Product Specification
| Alternative Name: | Matrix metalloproteinase 9, Gelatinase B, 92kDa Type IV collagenase |
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| MW: | ~92kDa. |
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| Source: | Isolated from stimulated human neutrophil granulocytes (buffy coat). Requires activation. |
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| EC: | 3.4.24.35 |
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| UniProt ID: | P14780 |
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| Concentration: | ~100µg/ml |
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| Formulation: | Liquid. In 50mM TRIS-HCl, pH 7.0, containing 200mM sodium chloride, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ 35 and 0.05% sodium azide. |
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| Purity: | ≥95% (SDS-PAGE, Western blot): no other MMP contaminants are detectable |
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| Specific Activity: | ≥1’400mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol 2,4-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0. |
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| Shipping: | Shipped on Dry Ice |
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| Long Term Storage: | -80°C |
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| Use/Stability: | Stable for 1 week when stored at +4°C and for several weeks when stored at -20°C. |
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| Handling: | Avoid freeze/thaw cycles. |
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| Scientific Background: | MMP-9 hydrolyzes the extracellular matrix, e.g. collagen types IV, V and IX and gelatin. |
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| Technical Info/Product Notes: | Precursor enzyme needs activation using 2mM AMPA (aminophenylmercuric acetate) for 60-120 min. or 100µg/ml TPCK-trypsin for 30 min. at 37°C. If required trypsin can be inhibited by incubation with 10 µl of 1mg/ml aprotinin solution for 10 min. at 25°C. If working with MMP-9/TIMP-1 complexes, it is recommended to use stromelysin-1 (MMP-3) for activation. Incubation at 37°C for 2 hours at 40:1 (MMP-9:stromelysin-1) will remove only the propeptide to give the active form of the enzyme. The active enzyme is inhibited by TIMP-1 (tissue inhibitor of matrix metalloproteinase-1) and by chelators of divalent cations like EDTA or o-phenantroline. |
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Product Literature References
Matrix Metalloproteinase (MMP) Proteolysis of the Extracellular Loop of Voltage-gated Sodium Channels and Potential Alterations in Pain Signaling: A.G. Remacle, et al.; J. Biol. Chem.
290, 22939 (2015),
Abstract;
Full Text
Progelatinase B forms from human neutrophils. complex formation of monomer/lipocalin with TIMP-1: H. Kolkenbrock, et al.; Biol. Chem.
377, 529 (1996),
Abstract;
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases: C.G. Knight, et al.; FEBS Lett.
296, 263 (1992),
Abstract;
Synthetic substrates for vertebrate collagenase: Y. Masui, et al.; Biochem. Med.
17, 215 (1977),
Abstract;
