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Epitope Mapping of an Anti-HER2 Monoclonal Antibody (H2Mab-181) Using Enzyme-Linked Immunosorbent Assay
Teizo Asano1, Junko Takei1, Hiroyuki Suzuki2
1Department of Antibody Drug Development and Tohoku University Graduate School of Medicine, Sendai, Japan.
Human epidermal growth factor receptor 2 (HER2) is a type I transmembrane 185 kDa protein expressed in various types of normal or cancer cells. Overexpression of HER2 is found in many cancers and is related to cell proliferation, differentiation, and migration. We recently developed a novel anti-HER2 monoclonal antibody, H2Mab-181, by immunizing mice with the purified recombinant extracellular domain of HER2. H2Mab-181 can specifically and sensitively detect HER2 not only in flow cytometry and Western blotting for gastric cancer cell lines, but also in immunohistochemical analyses for gastric cancer tissues. In this study, we analyzed the binding epitope of H2Mab-181 to HER2 using enzyme-linked immunosorbent assay (ELISA). Results showed that the H2Mab-181 epitope was determined to be Gly383, Asp384, Ala386, Asn388, and Pro391 by ELISA.
Human epidermal growth factor receptor 2 (HER2) is a type I transmembrane 185 kDa protein expressed in various types of normal or cancer cells. Overexpression of HER2 is found in many cancers and is related to cell proliferation, differentiation, and migration. We recently developed a novel anti-HER2 monoclonal antibody, H2Mab-181, by immunizing mice with the purified recombinant extracellular domain of HER2. H2Mab-181 can specifically and sensitively detect HER2 not only in flow cytometry and Western blotting for gastric cancer cell lines, but also in immunohistochemical analyses for gastric cancer tissues. In this study, we analyzed the binding epitope of H2Mab-181 to HER2 using enzyme-linked immunosorbent assay (ELISA). Results showed that the H2Mab-181 epitope was determined to be Gly383, Asp384, Ala386, Asn388, and Pro391 by ELISA.
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