Abstract
Galectin-1 is a β-galactoside-binding lectin that has been implicated as a suppressive molecule in cancer and autoimmune diseases. Gal-1 has known immunomodulatory activity and was found to be expressed on regulatory T cells, leading to the potential for targeted immunotherapies. Anti-Gal-1 monoclonal antibodies were generated in this study using classical hybridoma techniques. MAb 6F3 was found to bind to Gal-1 by Western blot and ELISA. Flow cytometry was used to determine cell surface and intracellular binding of mAb 6F3 to Gal-1 in PBMC-derived Tregs and tumor cells, including Treg-like cell lines. These results suggest mAb 6F3 may be used to further study Gal-1 protein expression and function.
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