EphA2 Protein, Human (Active, sf9, His-GST)

EphA2 protein is a receptor tyrosine kinase that interacts with various membrane-bound ephrin-A family ligands on neighboring cells, leading to bidirectional signaling. This receptor is involved in regulating cell migration, adhesion, proliferation, and differentiation through forward and reverse signaling pathways. It plays a role in cell adhesion and differentiation by interacting with DSG1/desmoglein-1 and inhibiting the ERK1/ERK2 signaling pathway. Additionally, EphA2 protein may be involved in UV radiation-induced apoptosis and stimulate chemotactic cell migration independently of ligand binding. During development, it contributes to pattern formation and the development of fetal tissues, including angiogenesis, hindbrain development, and mammary gland morphogenesis. EphA2 protein also interacts with Ephrin-A5/EFNA5 to regulate lens fiber cells' shape and interactions, crucial for maintaining lens transparency. Moreover, it plays a role in bone remodeling by regulating osteoclastogenesis and osteoblastogenesis through its interaction with Ephrin-A2/EFNA2. Notably, EphA2 protein acts as a receptor for hepatitis C virus (HCV) in hepatocytes, facilitating viral cell entry by promoting the formation of CD81-CLDN1 receptor complexes and enhancing membrane fusion with HCV envelope glycoproteins.