>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.
31 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.
29 kDa, reducing conditions
Read Publication using 1785-MP in the following applications:
Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
Dilute rhMMP-16 to 80 µg/mL in Activation Buffer.
Dilute rhFurin to 1.76 µg/mL in Activation Buffer.
Mix equal volumes of 80 µg/mL of rhMMP-16 and 1.76 µg/mL of rhFurin together.
Incubate at 37 °C for 1 hour to activate rhMMP-16.
After incubation, dilute activated rhMMP-16 to 2 ng/µL in Assay Buffer.
Dilute Substrate to 20 µM in Assay Buffer.
In plate, load 50 µL of 2 ng/µL rhMMP-16, and start the reaction by adding 50 µL of 20 µM Substrate to wells. As a Substrate Blank, load 50 µL of Assay Buffer and 50 µL of 20 µM Substrate.
Read at excitation and emission wavelengths of 320 nm and 405 nm, 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-16: 0.1 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-16/MT3-MMP Protein, CF
chromosome 8 open reading frame 57
matrix metallopeptidase 16 (membrane-inserted)
matrix metalloproteinase 16 (membrane-inserted)
Membrane-type matrix metalloproteinase 3
Membrane-type-3 matrix metalloproteinase
Putative transmembrane protein C8orf57
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 (ECM). MMP‑16 (MT3-MMP) is found in brain, lung, placenta, smooth muscle cells, and malignant tumor tissues including oral melanoma and renal carcinoma (1). MMP‑16 has been shown to activate proMMP-2 and degrade various ECM components including native collagens (2, 3). MMP‑16 has been proposed to possess the potential to directly enhance the growth and invasiveness of cells in vivo, two critical processes for development and carcinogenesis (4). Structurally, MMP‑16 consists of the following domains: a pro domain containing the furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplamasic tail (1). The structure of the catalytic domain in complex with a hydroxamate inhibitor has been solved (5). The recombinant human MMP‑16PC consists of the pro and catalytic domains, which can be activated by treatment with furin.
Takino, T. et al. (1995) J. Biol. Chem. 270:23013.
Shofuda, K. et al. (1997) J. Biol. Chem. 272:9749.
Shimada, T. et al. (1999) Eur. J. Biochem. 262:907.
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