MMP9 (Cleaved-Phe107) rabbit pAb - 50 μL

Catalytic activity: Cleavage of gelatin types I and V and collagen types IV and V. Cofactor: Binds 2 zinc ions per subunit. Cofactor: Binds 3 calcium ions per subunit. Disease: Defects in MMP9 may be a cause of susceptibility to lumbar disk herniation (LDH) [MIM: 603932]. LDH is the predominant cause of low-back pain and unilateral leg pain. Domain: 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. enzyme regulation: Inhibited by histatin-3 1/24 (histatin-5). 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. induction: Activated by 4-aminophenylmercuric acetate and phorbol ester. miscellaneous: In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status. PTM: N- and O-glycosylated. PTM: 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. similarity: Belongs to the peptidase M10A family. similarity: Contains 3 fibronectin type-II domains. similarity: Contains 4 hemopexin-like domains. subunit: Exists as monomer, disulfide-linked homodimer, and as a heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form. tissue specificity: Produced by normal alveolar macrophages and granulocytes.