General description

Monomeric, native MMP-9 from stimulated human neutrophils. Requires activation prior to use.

Note: 1 mU = 1 milliunit.

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.

Legal Information

Brij is a registered trademark of Croda International PLC

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Other Notes

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.

Packaging

5 µg in Plastic ampoule

Please refer to vial label for lot-specific concentration.

Physical form

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.

Preparation Note

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

Reconstitution

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

Unit Definition

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.

Warning

Toxicity: Standard Handling (A)