Triticum vulgaris Lectin (WGA) - MagneZoom™

Wheat germ agglutinin (WGA) is a lectin that is affinity purified from Triticum vulgaris and non-enzymatically binds to N-acetyl-D-glucosamine and sialic acid residues of glycoproteins and glycolipids. This lectin protects Triticum vulgaris from insects, yeast and bacteria. WGA consists of two subunits and has a molecular weight of 36 kDa. It is an acidic protein and has mitogenic activity toward lymphocytes. It agglutinates erythrocytes and most types of malignant cells.

Similar to insulin, WGA enhances the rate of glucose oxidation in isolated fat cells.  and is used for isolation and fractionation of insulin receptors. A recent time-of-addition study made it evident that WGA inhibits infection with SARS-CoV-2 by inhibiting replication when the lectin is incubated with the virus and added to cells during infection. The data from the same study indicated the mode of action is an interaction between WGA and the viral envelope, causing neutralization of the virus. It is possible this occurs via the highly glycosylated spike proteins. WGA has been used in oral squamous cell carcinoma staining techniques to test the degree of cell cohesion. It has been shown to inhibit melanoma cell proliferation in a dose-dependent manner. Cytotoxic activity on cancer cell lines is characteristic of WGA. The effects of its binding have been studied in a plethora of cancers including but not limited to hepatoma, choriocarcinoma, osteosarcoma, and some pancreatic cancers.

Triticum vulgaris Lectin (WGA) - MagneZoom are silica-coated super paramagnetic beads covalently linked to Wheat Germ Agglutinin (WGA). The aminated paramagnetic beads are immobilized using EDC and stabilized in a buffer to retain maximum activity. These beads are ideal for iP applications to pull down glycoproteins.

bioWORLD's products are supplied for LABORATORY RESEARCH USE ONLY. The product may not be used as a drug, agricultural or pesticidal product, food additive or as a household chemical

Specifications:

• Suspension: 25 mg magnetic beads/mL

• Particle size (average): 2-5 µm

• Ligand: Triticum vulgaris (Wheat Germ) Lectin (WGA)

• Ligand density: ~3 mg/mL

• Binding Capacity: 2-3 mg/mL

• pH stability: 4-9 (for use), 2-10 (for cleaning)

• Supplied in: Saline solution/0.02% sodium azide

Application

iP applications

References

Auth, J., Fröba, M., Große, M., Rauch, P., Ruetalo, N., Schindler, M., Morokutti-Kurz, M., Graf, P., Dolischka, A., Prieschl-Grassauer, E., Setz, C., & Schubert, U. (2021). Lectin from Triticum vulgaris (WGA) Inhibits Infection with SARS-CoV-2 and Its Variants of Concern Alpha and Beta. International journal of molecular sciences, 22(19), 10205. https://doi.org/10.3390/ijms221910205

Johnson, R. J., Simpson, S., Van Epps, D. E., & Chenoweth, D. E. (1992). Wheat germ agglutinin inhibits the C5a receptor interaction: implications for receptor microheterogeneity and ligand binding site. Journal of leukocyte biology, 52(1), 3–10. https://doi.org/10.1002/jlb.52.1.3

Loréa, P., Goldschmidt, D., Darro, F., Salmon, I., Bovin, N., Gabius, H. J., Kiss, R., & Danguy, A. (1997). In vitro characterization of lectin-induced alterations on the proliferative activity of three human melanoma cell lines. Melanoma research, 7(5), 353–363. https://doi.org/10.1097/00008390-199710000-00001

Schwarz, R. E., Wojciechowicz, D. C., Picon, A. I., Schwarz, M. A., & Paty, P. B. (1999). Wheatgerm agglutinin-mediated toxicity in pancreatic cancer cells. British journal of cancer, 80(11), 1754–1762. https://doi.org/10.1038/sj.bjc.6690593

Silveyra, E., Bologna-Molina, R., Gónzalez-Gónzalez, R., & Arocena, M. (2021). The Tissue Architecture of Oral Squamous Cell Carcinoma Visualized by Staining Patterns of Wheat Germ Agglutinin and Structural Proteins Using Confocal Microscopy. Cells, 10(9), 2466. https://doi.org/10.3390/cells10092466

Wang, H., Ng, T. B., Ooi, V. E., & Liu, W. K. (2000). Effects of lectins with different carbohydrate-binding specificities on hepatoma, choriocarcinoma, melanoma and osteosarcoma cell lines. The international journal of biochemistry & cell biology, 32(3), 365–372. https://doi.org/10.1016/s1357-2725(99)00130-2