EGFR Antibody
Description
Product Specs
Product Science Overview
The Epidermal Growth Factor Receptor (EGFR) is a transmembrane protein that plays a crucial role in the regulation of cell growth, survival, proliferation, and differentiation. It is a member of the ErbB family of receptors, which includes EGFR (ErbB1), HER2/neu (ErbB2), HER3 (ErbB3), and HER4 (ErbB4). EGFR is activated by binding to its specific ligands, such as epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-α), leading to receptor dimerization and autophosphorylation on tyrosine residues. This activation triggers a cascade of downstream signaling pathways, including the MAPK, PI3K/AKT, and JAK/STAT pathways, which are involved in various cellular processes.
Overexpression or mutation of EGFR is associated with the development and progression of various cancers, including non-small cell lung cancer, colorectal cancer, and glioblastoma. EGFR overexpression is often correlated with poor prognosis and resistance to conventional therapies. As a result, EGFR has become a critical target for cancer therapy, with several therapeutic agents developed to inhibit its activity. These agents include monoclonal antibodies (e.g., cetuximab and panitumumab) that target the extracellular domain of EGFR and small molecule tyrosine kinase inhibitors (e.g., erlotinib and gefitinib) that inhibit its intracellular kinase activity .
Mouse anti-human EGFR antibodies are monoclonal antibodies generated in mice that specifically recognize and bind to human EGFR. These antibodies are widely used in research and clinical applications to study EGFR function, signaling, and its role in cancer. They are also employed in diagnostic assays and as therapeutic agents.
Mouse anti-human EGFR antibodies exert their effects through several mechanisms:
- Blocking Ligand Binding: These antibodies can block the binding of natural ligands (e.g., EGF and TGF-α) to EGFR, preventing receptor activation and downstream signaling.
- Receptor Internalization and Degradation: Binding of the antibodies to EGFR can induce receptor internalization and degradation, reducing the number of receptors available on the cell surface.
- Antibody-Dependent Cellular Cytotoxicity (ADCC): These antibodies can recruit immune cells, such as natural killer (NK) cells, to the tumor site, leading to the destruction of cancer cells through ADCC.
- Complement-Dependent Cytotoxicity (CDC): The antibodies can activate the complement system, resulting in the formation of membrane attack complexes that lyse cancer cells .
Mouse anti-human EGFR antibodies have shown significant clinical benefits in the treatment of various cancers. For example, cetuximab and panitumumab are approved for the treatment of metastatic colorectal cancer and head and neck squamous cell carcinoma. These antibodies have demonstrated efficacy in improving overall survival and progression-free survival in patients with EGFR-expressing tumors .
