ADAM9 Recombinant Rabbit mAb (S-3270-74)

ADAM9 (A Disintegrin And Metalloproteinase 9) is a transmembrane glycoprotein belonging to the ADAM family of membrane-anchored metalloproteinases, characterized by a multi-domain structure comprising a prodomain, metalloprotease domain with zinc-binding catalytic site, disintegrin domain mediating cell-cell and cell-matrix interactions, cysteine-rich region, EGF-like domain, transmembrane helix, and cytoplasmic tail. As a sheddase, ADAM9 cleaves diverse substrates including epidermal growth factor receptor (EGFR) ligands (such as HB-EGF and amphiregulin), amyloid precursor protein (APP), Notch receptors, and adhesion molecules, thereby regulating signaling pathways involved in cell proliferation, migration, and adhesion. Beyond its proteolytic activity, ADAM9 functions as an adhesion molecule through its disintegrin domain, interacting with integrins (particularly α6β1 and α9β1) and extracellular matrix components like fibronectin and gelatin. Dysregulated ADAM9 expression correlates with pathological conditions, notably promoting tumor progression, metastasis, and angiogenesis in various cancers (including breast, prostate, and pancreatic cancer) by facilitating cancer cell invasion and shedding of membrane-bound growth factors, while also implicating roles in inflammatory responses and neurodegenerative diseases such as Alzheimer's disease.