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MMP-2/TIMP-2 proenzyme complex (human fibroblasts)

ALX-200-420-C005 5 µg 172.00 USD
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Product Details

Alternative Name:Matrix metalloproteinase 2/Tissue inhibitor of metalloproteinase 2 Complex
Source:Isolated from human rheumatoid synovial fibroblasts. Requires activation.
EC: (MMP-2)
UniProt ID:P08253 (MMP-2), P16035 (TIMP-2)
Formulation:Liquid. In 50mM TRIS-HCl pH 7.0, 200mM sodium chloride, 5mM CaCl2, 1µM ZnCl2, 0.05% NaN3 and 0.05% BRIJ 35.
Purity:≥95% (SDS-PAGE, Western blot)
Purity Detail:No other MMP contaminants are detectable.
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.
Shipping:Dry Ice
Short Term Storage:-20°C
Long Term Storage:-80°C
Use/Stability:Do always keep the enzyme on ice.
Handling:Avoid freeze/thaw cycles.
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).
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.
Regulatory Status:RUO - Research Use Only

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;

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