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| Product Name | MMP-3, Recombinant, Human (Stromelysin-1, SL-1, Transin-1) |
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| Description | Purity ≥98% by SDS-PAGE gel and HPLC analyses. Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-3 degrades fibronectin, laminin, collagens III, IV, and X, and cartilage proteoglycans. Recombinant human MMP-3 is a 42.8kD protein containing the entire catalytic N-terminal domain and the C-terminal domain (378 amino acids). Biological Activity: MMP-3 activity was measured by its ability to cleave a chromogenic peptide MMP-3 substrate at room temperature. At a MMP-3 concentration of 2.5ug/ml, 50% cleavage was achieved at an |
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| Size | 2ug, 10ug |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | n/a |
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| Gene, Accession, CAS # | n/a |
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| Catalog # | 143442 |
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| Order / More Info | MMP-3, Recombinant, Human (Stromelysin-1, SL-1, Transin-1) from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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