Epidermal Growth Factor Receptor Sf9 Human Recombinant
Epidermal Growth Factor Receptor Human Recombinant Sf9, Active
Epidermal Growth Factor Receptor, CHO Human Recombinant
The Epidermal Growth Factor Receptor (EGFR), also known as ErbB-1 or HER1, is a transmembrane protein that belongs to the ErbB family of receptor tyrosine kinases. This family includes four closely related receptors: EGFR (ErbB-1), HER2/neu (ErbB-2), HER3 (ErbB-3), and HER4 (ErbB-4) . EGFR is a receptor for members of the epidermal growth factor family of extracellular protein ligands .
Key Biological Properties: EGFR is a transmembrane protein activated by binding specific ligands, such as epidermal growth factor (EGF) and transforming growth factor alpha (TGF-α) . Upon activation, EGFR undergoes a transition from an inactive monomeric form to an active homodimer .
Expression Patterns and Tissue Distribution: EGFR is expressed in many tissues, including epithelial tissues, and plays a crucial role in the regulation of cell growth, survival, proliferation, and differentiation . It is also found in various human tissues, including the skin, lungs, and gastrointestinal tract .
Primary Biological Functions: EGFR regulates key processes of cell biology, including cell proliferation, survival, and differentiation . It is essential for the development and maintenance of epithelial tissues .
Role in Immune Responses and Pathogen Recognition: EGFR plays a role in the immune response by modulating the activity of immune cells and influencing the production of cytokines . It is also involved in pathogen recognition and the host response to viral infections .
Mechanisms with Other Molecules and Cells: EGFR is activated by ligand binding, which induces dimerization and autophosphorylation of tyrosine residues in its intracellular domain . This activation triggers downstream signaling cascades, including the MAPK, PI3K, and JAK/STAT pathways .
Binding Partners and Downstream Signaling Cascades: EGFR interacts with various binding partners, such as SH2 and PTB domain-containing proteins, which mediate its downstream signaling . These signaling pathways regulate cellular processes such as proliferation, migration, and survival .
Regulatory Mechanisms Controlling Expression and Activity: EGFR expression and activity are regulated by multiple mechanisms, including transcriptional regulation, post-translational modifications, and feedback loops . Phosphorylation of specific tyrosine residues and interactions with phosphotyrosine phosphatases (PTPs) are key regulatory mechanisms .
Transcriptional Regulation and Post-Translational Modifications: EGFR transcription is regulated by various transcription factors, while post-translational modifications, such as phosphorylation, ubiquitination, and glycosylation, modulate its activity and stability .
Biomedical Research: EGFR is extensively studied in biomedical research due to its role in cell signaling and cancer . It serves as a model for understanding receptor tyrosine kinase signaling and its implications in diseases .
Diagnostic Tools and Therapeutic Strategies: EGFR is a critical biomarker and therapeutic target in cancer diagnosis and treatment . Targeted therapies, such as tyrosine kinase inhibitors (TKIs) and monoclonal antibodies, have been developed to inhibit EGFR signaling in cancers with EGFR overexpression or mutations .
Role Throughout the Life Cycle: EGFR is essential for normal development, tissue homeostasis, and regeneration . It plays a critical role in embryonic development, particularly in the formation of epithelial tissues . In adults, EGFR maintains tissue integrity and promotes wound healing . Dysregulation of EGFR signaling is associated with aging and various diseases, including cancer and neurodegenerative disorders .