|Other Names||Disintegrin and metalloproteinase domain-containing protein 9, ADAM 9, 3424-, Cellular disintegrin-related protein, Meltrin-gamma, Metalloprotease/disintegrin/cysteine-rich protein 9, Myeloma cell metalloproteinase, ADAM9, KIAA0021, MCMP, MDC9, MLTNG|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7437b was selected from the C-term region of human ADAM9. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||KIAA0021, MCMP, MDC9, MLTNG|
|Function||Cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5. May mediate cell-cell, cell- matrix interactions and regulate the motility of cells via interactions with integrins.|
|Cellular Location||Isoform 1: Cell membrane; Single-pass type I membrane protein|
|Tissue Location||Widely expressed. Expressed in chondrocytes. Isoform 2 is highly expressed in liver and heart|
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Provided below are standard protocols that you may find useful for product applications.
ADAM9 is a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. This protein interacts with SH3 domain-containing proteins, binds mitotic arrest deficient 2 beta protein, and is also involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor.
Weskamp G., Kraetzschmar J., Reid M.S.J. Cell Biol. 132:717-726(1996)Hotoda N., Koike H.Biochem. Biophys. Res. Commun. 293:800-805(2002)McKie N., Edwards T., Dallas D.J.Biochem. Biophys. Res. Commun. 230:335-339(1997)
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