MMP9 Antibody - #BF0560
*The optimal dilutions should be determined by the end user.
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# BF0560, RRID:AB_2833940.
82 kDa matrix metalloproteinase-9; 92 kDa gelatinase; 92 kDa type IV collagenase; CLG 4B; CLG4B; Collagenase Type 4 beta; Collagenase type IV 92 KD; EC 126.96.36.199; Gelatinase 92 KD; Gelatinase B; Gelatinase beta; GelatinaseB; GELB; Macrophage gelatinase; MANDP2; Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); Matrix Metalloproteinase 9; MMP 9; MMP-9; MMP9; MMP9_HUMAN; Type V collagenase;
Purified recombinant fragment of human MMP9 expressed in E. Coli.
Detected in neutrophils (at protein level) (PubMed:7683678). Produced by normal alveolar macrophages and granulocytes.
PTMs - P14780 As Substrate
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.
Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.
N- and O-glycosylated.
Secreted>Extracellular space>Extracellular matrix.
Detected in neutrophils (at protein level). Produced by normal alveolar macrophages and granulocytes.
Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with LCN2. Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1.
(Microbial infection) Interacts with Staphylococcus aureus protein SSL5; this interaction inhibits MMP9 activity.
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Belongs to the peptidase M10A family.
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