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order histories, retained contact details for faster checkout, review submissions, and special promotions.
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.
ADAM10 (A disintegrin and metalloproteinase domain-containing protein 10, CD156c) is a cell surface protein that is responsible for the proteolytic release of other cell-surface proteins on endothelial cells, including soluble JAM3, heparin-binding epidermal growth-like factor, TNF-alpha, E-cadherin and ephrin-A2. It is further responsible for the constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) and contributes to the normal cleavage of the cellular prion protein. It also has vesicle-based protease activity. ADAM10 also regulates the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Increased expression of this protein in hippocampal neuronal synapses is found in the brains of Alzheimer’s disease patients. In breast cancer, inhibitors that target ADAM10 used in conjunction with Herceptin may be an effective therapy for some HER2-upregulated patients. In immunohistochemistry, ADAM10 has membranous and cytoplasmic staining in a variety of tissues including the brain, thyroid, gastrointestinal tract, liver, kidney, reproductive tissues, skin and immune tissues.
References: Cold Spring Harbor Perspectives in Medicine. 2 (5): a006270, PMID: 22553493; Cancer Biology & Therapy. 5 (6): 657–64, PMID: 16627989; PLoS One. 2016 May 25;11(5):e0156184, PMID: 27224017;