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| Product Name | Matrix Metalloproteinase-3, Recombinant, Human (MMP-3, Stromelysin-1, Transin-1) |
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| Description | Purity ~98% (RP-HPLC, SDS-PAGE). MMP-3 enzyme is also known as Stromelysin-1 or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk. MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and super activates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta. Source: Recombinant protein corresponding to a single, non-glycosylated, polypeptide chain containing 230aa from human MMP-3, expressed in E. coli. Molecular Weight: ~22kD Specific Activity: ~1250mU/mg protein (H. Nagase, et al; J. Biol. Chem. 269, 20952, 1994). |
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| Size | 5ug |
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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 # | 209087 |
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| Order / More Info | Matrix Metalloproteinase-3, Recombinant, Human (MMP-3, Stromelysin-1, Transin-1) from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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