MMP-9, Monomer, Human Neutrophil

Toxicity: Standard Handling (A)

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.

Note: 1 mU = 1 milliunit.

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.

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.

Please refer to vial label for lot-specific concentration.

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.

Following initial thaw, aliquot and freeze (-70°C).

Prepared from stimulated neutrophils that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

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