|Application ||WB, E|
|Calculated MW||78458 Da|
|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||Purified His-tagged MMP9 protein(Fragment) was used to produced this monoclonal antibody.|
|Format||Mouse monoclonal antibody supplied in crude ascites with 0.09% (W/V) sodium azide.|
|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||MMP9 Antibody (Ascites) is for research use only and 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 MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene 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. [provided by RefSeq].
Lacchini, R., et al. Clin. Chim. Acta 411 (23-24), 1940-1944 (2010) :
Chambers, M.A., et al. Biochem. Biophys. Res. Commun. 400(3):403-408(2010)
Beeghly-Fadiel, A., et al. Breast Cancer Res. Treat. (2010) In press :
Szczudlik, P., et al. Neurol. Neurochir. Pol. 44(4):350-357(2010)
Mossbock, G., et al. Mol. Vis. 16, 1764-1770 (2010) :
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