ADAM10 Antibody #14194

Members of the ADAM (a disintegrin and a metalloprotease) family of multidomain membrane proteins influence cell signaling and adhesion by shedding cell surface proteins, such as cytokines and growth factors. This process influences cell-extracellular matrix (ECM) adhesion and ECM remodeling. Conserved domains found in most ADAM family proteins include a prodomain, a zinc-dependent metalloprotease domain, a disintegrin domain, a carboxy-terminal cysteine-rich domain, an EGF-like sequence, and a short cytoplasmic tail (1,2).
The ADAM metallopeptidase domain 10 (ADAM10) is a plasma membrane proteinase that cleaves membrane-bound proteins targeted for regulated intramembrane proteolysis (RIP). The ADAM10 prodomain acts as a chaperone that stabilizes mature ADAM protein folding, and prevents target-protein shedding through inhibition of ADAM10 proteinase activity (3,4). Mature ADAM10 is the major α-secretase responsible for cleavage of Notch, APP, cadherins, and prion protein (5-7). The ADAM10 protein cleaves receptor tyrosine kinases and their associated ligands and displays a wide range of regulatory functions across related signaling pathways (8). Research studies using knockout mice demonstrate that loss of ADAM10 results in defects in cortex formation, lymphocyte development, and cardiovascular development (9-11). Increased ADAM10 protein expression correlates with progression of many types of cancer (i.e. gastric cancer, hepatocellular carcinoma, and brain glioma), due to increased cancer cell migration, metastasis, and invasion (12-14). Mutations in the corresponding ADAM10 gene result in a rare, autosomal dominant pigmentation disorder known as reticulate acropigmentation of Kitamura (15).