Recombinant Human ADAM8

Background

ADAM metallopeptidase domain 8 (ADAM8), also known as CD156a, is a member of the ADAM family of proteins, which are zinc-dependent transmembrane proteins involved in various biological processes such as cell adhesion, migration, proteolysis, and signaling. ADAM8 is primarily known for its role in inflammation, immune response, and cancer progression. ADAM8 consists of 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 ADAM8 to participate in cell-cell and cell-matrix interactions and to proteolytically process various substrates.ADAM8 is expressed in various tissues and cell types, including leukocytes (white blood cells), lung epithelial cells, and certain cancer cells. Its expression is often upregulated in response to inflammatory stimuli, suggesting a role in immune responses.ADAM8 is implicated in the regulation of inflammation and immune responses. It has been shown to modulate leukocyte migration, cytokine production, and antigen presentation.ADAM8 can mediate cell adhesion to extracellular matrix components such as fibronectin and collagen. It also plays a role in cell migration by cleaving cell surface proteins involved in cell adhesion and signaling.ADAM8 possesses metalloprotease activity and can cleave various substrates, including cytokines, cell surface receptors, and extracellular matrix proteins. This proteolytic activity can influence cell behavior and tissue remodeling.ADAM8 has been linked to inflammatory diseases such as asthma, rheumatoid arthritis, and multiple sclerosis. It contributes to the pathogenesis of these conditions by modulating immune cell function and inflammation. ADAM8 is also overexpressed in several cancers, including breast cancer, lung cancer, and glioblastoma. Its upregulation is associated with tumor progression, invasion, metastasis, and angiogenesis. ADAM8's proteolytic activity can facilitate cancer cell migration and invasion by cleaving extracellular matrix components and cell adhesion molecules.