Anti-ADAM10/ADAM10 Antibody Picoband® Fluoro594 Conjugated

ADAM10, A Disintegrin and Metalloproteinase Domain 10, is also know as AD10. ADAM10 is a member of the ADAM family and members of this family are cell surface proteins with a unique structure possessing both potential adhesion and protease function. The ADAM10 gene is mapped to chromosome 15q21.3-q23. ADAM proteins contain an N-terminal signal sequence, followed by a prodomain, a metalloprotease-like domain, a disintegrin-like domain, a cysteine-rich region, an EGF -like repeat, a transmembrane domain, and a C-terminal cytoplasmic tail. Conversion of the membrane-bound precursor to a secreted mature protein is mediated by a protease termed TNFA convertase. ADAM10 possesses TNFA convertase activity.

Disintegrin and metalloproteinase domain-containing protein 10; ADAM 10;3.4.24.81; CDw156; Kuzbanian protein homolog; Mammalian disintegrin-metalloprotease; CD156c; ADAM10; KUZ, MADM

Apoptosis, Cancer, Cell Biology, Cell Death, Cytoskeleton/ECM, ECM Enzymes, Extracellular Matrix, Invasion/Microenvironment, Metalloprotease, Proteolysis/Ubiquitin, Proteolytic Enzymes, Receptors, Signal Transduction

Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth- like factor, ephrin-A2 and for constitutive and regulated alpha- secretase cleavage of amyloid precursor protein (APP) . Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. May regulate the EFNA5-EPHA3 signaling. .

1. Wolfsberg, T. G., Primakoff, P., Myles, D. G., White, J. M.ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions.J. Cell Biol. 131: 275-278, 1995. 2. Yamazaki, K., Mizui, Y., Tanaka, I.Radiation hybrid mapping of human ADAM10 gene to chromosome 15.Genomics 45: 457-459, 1997. 3. Lunn, C. A., Fan, X., Dalie, B., Miller, K., Zavodny, P. J., Narula, S. K., Lundell, D.Purification of ADAM 10 from bovine spleen as a TNFalpha convertase.FEBS Lett. 400: 333-335, 1997.

Cell membrane; Single-pass type I membrane protein. Endomembrane system; Single-pass type I membrane protein. Is localized in the plasma membrane but is predominantly expressed in the Golgi apparatus and in released membrane vesicles derived likely from the Golgi.