A Disintegrin And Metalloprotease 9 (ADAM9) Antibody

Background

ADAM metallopeptidase domain 9 (ADAM9) is another member of the ADAM family of proteins, sharing structural similarities and functional properties with ADAM8. Like other ADAM proteins, ADAM9 contains several domains, including a metalloprotease domain, a disintegrin domain, a cysteine-rich domain, an EGF-like domain, a transmembrane domain, and a cytoplasmic tail. These domains enable ADAM9 to interact with other proteins and participate in various cellular processes.ADAM9 is widely expressed in various tissues and cell types, including the brain, heart, lungs, kidneys, and reproductive organs. Its expression pattern suggests diverse roles in physiological processes.ADAM9 plays a role in cell adhesion and migration by interacting with extracellular matrix components and cell surface receptors. It can promote cell migration by cleaving adhesion molecules and releasing cell-to-cell or cell-to-matrix contacts. As a metalloprotease, ADAM9 has the ability to cleave and process various substrates, including growth factors, cytokines, cell surface receptors, and extracellular matrix proteins. This proteolytic activity allows ADAM9 to regulate signaling pathways, cell behavior, and tissue remodeling. ADAM9 is often upregulated in various cancers, including breast cancer, lung cancer, prostate cancer, and pancreatic cancer. Its overexpression is associated with tumor progression, invasion, metastasis, and angiogenesis. ADAM9 promotes cancer cell migration and invasion by cleaving extracellular matrix proteins and cell adhesion molecules.ADAM9 has been implicated in neurological disorders such as Alzheimer's disease and multiple sclerosis. Its expression in the brain suggests potential roles in synaptic plasticity, neuronal migration, and myelination.ADAM9 has also been linked to cardiovascular diseases such as atherosclerosis and cardiac remodeling. Its involvement in cell adhesion, migration, and proteolysis may contribute to vascular remodeling and plaque formation