Phospho-EGFR (Tyr1173) antibodies are immunological tools designed to detect the activated form of the epidermal growth factor receptor (EGFR) when phosphorylated at tyrosine residue 1173. EGFR, a receptor tyrosine kinase, plays a central role in regulating cell proliferation, survival, and differentiation. Upon ligand binding (e.g., EGF or TGF-α), EGFR undergoes dimerization and autophosphorylation at specific tyrosine residues, including Tyr1173. within its intracellular domain. This phosphorylation event creates docking sites for downstream signaling adaptors like Grb2 and Shc, activating pathways such as MAPK/ERK and PI3K/AKT, which drive oncogenic processes.
Phospho-EGFR (Tyr1173) antibodies are widely used in research to study EGFR activation status in cancer, particularly in tumors with EGFR overexpression or mutations (e.g., non-small cell lung cancer). These antibodies enable detection of phosphorylated EGFR via techniques like Western blotting, immunohistochemistry, or flow cytometry, providing insights into receptor activity, therapeutic response, and resistance mechanisms. Dysregulated EGFR signaling is linked to tumor progression, making Tyr1173 phosphorylation a potential biomarker for targeted therapies (e.g., tyrosine kinase inhibitors). Validation of these antibodies ensures specificity for the phosphorylated epitope, avoiding cross-reactivity with other EGFR phospho-sites (e.g., Tyr1068 or Tyr1045) or unrelated proteins. Their application aids in both basic research and clinical investigations aimed at understanding EGFR-driven malignancies and optimizing therapeutic strategies.