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| Product Name | Matrix Metalloproteinase 8, Human |
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| Description | Purity ~90% (SDS-PAGE). The progelatinase A, a member of the matrix metalloproteinase (MMP) family, has been isolated from macrophages and fibroblasts. Gelatinase A hydrolyses several components of the extracellular matrix, e.g. the collagen types IV, V and XI and gelatin. Progelatinase A complexed via their C-terminal domain with TIMP-2 was isolated from culture media of different cell types. This complex shows both properties of its constituents: Like TIMP-2 it inhibits active matrix metalloproteinases and like gelatinase it shows proteolytic activity after activation with APMA (4-aminophenylmercury acetate). However, its proteolytic activity is less than 10% of that of gelatinase A not complexed with TIMP-2. In contrast to the other MMPs the progelatinase A cannot be activated by the serine proteinase trypsin. Until quite recently a potential natural activator that can transform latent progelatinase A into the active form was unknown. It was shown that the catalytic domain of the me |
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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 | Matrix Metalloproteinase 8, Human (MMP8, MMP-8, CLG1, HNC, Neutrophil Collagenase, PMNL Collagenase, PMNL-CL) |
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| Gene, Accession, CAS # | SwissProt: P22894 |
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| Catalog # | M2424-08C |
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| Order / More Info | Matrix Metalloproteinase 8, Human from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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