Product Details
| Alternative Name: | Matrix metalloproteinase 2/Tissue inhibitor of metalloproteinase 2 Complex |
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| Source: | Isolated from human rheumatoid synovial fibroblasts. Requires activation. |
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| EC: | 3.4.24.24 (MMP-2) |
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| UniProt ID: | P08253 (MMP-2), P16035 (TIMP-2) |
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| Concentration: | ~50µg/ml |
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| Formulation: | Liquid. In 50mM TRIS-HCl pH 7.0, 200mM sodium chloride, 5mM CaCl2, 1µM ZnCl2, 0.05% NaN3 and 0.05% BRIJ 35. |
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| Purity: | ≥95% (SDS-PAGE, Western blot) |
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| Purity Detail: | No other MMP contaminants are detectable. |
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| Specific Activity: | ≥30mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol Dnp-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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| Short Term Storage: | -20°C |
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| Long Term Storage: | -80°C |
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| Use/Stability: | Do always keep the enzyme on ice. |
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| Handling: | Avoid freeze/thaw cycles. |
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| Scientific Background: | MMP-2 and TIMP-2 form a stable, but non-covalent 1:1 stoichiometric complex. The complex inhibits active matrix MMP's like collagenases and gelatinases and shows proteolytic activity after activation with APMA (4-aminophenylmercury acetate). |
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| Technical Info/Product Notes: | Precursor enzyme needs activation using 2mM AMPA (aminophenylmercuric acetate) or 1mM mersalylic acid for 60-120 min. at 37°C. Do not use trypsin for activation! Do not dilute the enzyme for activation! 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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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Cellular uptake of proMMP-2:TIMP-2 complexes by the endocytic receptor megalin/LRP-2: M. Johanns, et al.; Sci. Rep.
7, 4328 (2017),
Application(s): Surface plasmon resonance analysis & Radioligand binding assay,
Abstract;
Full Text
Activation of progelatinase A and progelatinase A/TIMP-2 complex by membrane type 2-matrix metalloproteinase: H. Kolkenbrock, et al.; Biol. Chem.
378, 71 (1997),
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;
The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor: H. Kolkenbrock, et al.; Eur. J. Biochem.
198, 775 (1991),
Abstract;
Synthetic substrates for vertebrate collagenase: Y. Masui, et al.; Biochem. Med.
17, 215 (1977),
Abstract;
