EPHA2 Antibodies

Structure of EPHA2

EPHA2 is a type I transmembrane protein with a molecular weight of approximately 130 kDa. The molecular weight of this protein varies among different species, mainly due to the subtle changes in the glycosylation modification degree of its extracellular domain and the amino acid sequence.

EPHA2 is composed of 975 amino acids. Its structure includes an extracellular region (consisting of a ligand-binding domain, a fibronectin III repeat sequence, and two calcium-dependent domains), a transmembrane region, and an intracellular tyrosine kinase domain. The ligand binding mechanism of this protein depends on the global conformational changes in its extracellular region: when binding to the ephrin-A ligand, the two EPHA2 molecules form a dimer, initiating the autophosphylation of specific residues (such as Y594 and Y772) in the tyrosine kinase domain, thereby initiating downstream signal transduction. This precise conformational regulation mechanism ensures that EPHA2 can play a crucial guiding role in processes such as cell communication, tissue boundary formation, and cell migration.

Fig. 1 Schematic representation of EphA2-driven mechanisms in cancer.¹

Key structural properties of EPHA2:

• The extracellular region contains ligand-binding domains and fibronectin repeats
• A single transmembrane helix is anchored to the cell membrane
• Intracellular parts as the typical tyrosine kinase catalytic domain structure
• Carboxyl terminal of hydrophobic amino acids regulate its phosphorylation activity

Functions of EPHA2

The EPHA2 receptor plays a core role in cell communication and tissue construction, and its function shows significant context dependence: it guides cell localization in normal tissues, while promoting malignant progression in pathological conditions.

The signal output of EPHA2 is highly dependent on its tyrosine phosphorylation status: ligand activation triggers auto-phosphorylation and initiates inhibitory signals, while non-ligand activation leads to abnormal phosphorylation patterns, which in turn drive cancer-promoting signals. This bidirectional regulatory mechanism explains the functional differences between EPHA2 in development and disease.

Applications of EPHA2 and EPHA2 Antibody in Literature

1. Toracchio, Lisa, et al. "EphA2 in cancer: molecular complexity and therapeutic opportunities." International Journal of Molecular Sciences 25.22 (2024): 12191. https://doi.org/10.3390/ijms252212191

The article indicates that the oncoprotein EphA2 has a complex function and drives tumor deterioration. Limited by traditional therapies, new strategies based on their molecular mechanisms, such as immunotherapy and PROTAC degraders, have shown great therapeutic potential.

2. Xiao, Ta, et al. "Targeting EphA2 in cancer." Journal of hematology & oncology 13.1 (2020): 114. https://doi.org/10.1186/s13045-020-00944-9

The article indicates that EphA2 is highly expressed in tumors and is a potential therapeutic target. Its signaling axis with the ligand ephrin A1 promotes carcinogenesis and drug resistance. Although the clinical efficacy of existing targeted drugs is limited, it remains an important research and development direction for anti-cancer strategies.

3. Gai, Qu-Jing, et al. "EPHA2 mediates PDGFA activity and functions together with PDGFRA as prognostic marker and therapeutic target in glioblastoma." Signal transduction and targeted therapy 7.1 (2022): 33. https://doi.org/10.1038/s41392-021-00855-2

This study reveals that EPHA2 is a new potential receptor for PDGFA, and the combination of the two can independently activate cancer-promoting signals. Simultaneous inhibition of EPHA2 and PDGFRA can synergistically prevent the growth of glioma, overcome single-drug resistance, and provide a new treatment strategy.

4. El Fakiri, Mohamed, et al. "Development and preclinical characterization of a novel radiotheranostic EphA2-targeting bicyclic peptide." Theranostics 14.12 (2024): 4701. https://doi.org/10.7150/thno.96641

This study developed a novel bicyclic peptide, BCY18469, as an EPHA2-targeted radioactive diagnostic and therapeutic agent. It has demonstrated excellent properties such as high affinity, specific tumor enrichment and rapid renal clearance in preclinical studies, indicating the great potential of bicyclic peptides in diagnosis and treatment applications.

5. Giordano, Giorgia, et al. "Targeting the EphA2 pathway: could it be the way for bone sarcomas?." Cell Communication and Signaling 22.1 (2024): 433. https://doi.org/10.1186/s12964-024-01811-7

This study indicates that EphA2 is overexpressed in osteosarcoma and is a key oncoprotein mediating metastasis and chemotherapy resistance. For unresectable advanced patients, targeting EphA2 provides a new strategy for the precise diagnosis and treatment of osteosarcoma, chondrosarcoma and Ewing's sarcoma.

Creative Biolabs: EPHA2 Antibodies for Research

Creative Biolabs specializes in the production of high-quality EPHA2 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom EPHA2 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our EPHA2 antibodies, custom preparations, or technical support, contact us at email.