Recombinant Human MMP9 protein (Catalytic domain) (ab82907)

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.

Produced by normal alveolar macrophages and granulocytes.

Intervertebral disc disease
Metaphyseal anadysplasia 2

Belongs to the peptidase M10A family.
Contains 3 fibronectin type-II domains.
Contains 4 hemopexin repeats.

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.

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.