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The MMP multipack-2 contains 10µg each of five highly active recombinant MMP catalytic domains: MMP-3, MMP-7, MMP-10, MMP-11, and MMP-12.
The matrix metalloproteinases, or MMPs, are extracellular proteases that function at a neutral pH to cleave a wide variety of substrates. These include basement membrane and extracellular matrix components, growth and death factors, cytokines, and cell and matrix adhesion molecules. The broad range of substrate specificities and expression patterns of MMPs results in their involvement in many different processes, both normal and pathological. Aberrant expression has been noted in cancer, angiogenesis, arthritis, inflammation, periodontal disease, emphysema, multiple sclerosis, pre-eclampsia, and chronic wounds, among others. The general structure of an MMP protein consists of a pre domain to direct secretion from the cell, a pro domain, a catalytic domain, and a C-terminal hemopexin domain. The catalytic site involves a coordinately-bound zinc ion. The inactive, or zymogen, form of the enzyme is activated by disruption of one of the coordinate bonds, usually via proteolytic removal of the pro domain.
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| Regulatory Status |
RUO – Research Use Only |
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Related Products
| Alternative Name | Matrix metalloproteinase 11, Stromelysin-3 |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E. coli. Active Matrix Metalloproteinase-11 (MMP-11, Stromelysin-3) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-11 (Phe98-Ser266, NM_005940) with a C-terminal purification tag. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected. It may be an important link between obesity and cancer. |
| Alternative Name | Matrix metalloproteinase 10, Stromelysin-2 |
|---|---|
| Source | Produced in E. coli. Active Matrix Metalloproteinase-10 (MMP-10, stromelysin-2, transin-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-10 (Phe99-Glu271, NM_2425) with a C-terminal purification tag. This comprises an active form of MMP-10 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected. |
| Alternative Name | Matrix metalloproteinase 3, Stromelysin-1, Transin-1 |
|---|---|
| Purity | ≥95% (SDS-PAGE) |
| Source | Produced in E. coli. Active Matrix Metalloproteinase-3 (MMP-3, stromelysin-1, transin) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-3 (Phe100-Thr272, NM_002422) with a C-terminal purification tag. |