ECE1 (Endothelin-converting enzyme 1) is a membrane-bound metalloprotease primarily involved in the biosynthesis of endothelin-1 (ET-1), a potent vasoconstrictor peptide. Discovered in the early 1990s, ECE1 cleaves the inactive precursor big endothelin-1 to produce mature ET-1. which regulates vascular tone, cell proliferation, and hormonal balance. Its expression is observed in endothelial cells, smooth muscle cells, and various tissues, including the lungs, kidneys, and heart. Dysregulation of ECE1 activity has been linked to cardiovascular diseases (e.g., hypertension, pulmonary arterial hypertension), cancer progression, and fibrotic disorders.
ECE1 antibodies are essential tools for detecting and quantifying ECE1 protein levels in research. They enable the study of ECE1's cellular localization, expression patterns, and regulatory mechanisms through techniques like Western blotting, immunohistochemistry, and ELISA. Specific antibodies targeting different ECE1 isoforms (e.g., ECE1a, ECE1b) help clarify isoform-specific functions. Additionally, ECE1 inhibitors are explored as therapeutic agents, making these antibodies critical for validating drug efficacy and target engagement in preclinical models. Recent studies also investigate ECE1's role in tumor angiogenesis and metastasis, expanding its relevance beyond cardiovascular biology. Commercial ECE1 antibodies are typically validated for cross-reactivity and specificity across human, mouse, and rat samples.