there is a wide spectrum of specialist applications, including:
- As carriers of chemotherapeutic agents
- As mitogens, for fractionation of animal cells
- Investigations of cellular surfaces
Lectins can be used to bind to the sugar residues on microbial surfaces, and are important diagnostic reagents in clinical microbiology. They can be used to isolate one cell or virus from a mixture, or to study one process amongst several. Lectins have been used successfully as epidemiologic as well as taxonomic markers of specific microorganisms.
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