Triticum vulgare Lectin Production Service

Triticum vulgare Lectin Production Service

Triticum vulgare lectin (WGA) is a highly conservative class of chitin-binding lectin derived from Gramineae. It is a dimer with a molecular weight of 36 kDa, associated with two identical polypeptide chains with 171 residues. WGA shows high specificity for N-acetyl-D-glucosamine (NAcGlc) and N-acetyl-D-neuronal ammonia (NAcNeu).

WGA Extraction and Purification Service at CD BioGlyco

The content of WGA in wheat embryos is low and the purification process is complicated, resulting in lower yield and specific activity of WGA. At CD BioGlyco, we continuously optimize the extraction and purification processes to provide our clients with WGA production services with high yield and high purity.

Select fresh wheat germ and add organic solvent several times to remove lipids. In the natural air state, our researchers dry and grind the germ. The powder is dissolved in the buffer and extracted by stirring for 3-4h. Multiple repeated centrifugations are performed to collect the supernatant. Add ammonium sulfate for salting out, overnight at 4°C. Centrifugate the buffer again and collect the precipitat. Heat treat the precipitate in a water bath for some time. We collect the supernatant by multiple centrifugation at low temperatures. The precipitate is removed by centrifugation after dialysis. Purifications are purified using affinity and gel filtration columns.

Flow chart of extraction and purification of WGA. (CD BioGlyco) Fig.1 Flow chart of extraction and purification of WGA. (CD BioGlyco)

Publication

Paper Title: Cytoagglutination and cytotoxicity of Wheat Germ agglutinin isolectins against normal lymphocytes and cultured leukemic cell lines--relationship between structure and biological activity

Journal: Biochimica Biophysica Acta

IF: 6.219

Results: The three separations of WGA were structurally distinguishable and had high homology in amino acid composition. WGA-isolectins bound to leukemia cells to different degrees, showing different agglutination capacity and activity expression. Of these, WGA-2 binding was the strongest and the bioactive expression of WGA-3 was low. However, the three separations interacted similarly with the normal lymphocytes.

Plot of WGA-isolectin toxicity assay on normal and leukemic cell lines. Fig.2 Plot of WGA-isolectin toxicity assay on normal and leukemic cell lines. (Ohba, et al., 2003)

Applications of WGA

  • WGA has a strong affinity for mucus secretions from the intestinal mucosa and salivary glands, thus exposing previously protected intestinal epithelial cells to lectin-cell interactions.
  • WGA has potential in cancer treatment strategies. For example, WGA is found to induce lectin-dependent macrophage-mediated cytotoxicity in human bladder tumors (T-24).
  • WGA plays an important role in the study of morphological and functional microheterogeneity and transport mechanisms in rats and rabbits, including the isolation of specific types of cells.
  • WGA is used to enable quantitative binding of heterologous mucin fragments to nitrocellulose membranes.
  • WGA labeling combined with glycosidase digestion is used to identify sugar complexes within the cat submandibular gland as lectin receptors or to determine the effect of adjacent oligosaccharides on the affinity of lectins to several sugars, respectively.
  • WGA coupled with the cell surface glycoproteins is used to identify specific cellular populations, as well as to inhibit or promote certain immune or physiological activities.
  • WGA induces apoptosis in various normal and malignant variable cells with high efficiency.
  • WGA binds to the lectin receptor and plays a hormonal effect similar to the animal adipose tissue as insulin.

Advantages of Us

  • The miscellaneous proteins are further removed by gel filtration chromatography, and the process is efficient and simple. The purified WGA is performed on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) with a single band.
  • The miscellaneous proteins are quickly and efficiently removed by salting out grading and selective heat treatment.

CD BioGlyco has many years of extraction and purification experience in Natural Lectin Production. Specifically, we provide Plant Lectin Production Service, Animal Lectin Production Service, and Fungal Lectin Production Service. Please feel free to contact us if you would like to learn more about the manufacturing of WGA lectin.

References:

  1. Bassett, E.W. Large scale preparation of wheat germ agglutinin. Prep Biochem. 1975, 5(5-6): 461-77.
  2. Ohba, H.; et al. Cytoagglutination and cytotoxicity of Wheat Germ agglutinin isolectins against normal lymphocytes and cultured leukemic cell lines--relationship between structure and biological activity. Biochim Biophys Acta. 2003, 1619(2): 144-50.
This service is for Research Use Only, not intended for any clinical use.

Christmas 2024

About Us

CD BioGlyco is a world-class biotechnology company with offices in many countries. Our products and services provide a viable option to what is otherwise available.

Contact Us

Copyright © CD BioGlyco. All rights reserved.
0