|Application ||WB, IHC-P|
|Reactivity||Human, Guinea Pig|
|Dilution||IHC-P (5 µg/ml), WB (2-4 µg/ml),|
|Other Names||Matrix metalloproteinase-9, MMP-9, 22.214.171.124, 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||Recognizes pro (latent) and activated forms of human MMP-9 at 92kD and ~86kD, respectively. Shows no cross-reaction with pro and active forms of other MMPs.|
|Reconstitution & Storage||Long term: Add glycerol (40-50%) -20°C; Short term: +4°C|
|Precautions||MMP9 / Gelatinase B Antibody (Internal) 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.
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.
Wilhelm S.M.,et al.J. Biol. Chem. 264:17213-17221(1989).
Huhtala P.,et al.J. Biol. Chem. 266:16485-16490(1991).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Deloukas P.,et al.Nature 414:865-871(2001).
Sato H.,et al.Oncogene 8:395-405(1993).
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