ERBB4 (also known as HER4) is a member of the epidermal growth factor receptor (EGFR) tyrosine kinase family, which includes EGFR (HER1), ERBB2 (HER2), and ERBB3 (HER3). It plays critical roles in cell proliferation, differentiation, survival, and migration by binding to ligands like neuregulins (NRGs) and activating downstream signaling pathways such as PI3K/AKT and MAPK. Structurally, ERBB4 consists of an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyrosine kinase domain. Unlike other EGFR family members, ERBB4 undergoes unique proteolytic processing, generating soluble intracellular fragments that can translocate to the nucleus and regulate gene expression.
ERBB4 antibodies are essential tools for studying its expression, activation, and functional roles in both physiological and pathological contexts. These antibodies are widely used in techniques like Western blotting, immunohistochemistry (IHC), and flow cytometry to detect ERBB4 protein levels, phosphorylation status, and localization in tissues or cell lines. Dysregulation of ERBB4 is implicated in various cancers (e.g., breast, lung, and melanoma), neurodevelopmental disorders, and heart diseases, making it a potential therapeutic target. For instance, monoclonal antibodies targeting ERBB4 are explored for their ability to block ligand binding or receptor dimerization, thereby inhibiting oncogenic signaling. However, ERBB4's role remains context-dependent, acting as either a tumor suppressor or promoter depending on splice variants and cellular microenvironment. Research using ERBB4 antibodies continues to clarify its dual functions and therapeutic potential.