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ADAM Metallopeptidase Domain 17 (ADAM17) (Isoform 1) antibody
|Synonyms||CSVP, TACE, ADAM18, CD156B, MGC71942, Tace, CD156b, ADAM17, adam17, si:dkey-81b15.2|
Alternatives Immunohistochemistry (IHC)
|11 references available|
|Price||288.75 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 5 to 7 Business Days|
|Immunogen||Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human ADAM17 (a disintegrin and metalloproteinase domain 17 isoform 1 preproprotein)|
|Description||The ADAM17 (a disintegrin and metalloprotease (ADAM) domain 17) is a member of the ADAM protein family. Members of this family are membraneanchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biologic processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The ADAM17 functions as a tumor necrosis factor-alpha converting enzyme.It binds mitotic arrest deficient 2 protein and also plays a prominent role in the activation of the Notch signaling pathway.|
|Application Notes||ELISA, Western blotting: 1µg/ml for 2hrs.|
|Purification||Purified by antigen-specific affinity chromatography.|
|Buffer||This antibody is stored in PBS, 50% glycerol|
|Preservative||0.01% Sodium Azide|
|Storage||Store at -20°C.|
|Research Area||Cancer, Proteolysis / Ubiquitin, Metalloprotease, Alzheimer's Disease|
|Restrictions||For Research Use only|
Díaz-Rodríguez, Montero, Esparís-Ogando et al.: "Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding." in: Molecular biology of the cell, Vol. 13, Issue 6, pp. 2031-44, 2002 (PubMed).
Peiretti, Deprez-Beauclair, Bonardo et al.: "Identification of SAP97 as an intracellular binding partner of TACE." in: Journal of cell science, Vol. 116, Issue Pt 10, pp. 1949-57, 2003 (PubMed).
Gschwind, Hart, Fischer et al.: "TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells." in: The EMBO journal, Vol. 22, Issue 10, pp. 2411-21, 2003 (PubMed).
Shao, Ueki, Nadel: "Tumor necrosis factor alpha-converting enzyme mediates MUC5AC mucin expression in cultured human airway epithelial cells." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 100, Issue 20, pp. 11618-23, 2003 (PubMed).
Valeva, Walev, Weis et al.: "A cellular metalloproteinase activates Vibrio cholerae pro-cytolysin." in: The Journal of biological chemistry, Vol. 279, Issue 24, pp. 25143-8, 2004 (PubMed).
Solomon, Rosenblum, Gonzales et al.: "Pronounced diversity in electronic and chemical properties between the catalytic zinc sites of tumor necrosis factor-alpha-converting enzyme and matrix metalloproteinases despite their high structural similarity." in: The Journal of biological chemistry, Vol. 279, Issue 30, pp. 31646-54, 2004 (PubMed).
Allinson, Parkin, Condon et al.: "The role of ADAM10 and ADAM17 in the ectodomain shedding of angiotensin converting enzyme and the amyloid precursor protein." in: European journal of biochemistry / FEBS, Vol. 271, Issue 12, pp. 2539-47, 2004 (PubMed).
Lee, Rapti, Murphy: "Delineating the molecular basis of the inactivity of tissue inhibitor of metalloproteinase-2 against tumor necrosis factor-alpha-converting enzyme." in: The Journal of biological chemistry, Vol. 279, Issue 43, pp. 45121-9, 2004 (PubMed).
Schäfer, Marg, Gschwind et al.: "Distinct ADAM metalloproteinases regulate G protein-coupled receptor-induced cell proliferation and survival." in: The Journal of biological chemistry, Vol. 279, Issue 46, pp. 47929-38, 2004 (PubMed).
Shao, Nadel: "Dual oxidase 1-dependent MUC5AC mucin expression in cultured human airway epithelial cells." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, Issue 3, pp. 767-72, 2005 (PubMed).
Rabie, Strehl, Ludwig et al.: "Evidence for a role of ADAM17 (TACE) in the regulation of platelet glycoprotein V." in: The Journal of biological chemistry, Vol. 280, Issue 15, pp. 14462-8, 2005 (PubMed).