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HomeGlycobiologyLectin Selection Guide: A Useful Guide for Selecting the Right Lectin

Lectin Selection Guide: A Useful Guide for Selecting the Right Lectin

Need a lectin for your research but aren’t sure which one to choose? Explore our lectin selection guide, conveniently organized by lectin source/species, carbohydrate specificity, and more to find the right lectin for your research.

Diagram depicting lectin strategies in glycoproteomic research. Lectins vary based on their properties such as lectin source/species, carbohydrate specificity, mitogenic and agglutinating activities, and more.

What Are Lectins?

Lectins are proteins or glycoproteins from non-immune origins that are known to bind to specific carbohydrate structures. They agglutinate cells and/or precipitate complex carbohydrates. Lectins are isolated from a wide variety of natural sources, both plant and animal. Recombinant human and rat galectins are expressed in Escherichia coli. The agglutination activity of these highly specific carbohydrate-binding molecules is usually inhibited by a simple monosaccharide, but for some lectins di-, tri-, and even polysaccharides are required. 

Lectin Selection Guide

Lectins have unique carbohydrate specificities and can be used for various applications, such as cell surface labeling, glycoprotein purification, and carbohydrate analysis. Our lectin product line includes lectins from various sources such as plants, bacteria, and animals. These proteins have a wide range of biological activities such as mitogenic and agglutinating activities on certain cell types, making them useful for many different research areas.

In this lectin selection guide, we present various lectins along with their specific carbohydrate recognition specificities, mitogenic and agglutinating activities for certain cell types, and recommended applications. This comprehensive guide will aid in the selection of the most suitable lectin for your research needs.


Arachis hypogaea (peanut)

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Artocarpus heterophyllus (jackfruit)

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Bandeiraea simplicifolia (Griffonia simplicifolia)

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Canavalia ensiformis (jack bean)

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Dolichos biflorus (horse gram)

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Erythrina cristagalli (coral tree)

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Galanthus nivalis (snowdrop)

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Glycine max (soybean)

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Helix pomatia (snail)

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Homo sapiens

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Lens culinaris (lentil)

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Lycopersicon esculentum (tomato)

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Phaseolus vulgaris (red kidney bean)

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Phytolacca americana (pokeweed)

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Pisum sativum (pea)

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Pseudomonas aeruginosa

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Triticum vulgaris (wheat germ)

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Ulex europaeus (gorse, furze)

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Wisteria floribunda

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Footnotes

  1. Mitogenic for neuraminidase-treated lymphocytes
  2. Inhibits mitogenic activity of PHA
  3. Non-agglutinating and mitogenic
  4. More rare, only for specific structures; See references for more detail
  5. Isolectin B4 enriched for specificity against Blood Type B, but some Type A agglutination activity may be present
  6. Agglutinates neuraminidase-treated O-type RBCs
  7. Stronger binding to Forssman antigen than blood group A
  8. Has anti-mitogenic activity
  9. If empty, lectin may have agglutinating activities, but may not be characterized or is not specific to erythrocytes or leukocytes
  10. Not considered mitogenic, but will induce cytokine production

References

1.
Bojar D, Meche L, Meng G, Eng W, Smith DF, Cummings RD, Mahal LK. 2022. A Useful Guide to Lectin Binding: Machine-Learning Directed Annotation of 57 Unique Lectin Specificities. ACS Chem. Biol.. 17(11):2993-3012. https://doi.org/10.1021/acschembio.1c00689
2.
Ashraf MT, Khan RH. 2003. Med Sci Monit.(9(11)):RA265-269.
3.
1994. Histochemical Study of Glycoconjugates in the Actinopterygian Olfactory System. Lectins: Biology, Biochemistry, Clinical Biochemistry. Textop. Volume 6p 727.
4.
Tsaneva M, Van Damme EJM. 2020. 130 years of Plant Lectin Research. Glycoconj J. 37(5):533-551. https://doi.org/10.1007/s10719-020-09942-y
5.
1995. Histochemical Study of Glycoconjugates in the Actinopterygian Olfactory System. Lectins: Biology, Biochemistry, Clinical Biochemistry. Textop. Volume 10p 29.
6.
Muraille E, Pajak B, Urbain J, Leo O. 1999. Carbohydrate-Bearing Cell Surface Receptors Involved in Innate Immunity: Interleukin-12 Induction by Mitogenic and Nonmitogenic Lectins. Cellular Immunology. 191(1):1-9. https://doi.org/10.1006/cimm.1998.1401
7.
Barre A, Bourne Y, Van Damme E, Rougé P. Overview of the Structure–Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi. IJMS. 20(2):254. https://doi.org/10.3390/ijms20020254
8.
IGLESIAS JL, LIS H, SHARON N. 1982. Purification and Properties of a d-Galactose/N-Acetyl-d- galactosamine-Specific Lectin from Erythrina cristagalli. Eur J Biochem. 123(2):247-252. https://doi.org/10.1111/j.1432-1033.1982.tb19760.x
9.
Wu AM, Wu JH, Tsai M, Yang Z, Sharon N, Herp A. 2007. Differential affinities of Erythrina cristagalli lectin (ECL) toward monosaccharides and polyvalent mammalian structural units. Glycoconj J. 24(9):591-604. https://doi.org/10.1007/s10719-007-9063-y
10.
Modenutti CP, Capurro JIB, Di Lella S, Martí MA. The Structural Biology of Galectin-Ligand Recognition: Current Advances in Modeling Tools, Protein Engineering, and Inhibitor Design. Front. Chem.. 7 https://doi.org/10.3389/fchem.2019.00823
11.
Nagae M, Nishi N, Nakamura-Tsuruta S, Hirabayashi J, Wakatsuki S, Kato R. 2008. Structural Analysis of the Human Galectin-9 N-terminal Carbohydrate Recognition Domain Reveals Unexpected Properties that Differ from the Mouse Orthologue. Journal of Molecular Biology. 375(1):119-135. https://doi.org/10.1016/j.jmb.2007.09.060
12.
Tateno H, Nakamura-Tsuruta S, Hirabayashi J. 2009. Comparative analysis of core-fucose-binding lectins from Lens culinaris and Pisum sativum using frontal affinity chromatography. Glycobiology. 19(5):527-536. https://doi.org/10.1093/glycob/cwp016
13.
Nachbar M, Oppenheim J, Thomas J. 1980. Lectins in the U.S. Diet. Isolation and characterization of a lectin from the tomato (Lycopersicon esculentum).. Journal of Biological Chemistry. 255(5):2056-2061. https://doi.org/10.1016/s0021-9258(19)85992-6
14.
DALLAPELLEGRINA C, RIZZI C, MOSCONI S, ZOCCATELLI G, PERUFFO A, CHIGNOLA R. 2005. Plant lectins as carriers for oral drugs: Is wheat germ agglutinin a suitable candidate?. Toxicology and Applied Pharmacology. 207(2):170-178. https://doi.org/10.1016/j.taap.2005.01.001
15.
Sharon N. 2007. Lectins: Carbohydrate-specific Reagents and Biological Recognition Molecules. Journal of Biological Chemistry. 282(5):2753-2764. https://doi.org/10.1074/jbc.x600004200
16.
Kawakami K, Yamamoto Y, Onoue K. 1988. Effect of Wheat Germ Agglutinin on T Lymphocyte Activation. Microbiology and Immunology. 32(4):413-422. https://doi.org/10.1111/j.1348-0421.1988.tb01400.x
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