|Application ||WB, IF, ICC, E|
|Other Accession||NP_001101, 4557251|
|Calculated MW||85 kDa|
|Application Notes||ADAM10 can be used for detection of ADAM10 by Western blot at 1 - 2 µg/mL. This polyclonal antibody can also detect ADAM10 by immunohistochemistry at 2 µg/mL. For immunofluorescence start at 10 µg/mL.|
|Other Names||ADAM10 Antibody: RAK, kuz, AD10, AD18, MADM, CD156c, HsT18717, KUZ, Disintegrin and metalloproteinase domain-containing protein 10, CDw156, ADAM 10, ADAM metallopeptidase domain 10|
|Reconstitution & Storage||ADAM10 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||ADAM10 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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 (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed:26686862, PubMed:11786905, PubMed:29224781). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146).|
|Cellular Location||Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Note=Is localized in the plasma membrane but is predominantly expressed in the Golgi apparatus and in released membrane vesicles derived likely from the Golgi|
|Tissue Location||Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver.|
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Provided below are standard protocols that you may find useful for product applications.
ADAM10 Antibody: Proinflammatory cytokine tumor necrosis factor-alpha (TNF-α) contributes to a variety of inflammatory responses and programmed cell death. Notch receptor and its ligand participate in cell fate decisions during vertebrate development and are associated with several human disorders, including a T-cell lymphoma. TNF-α, notch and its ligand delta are all membrane-bond molecules, which are cleaved by proteases to release mature proteins or functional receptor. ADAM10, a metalloprotease-disintegrin in the family of mammalian ADAM (for a disintegrin and metalloprotease), was recently identified to cleave TNF-α, notch and its ligand delta. The genes encoding human, mouse, and bovine ADAM10 were recently cloned and designated ADAM 10, kuzbanian (KUZ), and MADM, respectively. ADAM10 mRNA is expressed in a variety of human and bovine tissues.
Rosendahl MS, Ko SC, Long DL, et al. Identification and characterization of a pro-tumor necrosis factor-α-processing enzyme from the ADAM family of zinc metalloproteases. J Biol Chem 1997;272:24588-93
Pan D, Rubin GM. Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 1997;90:271-80
Qi H, Rand MD, Wu X, Sestan N, Wang W, Rakic P, Xu T, Artavanis-Tsakonas S. Processing of the notch ligand delta by the metalloprotease Kuzbanian. Science 1999;283:91-4
Howard L, Lu X, Mitchell S, Griffiths S, Glynn P. Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. Biochem J 1996;317:45-50. (RD1299)
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