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| Product Name | Matrix Metalloproteinase 9 Pro Monomer (MMP-9, Collagenase 4, Gelatinase B) |
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| Description | Purity > 95% of total protein. MMP-9 monomer appears as a major band at 92kD in non-reducing SDS-PAGE. Human MMP-9 consists of 668aa with a calculated Mrof 76,240D. Due to N- and O-linked glycosylated the Mr in SDS-PAGE is about 92kD. Within the protein sequence, the following structural domains can be distinguished: An N-terminal propeptide, which confers latency to the proenzyme, a Ca2+ and Zn2+ ion-binding catalytic domain containing an insertion of three repeats homologous to type II repeats in the gelatin-binding region of fibronectin, and a C-terminal hemopexin-like domain. Catalytic and hemopexin domains are connected by a proline-rich sequence with homology to sequences in collagens. The gelatin-binding region and the hemopexin domain confer specific macromolecular substrate binding to MMP-9. The hemopexin domain of the latent enzyme binds TIMP-1. Activation of latent MMP-9 can be mediated by proteases like stromelysin, cathepsin G, kallikrein and trypsin or by incubation with |
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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 # | Accession: NM_004994.2, SwissProt: P14780 |
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| Catalog # | M2425-40 |
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| Order / More Info | Matrix Metalloproteinase 9 Pro Monomer (MMP-9, Collagenase 4, Gelatinase B) from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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