|Application ||WB, IHC, IP|
|Calculated MW||78458 Da|
|Other Names||MMP9, MMP-9, MMP 9, Matrix metalloproteinase-9, Matrix metalloproteinase 9, Gelatinase B, 92kDa type IV collagenase|
|Formulation||100 µg (0.5 mg/ml) affinity purified rabbit anti-rat MMP-9 polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 50% glycerol, 1% BSA, 0.02% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Precautions||MMP-9 Antibody 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.
The mammalian Matrix metalloproteinases (MMPs) degrade extracellular matrix in physiological and pathological processes. After cleavage of a single peptide domain of about 20 amino acids, the MMPs are secreted in latent forms. Upon activation, the N-terminal propeptide domain is cleaved to generate the active forms of MMP. MMP-9 (92 kDa type IV collagenase, Gelatinase-B) contains the basic structure of propeptide, catalytic, and hemopexin domains. It is an important proteinase in tissue remodeling.
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