|Other Names||Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB, 67 kDa matrix metalloproteinase-9, 82 kDa matrix metalloproteinase-9, MMP9, CLG4B|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6214a was selected from the C-term region of human MMP9 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized 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.|
|Function||May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.|
|Cellular Location||Secreted, extracellular space, extracellular matrix|
|Tissue Location||Produced by normal alveolar macrophages and granulocytes|
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Provided below are standard protocols that you may find useful for product applications.
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP9 degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
Tutton, M.G., et al., Int. J. Cancer 107(4):541-550 (2003).Behrens, P., et al., Int. J. Cancer 107(2):183-188 (2003).Van den Steen, P.E., et al., Biochem. Biophys. Res. Commun. 310(3):889-896 (2003).Zhao, Z., et al., J. Infect. Dis. 188(8):1098-1104 (2003).Matsuyama, A., et al., Circulation 108(12):1469-1473 (2003).
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