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Lectins and Specificity |
Lectin Characteristics and Properties
Lectins are proteins that form reversible complexes with mono- or oligosaccharide structures. The strength of the binding event increases with the number of molecular interactions and thus from monovalent interactions to multivalent complexes. In general lectin-carbohydrate interactions are weaker than antigen-antibody complexes and their affinity constants are in the range of Kd = 10-6 - 10-7 mol/L for glycoproteins. Most lectins have the ability to agglutinate erythrocytes as they bind to blood group antigens. Several lectins display a blood group specificity.
Areas of Application for AffiSep Lectin Technology
Lectins have been extensively used for the purification and characterization of glycoconjugates in a variety of research areas. The list below shows examples for possible applications of the AffiSep separation technology.
- Purification and characterization of glycoproteins like: antibodies, cytokines, tumor associated glycoproteins, hormones, inhibitors, growth factors, various enzymes, membrane proteins (receptors), or even toxins and viruses
- Separation and structural analysis of oligosaccharides or glycopetides cleaved from glycoproteins
- Pattern analysis for tissue comparison
- Detection of different glycoforms in glycoproteins
Lectin specificity
How to use this list:
The following list shows the glycan binding specificity of the lectins used as ligands. Please select the carbohydrate structure you want to separate. Then choose an appropriate lectin or a combination of lectins from the list. You will find a variety of products for each of the displayed lectins.
|
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| Mannose binding lectins |
| Con A |
Concanavalin A |
Canavalia ensiformis |
branched α-mannosidic structures;
high-mannose type,
hybrid type and
biantennary complex type N-Glycans |
| LCH |
Lentil lectin |
Lens
culinaris |
Fucosylated core region of bi- and triantennary
complex type N-Glycans |
| GNA |
Snowdrop lectin |
Galanthus
nivalis |
α 1-3 and α 1-6 linked high mannose structures |
| Galactose / N-acetylgalactosamine binding lectins |
| RCA |
Ricinus communis Agglutinin, RCA120 |
Ricinus communis |
Galβ1-4GlcNAcβ1-R |
| PNA |
Peanut Agglutinin |
Arachis hypogaea |
Galβ1-3GalNAcα1-Ser/Thr (T-Antigen) |
| AIL |
Jacalin |
Artocarpus integrifolia |
(Sia)Galβ1-3GalNAcα1-Ser/Thr
(T-Antigen) |
| VVL |
Hairy vetch lectin |
Vicia villosa |
GalNAcα-Ser/Thr (Tn-Antigen) |
| Sialic acid / N-acetylglucosamine binding lectins |
| WGA |
Wheat Germ agglutinin |
Triticum vulgaris |
GlcNAcβ1-4GlcNAcβ1-4GlcNAc, Neu5Ac
(sialic acid) |
| SNA |
Elderberry lectin |
Sambucus nigra |
Neu5Acα2-6Gal(NAc)-R |
| MAL |
Maackia amurensis lectin |
Maackia amurensis |
Neu5Ac/Gcα2-3Galβ1-4GlcNAcβ1-R |
| Fucose binding lectins |
| UEA |
Ulex europaeus agglutinin |
Ulex europaeus |
Fucα1-2Gal-R |
| AAL |
Aleuria aurantia lectin |
Aleuria aurantia |
Fucα1-2Galβ1-4(Fucα1-3/4)Galβ1-
4GlcNAc;
R2-GlcNAcβ1-4(Fucα1-6)GlcNAc-R1 |
|
* To get a general overview only basic structural information is demonstrated. For details please contact our technical support or see the cited literature. The structures represent only examples for a binding event. Often lectins bind with high affinity to complex and multiantennary saccharide structures. This list does not claim to be complete. |
 more lectins |
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Literature
Gabius, H.-J.; Gabius, S. (Eds.): Glycosciences - Status and Perspectives. Weinheim: Chapman & Hall, 1997. ISBN 3-8261-0073-5
Goldstein, I. J.; Poretz, R. D.: Isolation, Physicochemical Characterization, and Carbohydrate-Binding Specificity of Lectins. In: Liener, I. E.; Sharon, N.; Goldstein, I. J. ( Eds.) The Lectins - Properties, Functions and Applications in Biology and Medicine. Orlando: Academic Press, 1986, S. 33-243.
Debray, H.; Decout, D.; Strecker, G.; Spik, G.; Montreuil, J. (1981): Specificity of Twelve Lectins Towards
Oligosaccharides and Glycopeptides Related to N-Glycosylproteins. Eur. J. Biochem., 117, 41-55.
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