Development of an anti-human EphA2 monoclonal antibody Ea2Mab-7 for multiple applications

Ephrin type A receptor 2 (EphA2) binds to membrane-bound ligands, ephrin A1, A2, and A5, eliciting bidirectional signaling. This signaling regulates many physiological processes, such as tissue development, homeostasis, and regeneration. The dysregulation of the EphA2-ephrins axis contributes to var...

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Main Authors: Hiroyuki Satofuka, Hiroyuki Suzuki, Tomohiro Tanaka, Guanjie Li, Mika K. Kaneko, Yukinari Kato
Format: Article
Language:English
Published: Elsevier 2025-06-01
Series:Biochemistry and Biophysics Reports
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Online Access:http://www.sciencedirect.com/science/article/pii/S2405580825000858
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author Hiroyuki Satofuka
Hiroyuki Suzuki
Tomohiro Tanaka
Guanjie Li
Mika K. Kaneko
Yukinari Kato
author_facet Hiroyuki Satofuka
Hiroyuki Suzuki
Tomohiro Tanaka
Guanjie Li
Mika K. Kaneko
Yukinari Kato
author_sort Hiroyuki Satofuka
collection DOAJ
description Ephrin type A receptor 2 (EphA2) binds to membrane-bound ligands, ephrin A1, A2, and A5, eliciting bidirectional signaling. This signaling regulates many physiological processes, such as tissue development, homeostasis, and regeneration. The dysregulation of the EphA2-ephrins axis contributes to various diseases, including cancers. The high expression of EphA2 is observed in various cancers, which promotes cancer malignancy, whereas its levels are relatively low in most normal adult tissues. Therefore, EphA2 is a promising target for cancer therapy. We developed anti-human EphA2 monoclonal antibodies in this study using the Cell-Based Immunization and Screening method. Among them, a clone Ea2Mab-7 (IgG1, κ) exhibited a high affinity and sensitivity in flow cytometry. The dissociation constant values of Ea2Mab-7 for CHO/EphA2 and MDA-MB-231 cells were determined as 6.2 ± 1.3 × 10−9 M and 1.6 ± 0.4 × 10−9 M, respectively. Furthermore, Ea2Mab-7 can detect endogenous EphA2 in Western blot and immunohistochemistry. Therefore, the Ea2Mab-7 is highly versatile for basic research and is expected to contribute to clinical applications, such as antibody therapy and tumor diagnosis.
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spelling doaj-art-3a3ddc68f783413aaa7620c7cd4527172025-08-20T02:17:13ZengElsevierBiochemistry and Biophysics Reports2405-58082025-06-014210199810.1016/j.bbrep.2025.101998Development of an anti-human EphA2 monoclonal antibody Ea2Mab-7 for multiple applicationsHiroyuki Satofuka0Hiroyuki Suzuki1Tomohiro Tanaka2Guanjie Li3Mika K. Kaneko4Yukinari Kato5Department of Antibody Drug Development, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai, Miyagi, 980-8575, JapanDepartment of Antibody Drug Development, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai, Miyagi, 980-8575, JapanDepartment of Antibody Drug Development, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai, Miyagi, 980-8575, JapanDepartment of Antibody Drug Development, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai, Miyagi, 980-8575, JapanDepartment of Antibody Drug Development, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai, Miyagi, 980-8575, JapanCorresponding author.; Department of Antibody Drug Development, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai, Miyagi, 980-8575, JapanEphrin type A receptor 2 (EphA2) binds to membrane-bound ligands, ephrin A1, A2, and A5, eliciting bidirectional signaling. This signaling regulates many physiological processes, such as tissue development, homeostasis, and regeneration. The dysregulation of the EphA2-ephrins axis contributes to various diseases, including cancers. The high expression of EphA2 is observed in various cancers, which promotes cancer malignancy, whereas its levels are relatively low in most normal adult tissues. Therefore, EphA2 is a promising target for cancer therapy. We developed anti-human EphA2 monoclonal antibodies in this study using the Cell-Based Immunization and Screening method. Among them, a clone Ea2Mab-7 (IgG1, κ) exhibited a high affinity and sensitivity in flow cytometry. The dissociation constant values of Ea2Mab-7 for CHO/EphA2 and MDA-MB-231 cells were determined as 6.2 ± 1.3 × 10−9 M and 1.6 ± 0.4 × 10−9 M, respectively. Furthermore, Ea2Mab-7 can detect endogenous EphA2 in Western blot and immunohistochemistry. Therefore, the Ea2Mab-7 is highly versatile for basic research and is expected to contribute to clinical applications, such as antibody therapy and tumor diagnosis.http://www.sciencedirect.com/science/article/pii/S2405580825000858EphA2Monoclonal antibodyCell-Based Immunization and ScreeningFlow cytometryImmunohistochemistryBreast cancer
spellingShingle Hiroyuki Satofuka
Hiroyuki Suzuki
Tomohiro Tanaka
Guanjie Li
Mika K. Kaneko
Yukinari Kato
Development of an anti-human EphA2 monoclonal antibody Ea2Mab-7 for multiple applications
Biochemistry and Biophysics Reports
EphA2
Monoclonal antibody
Cell-Based Immunization and Screening
Flow cytometry
Immunohistochemistry
Breast cancer
title Development of an anti-human EphA2 monoclonal antibody Ea2Mab-7 for multiple applications
title_full Development of an anti-human EphA2 monoclonal antibody Ea2Mab-7 for multiple applications
title_fullStr Development of an anti-human EphA2 monoclonal antibody Ea2Mab-7 for multiple applications
title_full_unstemmed Development of an anti-human EphA2 monoclonal antibody Ea2Mab-7 for multiple applications
title_short Development of an anti-human EphA2 monoclonal antibody Ea2Mab-7 for multiple applications
title_sort development of an anti human epha2 monoclonal antibody ea2mab 7 for multiple applications
topic EphA2
Monoclonal antibody
Cell-Based Immunization and Screening
Flow cytometry
Immunohistochemistry
Breast cancer
url http://www.sciencedirect.com/science/article/pii/S2405580825000858
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