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Description
The monoclonal antibody B2C10 reacts with galectin-3, a 30 kDa protein. Galectin-3 is a member of the galectin family. The protein is composed of three domains: a small amino-terminal domain, a carboxyl-terminal carbohydrate recognition domain (CRD) and amino-terminal domain containing repeating elements. Galectin-3 is normally distributed in epithelia of many organs and various inflammatory cells, including macrophages, as well as dendritic cells and Kupffer cells. The expression of this lectin is up-regulated during inflammation, cell proliferation, cell differentiation and through trans-activation by viral proteins. The expression is also affected by neoplastic transformation: up-regulated in certain types of lymphomas and thyroid carcinoma, while down-regulated in other types of malignancies, such as colon, breast, ovarian and uterine carcinomas. Galectin-3 has been shown to function through both intracellular and extracellular actions. Related to its intracellular functions, galectin-3 has been identified as a component of heterogeneous nuclear ribonuclear protein (hnRNP), a factor in pre-mRNA splicing, and has been found to control cell cycle and prevent T cell apoptosis. On the other hand, this protein has also been demonstrated to function as extracellular molecule in activating various types of cells, including monocytes/macrophages, mast cells, neutrophils and lymphocytes. Galectin-3 has been shown to mediate cell-cell and cell-extracellular matrix interactions. The monoclonal antibody B2C10 inhibits the binding of 125I-labeled galectin-3 to IgE coated on microtiter plates, the galecin-3's hemagglutination activity and galectin-3-induced superoxide production by human neutrophils. This inhibitory activity of B2C10 is probably the result of its disruption of the self-association process. The epitope of the monoclonal antibody B2C10 is found within the first 45 amino acids of galectin-3. The antibody B2C10 does not react with Galecin-3C and is cross reactive with mouse galectin-3.