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About "Lectin"
[Discovery]
In 1888, Peter Hermann Stillmark of Estonia discovered a protein component (hemagglutinin) that agglutinates red blood cells from the seeds of the plant castor bean (Ricinus communis), and this molecule was named "ricin".1) In the early 1900s, Japanese Hideyo Noguchi also found lectins in the venom of pit vipers and discovered limulin as an invertebrate lectin from horseshoe crabs.2,3)
[Nomenclature]
The term "lectin" was coined in 1954 by William C. Boyd and Elizabeth Shapleigh, based on the Latin words "lego/legere" (to read, choose, or gather) and the suffix "-in", which denotes proteins, to describe substances from plants that show blood group-specific agglutination of red blood cells.4)
[Definition]
In 1980, Irwin J. Goldstein, R. Colin Hughes, Michel Monsigny, Toshiaki Osawa, and Nathan Sharon defined lectins as "carbohydrate-binding proteins that have the ability to agglutinate cells or precipitate polysaccharides and glycoproteins, and are not immune response products (antibodies)".5)
While some lectins cannot agglutinate cells due to a lack of multivalent binding sites, other molecules, such as glycosyltransferases, glycosidases, carbohydrate-related transporters and kinases, can agglutinate cells. In 1981, Jan Kocourek and Václav Hořejší proposed a broader definition of lectins as "carbohydrate-binding proteins that do not modify the sugars they bind to".6,7) Lectins are often classified based on carbohydrate-binding specificity or gene family, reflecting species differences and a wide range of functions.8)
[Applications]
Inspired by the differences in agglutination reactions of red blood cells from different animals toward various lectins, Karl Landsteiner discovered the human ABO-type blood group (glycan antigens) in 1900 and he won the Nobel Prize in 1930.9) Lectins have long been used for analyzing and profiling the distinct surface glycans of different cells. Recently, technologies such as "lectin microarray-based glycan profiling" and "DNA barcode-labeled lectin single-cell glycan analysis" have been developed, making lectins crucial in cutting-edge research on cell surface glycans.10,11)
Products
Hemagglutinin Lectin (Recombinant lectins)
- R0225
- Recombinant Polyporus squamosus lectin (= rPSL1a) expressed in Escherichia coli
- R0226
- Recombinant Laetiporus sulphureus lectin N-Terminal Domain (= rLSL-N) expressed in Escherichia coli
- R0227
- Recombinant Marasmius oreades agglutinin (= rMOA) expressed in Escherichia coli
- R0228
- Recombinant Sclerotium rolfsii lectin (= rSRL) expressed in Escherichia coli
- R0229
- Recombinant Griffithsia sp. lectin (= rGRFT) expressed in Escherichia coli
- L0169
- Lectin, Fucose specific (= AOL) from Aspergillus oryzae (5mg/mL, PBS pH6.5)
Product No. R0225, R0226, R0227, R0228, R0229 were commercialized under license from National Institute of Advanced Industrial Science and Technology (AIST), Japan.
Product No. L0169 was commercialized under license from GEKKEIKAN SAKE COMPANY, LTD.
Applications
The differences in the cellular glycans of animal red blood cells can be easily observed with our lectin series.
On Cellular Glycans
- The surface of cells is covered with various glycans.
- They exist as glycoproteins, glycolipids, and glycosaminoglycans (GAGs).
- The structures vary depending on the species.
- The surface glycans differ depending on the type of cell.
- Glycan structures change due to diseases.
- They play a role in cell-to-cell communication signaling.
Comparison of Hemagglutination Activity
Prepare a 2-fold PBS dilution series (25 μL) of each lectin solution in a 96-well plate. After washing the animal preserved blood from Japan Bioserum Co., Ltd. three times with PBS at 5-10 fold the volume, adjust the red blood cells to 2% (v/v) in PBS. Add 50 μL of the red blood cell suspension to each well and incubate at room temperature for 30 minutes before observation.
Related Product Category Page
Carbohydrate-binding Specificity of Lectins, Lectin-Biotin Conjugates, 、Lectin-Agarose (LecBeads) are as follows:
Related Product Spotlight Page
Product Brochures
References
- 1) Über Ricin, ein giftiges Ferment aus den Samen von Ricinus communis. L. und einigen anderen Euphorbiaceen
- 2) Snake venom in relation to haemolysis, bacteriolysis, and toxicity
- 3) On the multiplicity of the serum haemagglutinins of cold blooded animals
- 4) Specific Precipitating Activity of Plant Agglutinins (Lectins)
- 5) What should be called a lectin?
- 6) Defining a lectin
- 7) Lectins, 2nd Edition
- 8) Introduction to "Lectin"
- 9) Zur Kenntnis der antifermentativen, lytischen und agglutinierenden Wirkungen des Blutserums und der Lymphe
- K. Landsteiner, Zentralbl. Bakteriol. 1900, 27, 357.
- 10) Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling
- 11) scGR-seq: Integrated analysis of glycan and RNA in single cells
