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ADAM Metallopeptidase Domain 9 (ADAM9) (N-Term) Peptide

Name

ADAM Metallopeptidase Domain 9 (ADAM9)

Synonyms adam9-A, MDC9, ADAM-9, Adam9, zgc:101824, ADAM9, LOC100101585, MCMP, Mltng, KIAA0021, AU020942, mKIAA0021
Binding Site

N-Term

3 references available
Certificates ISO 9001:2008
Catalog no. ABIN697050
Quantity 0.1 mg
Price 49.50 $   Plus shipping costs $45.00
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Additional Information

Immunogen Synthetic peptide
Characteristics Blocking peptide for ADAM9 (N-term) antibody ABIN391640
Specificity The synthetic peptide sequence used to generate the antibody AP7437a was selected from the N-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.
Comments

Background: 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.

Application Details

Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles
Restrictions For Research Use only

Publications

Product Weskamp, Krätzschmar, Reid et al.: "MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains." in: The Journal of cell biology, Vol. 132, Issue 4, pp. 717-26, 1996 (PubMed).

McKie, Edwards, Dallas et al.: "Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes." in: Biochemical and biophysical research communications, Vol. 230, Issue 2, pp. 335-9, 1997 (PubMed).

Hotoda, Koike, Sasagawa et al.: "A secreted form of human ADAM9 has an alpha-secretase activity for APP." in: Biochemical and biophysical research communications, Vol. 293, Issue 2, pp. 800-5, 2002 (PubMed).