EphA2 Protein, Cynomolgus (HEK293, His-Avi)

EphA2 Protein is a receptor tyrosine kinase that interacts with membrane-bound ephrin-A ligands on adjacent cells, resulting in contact-dependent bidirectional signaling. This receptor mediates both forward signaling and reverse signaling pathways. Activation by ephrin-A1/EFNA1 regulates various cellular processes, including migration, integrin-mediated adhesion, proliferation, and differentiation. EphA2 also influences cell adhesion and differentiation through its interaction with DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 signaling pathway. Additionally, it may play a role in UV radiation-induced apoptosis and stimulate chemotactic cell migration independently of ligand binding. During development, EphA2 is involved in pattern formation and contributes to the development of fetal tissues, such as angiogenesis, hindbrain development, and mammary gland morphogenesis. Its interaction with ephrin-A5/EFNA5 is crucial for maintaining lens transparency by regulating the shape and interactions of lens fiber cells. Furthermore, EphA2 participates in bone remodeling by regulating osteoclastogenesis and osteoblastogenesis through its interaction with ephrin-A2/EFNA2.