>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
28 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Fluorescent Plate Reader (Model: Gemini EM by Molecular Devices) or equivalent
Dilute rmMMP-7 to 100 μg/mL in Assay Buffer.
Activate rmMMP-7 by adding APMA to a final concentration of 1 mM.
Incubate at 37 °C for 1 hour.
Dilute activated rmMMP-7 to 0.4 ng/μL in Assay Buffer.
Dilute Substrate to 20 μM in Assay Buffer.
In a plate, load 50 μL of 0.4 ng/μL rmMMP-7 and start the reaction by adding 50 μL of 20 μM substrate. Include a Substrate Blank containing 50 μL Assay Buffer and 50 μL of 20 μM Substrate.
Read at excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively in kinetic mode for 5 minutes.
Calculate specific activity:
Specific Activity (pmol/min/µg) =
Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)
*Adjusted for Substrate Blank **Derived using calibration standard MCA-Pro-Leu-OH (Bachem, Catalog # M-1975).
rmMMP-7: 0.020 μg
Substrate: 10 μM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse MMP-7 Protein, CF
matrix metallopeptidase 7 (matrilysin, uterine)
matrix metalloproteinase 7 (matrilysin, uterine)
Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-7 (matrilysin) is expressed in epithelial cells of normal and diseased tissues, and is capable of digesting a large series of proteins of the extracellular matrix including collagen IV and X, gelatin, casein, laminin, aggrecan, entactin, elastin and versican (1). MMP-7 is implicated in the activation of other proteinases such as plasminogen, MMP-1, MMP-2, and MMP-9. In addition to its roles in connective tissue remodeling and cancer, MMP-7 also regulates intestinal alpha ‑defensin activation in innate host defense, releases tumor necrosis factor-alpha in a model of herniated disc resorption, and cleaves FasL to generate a soluble form in a model of prostate involution. Structurally, MMP-7 is the smallest of the MMPs and consists of two domains: a pro-domain that is cleaved upon activation and a catalytic domain containing the zinc-binding site.
Woessner, J.F. (2004) in Handbook of Proteolytic Enzymes, Barrett, A.J. et al. eds. p. 532.
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