>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
52 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: SpectraMax Gemini EM by Molecular Devices) or equivalent
Dilute rhMMP-13 to 100 µg/mL in Assay Buffer.
Add APMA to a final concentration of 1 mM.
Incubate at 37 °C for 2 hours to activate.
Dilute activated rhMMP-13 to 0.2 ng/µL in Assay Buffer.
Dilute Substrate to 20 µM in Assay Buffer.
Load 50 µL of the 0.2 ng/µL rhMMP-13 into a black well plate 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).
rhMMP-13: 0.010 µg
Substrate: 10 µM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human MMP-13 Protein, CF
matrix metallopeptidase 13 (collagenase 3)
matrix metalloproteinase 13 (collagenase 3)
Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-13 (Collagenase-3) has been demonstrated to degrade a range of extracellular matrix proteins, including collagen types I, II, III, IV, IX, X and XIV, gelatin, aggrecan, perlecan and fibronectin. MMP-13 is distinguished from the other human collagenases by its effecient degradation of type II collagen. MMP-13 is expressed by fibroblasts, chrondrocytes and squamous epithelial cells. Structurally, MMP-13 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain.
Jeffery, J.J. (1998) in Collagenase 3. A.J. Barrett, et al. (eds): Handbook of Proteolytic Enzymes, San Diego: Academic Press, p. 1167.
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