|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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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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