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Lectins are also immune proteins that recognize and bind to specific carbohydrate targets.
Proteins of non-immune origin with at least one non-catalytic domain that can recognize and reversibly bind to specific carbohydrate structures are referred to as 'lectins'lectins
Since lectins bind to specific carbohydrate residues on the cell surface, the decrease in staining reflects the loss of these binding sites due to radiation-induced membrane damage.
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Galectins, which are frequently exposed on the cell plasma membrane, bind to specific carbohydrates, which may be conserved interspecies, thus explaining our data on CD98-dependent adhesion of mouse blastocysts.
E-selectin is a cell adhesion molecule expressed on activated endothelial cells that recognizes and binds to specific carbohydrate determinants, such as SLex and SLea present on surface glycoconjugates [30].
Lectins are carbohydrate-binding proteins, which recognize and bind to specific sugar moieties with high specificity [34].
They have the unique ability to recognize and bind reversibly to specific carbohydrate ligands without any chemical modification which distinguishes lectins from other carbohydrate binding proteins and enzymes and makes them invaluable tools in biomedical and glycoconjugate research.
ConA-like domains are often found in proteins involved in cell recognition and adhesion, and lectins and glucanases are known to reversibly bind to specific complex carbohydrates.
Lectins are (glyco proteins possessing at least one noncatalytic domain that recognize and bind reversibly to specific carbohydrates inside and outside cells (Drickamer 1988; Kilpatric 2002; Sharon and Lis 2004).
These proteins bind to specific sites on DNA and (for example) turn on expression of specific genes.
Lectins and glucanases exhibit the common property of reversibly binding to specific (complex) carbohydrates.
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