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Matrix metalloproteinase-12 (MMP12) is a macrophage-secreted elastase that is highly induced in the liver and lung in response to S. mansoni eggs and contains four hemopexin-like domains. MMP12 is a proteolytic enzyme responsible for the cleavage of plasminogen to angiotensin, which has an angiostatic effect. MMP12 promotes fibrosis by limiting the expression of specific ECM-degrading MMPs. MMP12 is a potent proinflammatory and oncogenic molecule. MMP12 up-regulation plays a critical role in emphysema to lung cancer transition that is facilitated by inflammation.
The recombinant human MMP12 consists of 164 amino acids and predicts a molecular mass of 18.2 KDa. A DNA sequence encoding human MMP12 (Gly106-Asn268) was expressed.
Measured by its ability to cleave the fluorogenic peptide substrate (Mca-PLGL-Dpa-AR-NH2), the specific activity is > 800 pmoles/min/µg.
Endotoxin < 1 EU/µg
Apparent Molecular Weight: 18 KDa, reducing conditions
Lyophilized from sterile 10 mM Hepes, 2 mM CaCl2, 250 mM NaCl, pH 7.0.
| Form | Lyophilized powder |
| Storage | Stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days and at -20°C for 3 months. |
[4] Jinzhi Li, et al. BMC Cancer. Elastin is a key factor of tumor development in colorectal cancer
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