Monomeric, native MMP-9 from stimulated human neutrophils. Matrix metalloproteinases (MMP) are members of a family of at least 20 zinc-dependent endoproteinases that function extracellularly at neutral pH. The enzymes are synthesized as latent or inactive zymogens that contain a regulatory propeptide. This propeptide confers latency by binding …
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Monomeric, native MMP-9 from stimulated human neutrophils. Matrix metalloproteinases (MMP) are members of a family of at least 20 zinc-dependent endoproteinases that function extracellularly at neutral pH. The enzymes are synthesized as latent or inactive zymogens that contain a regulatory propeptide. This propeptide confers latency by binding to the Zn²⁺ molecule present in the active site. MMP activation can be achieved through autoactivation, via cleavage by other MMPs or proteases, such as furin, urokinase, plasmin, and trypsin, or by treatment with organomercurial comounds. This preparation is highly purified native MMP-9 from stimulated human neutrophils. Requires activation prior to use. In 200 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, 1 µM ZnCl₂, 0.05% Brij® 35 Detergent, 0.05% NaN₃, pH 7.0. Reynolds, M. A., et al. 2003. Clin. Chem.49, 1733.
Kolkenbrock, H., et al. 1996. Biol. Chem. 377, 529.
Marcy, A.I., et al. 1991. Biochemistry30, 6476.
Stricklin, et al. 1983. Biochemistry22, 61. Prepared from stimulated neutrophils that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV. Following initial thaw, aliquot and freeze (-70°C). Toxicity: Standard Handling (A) One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol 2,4-DNP-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min at 37°C, pH 7.0.
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