|Application ||WB, IHC-P, FC, E|
|Calculated MW||90556 Da|
|Antigen Region||704-733 aa|
|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||This ADAM9 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 704-733 amino acids from the C-terminal region of human ADAM9.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||ADAM9 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||KIAA0021, MCMP, MDC9, MLTNG|
|Function||Probable zinc protease. May mediate cell-cell or cell- matrix interactions. Isoform 2 displays alpha-secretase activity for APP.|
|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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