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| Product Name | Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain |
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| Description | Appears as a predominant band at 58kD in SDS-PAGE (> 80% total protein). Matrix metalloproteinases (MMPs) are Zn2+-and Ca2+-dependent endopeptidases which function in the turnover of extracellular matrix components (1). Presently, eighteen secreted MMPs and five membrane-type MMPs (2-5) are known to be expressed in vertebrates. Human MT1-MMP consists of 559 amino acid residues with a calculated Mr of 63516 (2,3). The following domains and sequence regions are distinguished in MT1-MMP: Prodomain (Ser1-Arg88), catalytic domain (Tyr89-Gly261), junction between catalytic domain and hemopexin domain (Gly262-Gly292), hemopexin-like domain (Pro293-Cys485) and C-terminal sequence (Pro486-Val559) with transmembrane segment. When expressed in cells, the catalytic domain and the hemopexin domain of MT1-MMP become exposed on cell surfaces (2,6). A soluble form of MT1-MMP without transmembrane segment has been found in culture medium of a breast carcinoma cell line (7). MT1-MMP is expressed in adul |
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| Size | 5ug |
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| Concentration | n/a |
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| Applications | ELISA |
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| Other Names | Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain (MT1-MMP, MMP-14, Collagenase-3) Recombinant |
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| Gene, Accession, CAS # | Accession: NM_004995.2, SwissProt: P50281 |
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| Catalog # | M2429-06 |
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| Order / More Info | Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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