| BML-AK014-0001 | 1 Kit | 870.00 USD |  |
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| Applications: | FUNC, HTS |
| Application Notes: | Enzyme regulation and kinetics, comparative studies of substrate or inhibitor specificities, cleavage of target proteins. Assay or digest conditions can vary widely, but concentrations for the MMP enzymes can range between 10 and 300nM, or higher. Reaction temperatures can be between 25 and 37°C, and reaction times can range from 10 min to overnight, again depending on application and substrate. A typical assay buffer is 50mM HEPES, pH 7.0, 10mM CaCl2, 0.05% Brij-35. For more information, contact Enzo Life Sciences Technical Support. |
| Contents: |
Contains 10µg of each enzyme, provided in a screw-cap microfuge tube. MMP-7 (catalytic domain) (human), (recombinant) (Prod. No. BML-SE181), MMP-10 (catalytic domain) (human), (recombinant) (Prod. No. BML-SE329), MMP-11 (catalytic domain) (human), (recombinant) (Prod. No. BML-SE282), MMP-12 (catalytic domain) (human), (recombinant) (Prod. No. BML-SE138). |
| Formulation: | Liquid. Each enzyme is supplied in 50mM TRIS, pH 7.5, containing 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 30% glycerol, 0.5% Brij-35. |
| Concentration: | Please refer to Certificate of Analysis for individual lot numbers of component(s). |
| Handling: | Avoid freeze/thaw cycles. |
| Shipping: | Dry Ice |
| Long Term Storage: | -80°C |
| Scientific Background: | 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. |
| Technical Info/Product Notes: | Note: MMP-3 is unique in that its pH optimum is 6.0. Activity of this enzyme in pH 7.0 buffers is significantly reduced. Note: Human (but not mouse) MMP-11 has very unique substrate preferences, and only poorly cleaves typical MMP substrates. Use much higher substrate concentrations and longer incubation times. |
| Regulatory Status: | RUO - Research Use Only |
Matrix metalloproteinase (MMP) multipack-1 |
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| FUNC, HTS | Print as PDF | ||||||
| BML-AK013-0001 | 1 Kit | 899.00 USD | |
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MMP-3 (catalytic domain) (human), (recombinant) |
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| 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., ≥95% (SDS-PAGE) | Print as PDF | ||||||
| BML-SE109-0010 | 10 µg | 506.00 USD | |
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MMP-7 (catalytic domain) (human), (recombinant) |
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| Produced in E. coli. Active Matrix Metalloproteinase-7 (MMP-7, matrilysin, pump) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-7 (Tyr95-Lys267, NM_002423) with a C-terminal purification tag., ≥95% (SDS-PAGE) | Print as PDF | ||||||
| BML-SE181-0010 | 10 µg | 506.00 USD | |
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MMP-10 (catalytic domain) (human), (recombinant) |
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| 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. | Print as PDF | ||||||
| BML-SE329-0010 | 10 µg | 506.00 USD | |
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MMP-11 (catalytic domain) (human), (recombinant) |
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| 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., ≥95% (SDS-PAGE) | Print as PDF | ||||||
| BML-SE282-0010 | 10 µg | 419.00 USD | |
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MMP-12 (catalytic domain) (human), (recombinant) |
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| Produced in E. coli. Active Matrix Metalloproteinase-12 (MMP-12, metalloelastase, macrophage elastase; often confused with neutrophil elastase) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-12 (Phe99-Leu271, NM_002426) with a C-terminal purification tag., ≥95% (SDS-PAGE) | Print as PDF | ||||||
| BML-SE138-0010 | 10 µg | 488.00 USD | |
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