MMP9 (Cleaved-Met94) rabbit pAb

• Background:

  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.

• Description:

  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.

• Synonyms:

  Matrix metalloproteinase-9 (MMP-9;EC 3.4.24.35;92 kDa gelatinase;92 kDa type IV collagenase;Gelatinase B;GELB) [Cleaved into: 67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9]

• Gene ID:

  4318

• UniProt:

  P14780

• Cellular Locus:

  Secreted, extracellular space, extracellular matrix.

• Host:

  Rabbit

• Species Reactivity:

  Human, Rat, Mouse,

• Reactivity:

  Human; Rat; Mouse

• Immunogen:

  Synthesized peptide derived from human MMP9 (Cleaved-Met94)

• Clonality:

  Polyclonal

• Isotype:

  IgG

• Source:

  Rabbit

• Applications:

  WB, IHC

• Validated Applications:

  WB, IHC

• Stability:

  -20°C/1 year

• Concentration:

  1 mg/mL

• Dilution:

  WB 1:500-2000; IHC-p 1:50-300

• Molecular Weight:

  68 78kD

• Storage Conditions:

  PBS with 0.02% sodium azide and 50% glycerol pH 7.4. Store at -20°C. Avoid repeated freeze-thaw cycles.

• Observed Molecular Weight:

  68 - 78 kD

• Subcellular Location:

  Secreted, extracellular space, extracellular matrix .

• Other Product Names:

  Matrix metalloproteinase-9 (MMP-9; EC 3.4.24.35;92 kDa gelatinase;92 kDa type IV collagenase; Gelatinase B; GELB) [Cleaved into: 67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9]

• Gene ID (Human):

  4318

• SwissProt (Human):

  P14780