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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.

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
Fucosylated core region of bi- and triantennary complex type N-Glycans
GNA Snowdrop lectin Galanthus
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
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-

* 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

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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