Although monoclonal antibodies are promising, a truly fully human antibody is yet to be produced. Current human antibodies have the human sequence, but are produced in either transgenic animals or in phages. The aim of this paper was to produce a truly human antibody directed against an epitope of our choice, secreted by human plasma cells. The target protein was TMX2 one of the least studied disulfide isomerases. IgG and anti-TMX2 antibody were determined by both Elisa and western blot. TMX2 KD was evaluated by Surface Plasmon Resonance. TMX2 localization was determined by flow cytometry in MCF-7 cells. Efficiency was evaluated by MTT. Gene expression was evaluated by PCR. We have managed to produce two fully human antibodies directed against TMX2 protein. TMX2 protein was found both in the cytoplasm and cell membrane of breast cancer cells. RGCC TMX2 antibody recognizing an extracellular epitope increased cell proliferation. RGCC TMX2 antibody recognizing an intracellular epitope decreased cell proliferation and gene expression related to cancer survival, differentiation and metastasis. These findings suggest this platform is very promising for novel personalized therapies. TMX2 could be a novel target for cancer treatment.
Keywords: Antibody; TMX2; cancer; human; proliferation.
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