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Mouse ADAM9 Protein (His Tag)

AU020942,MDC9,mKIAA0021,Mltng

Catalog Number P50044-M08H
Organism Species Mouse
Host Human Cells
Synonyms AU020942,MDC9,mKIAA0021,Mltng
Molecular Weight The secreted recombinant mouse ADAM9 consists of 679 amino acids and has a calculated molecular mass of 74.9 kDa.
predicted N Gly 30
SDS-PAGE
Purity > 87 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mouse ADAM9 (Q61072) extracellular domain (Met 1-Asp 697) was expressed with a C-terminal polyhistidine tag.
Bio-activity
Research Area Cancer |Invasion microenvironment |Adhesion molecule |Extracelluar matrix |Extracellualr matrix proteases & regulators |A disintegrin and metalloproteinase (ADAM) & ADAMTS |
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background ADAM9 (A disintegrin and metallopeptidase domain 9, MDC9, meltrin gamma), is a type 1 transmembrane protein that has been associated with cancer development and metastases. ADAM9 is consistently overexpressed in various human cancers, and plays a role in tumorigenesis in mouse models. ADAM9 cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as EGF, FGFR2iiib, Tie-2, Flk-1, EphB4, CD40, VCAM-1, and VE-cadherin, and could represent a potential therapeutic target in tumors where it is highly expressed. ADAM9 belongs to a family of transmembrane, disintegrin-containing metalloproteinases involved in protein ectodomain shedding and cell-cell and cell-matrix interactions. ADAM-9 adhesive domain plays a role in regulating the motility of cells by interaction with beta1 integrins and modulates MMP synthesis.
Reference
  • Caltabiano R, et al. (2011) ADAM-9 expression in intestinal-type adenocarcinoma of the sinonasal tract. Appl Immunohistochem Mol Morphol. 19(3): 283-7.
  • Peduto L. (2009) ADAM9 as a potential target molecule in cancer. Curr Pharm Des. 15(20): 2282-7.
  • Zigrino P, et al. (2007) Role of ADAM-9 disintegrin-cysteine-rich domains in human keratinocyte migration. J Biol Chem. 282(42): 30785-93.