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MMP-9 proenzyme (human neutrophils), monomer

ALX-200-422-C005 5 µg 198.00 USD
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Product Details

Alternative Name:Matrix metalloproteinase 9, Gelatinase B, 92kDa Type IV collagenase
Source:Isolated from stimulated human neutrophil granulocytes (buffy coat). Requires activation.
UniProt ID:P14780
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.
Purity:≥95% (SDS-PAGE, Western blot): no other MMP contaminants are detectable
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.
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Use/Stability:Stable for 1 week when stored at +4°C and for several weeks when stored at -20°C.
Handling:Avoid freeze/thaw cycles.
Scientific Background:MMP-9 hydrolyzes the extracellular matrix, e.g. collagen types IV, V and IX and gelatin.
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.
Regulatory Status:RUO - Research Use Only

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;

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