Recombinant Human MMP-14/MT1-MMP Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Enzyme Activity

Order Details

Recombinant Human MMP-14/MT1-MMP Protein, CF Summary

Details of Functionality
Measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2 (Catalog # ES010). The specific activity is >450 pmol/min/µg, as measured under the described conditions.
E. coli-derived human MMP-14/MT1-MMP protein
Ala21-Gly284, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Structure / Form
Pro and catalytic domains
Protein/Peptide Type
Recombinant Enzymes
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.


  • Enzyme Activity
Theoretical MW
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.
31 kDa, reducing conditions
Read Publications using
918-MP in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Supplied as a 0.2 μm filtered solution in Tris, NaCl, CaCl2 and Glycerol.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Assay Procedure
  • Activation Buffer: 50 mM Tris, 1 mM CaCl2, 0.5% (w/v) Brij-35, pH 9.0
  • Assay Buffer: 50 mM Tris, 3 mM CaCl2, 1 µM ZnCl2, pH 8.5
  • Recombinant Human MMP‑14/MT1‑MMP (rhMMP-14) (Catalog # 918-MP)
  • Recombinant Human Furin (rhFurin) (Catalog # 1503-SE)
  • Substrate: MCA-Lys-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 (Catalog # ES010) 2 mM stock in DMSO
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Activate rhMMP-14 at 80 µg/mL with 1.72 µg/mL rhFurin in Activation Buffer.
  2. Incubate at 37 °C for 1.5 hours.
  3. Dilute activated rhMMP-14 to 1 ng/µL in Assay Buffer.
  4. Dilute Substrate to 80 µM in Assay Buffer.
  5. In a plate load 50 µL of 1 ng/µL rhMMP-14 to wells, and for a Substrate Blank load 50 µL of Assay Buffer.
  6. Start the reaction by adding 50 µL of 80 µM Substrate to wells.
  7. Read at excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively in kinetic mode for 5 minutes.
  8. 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).

Per Well:
  • rhMMP-14: 0.050 µg
  • Substrate: 40 µM
  • Notes

    This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

    Alternate Names for Recombinant Human MMP-14/MT1-MMP Protein, CF

    • EC 3.4.24
    • EC
    • matrix metallopeptidase 14 (membrane-inserted)
    • matrix metalloproteinase 14 (membrane-inserted)
    • matrix metalloproteinase-14
    • membrane type 1 metalloprotease
    • Membrane-type matrix metalloproteinase 1
    • Membrane-type-1 matrix metalloproteinase
    • MMP14
    • MMP-14
    • MMP-X1
    • MT1MMP
    • MT1-MMP
    • MT-MMP 1
    • MT-MMP1


    As the first member of membrane type (MT) MMPs, MMP-14, also known as MT1-MMP, plays an important role in extracellular matrix (ECM) remodeling by being able to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules such as CD44 and integrin alpha V (1). MMP-14 is therefore a key enzyme in many physiological and pathological processes such as angiogenesis and tumor invasion. Structurally, MMP-14 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 (2). Recombinant Human MMP-14 consists of the pro and catalytic domains, which can be activated by treatment with furin as described in the Activity Assay Protocol.

    1. Seike, M. (2003) Cancer Lett. 194:1.
    2. Sato, H. et al. (1994) Nature 370:61.

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    Publications for MMP-14/MT1-MMP (918-MP)(10)

    We have publications tested in 3 confirmed species: Human, Mouse, N/A.

    We have publications tested in 2 applications: Bioassay, Enzyme Assay.

    Filter By Application
    Enzyme Assay
    All Applications
    Filter By Species
    All Species
    Showing Publications 1 - 10 of 10.
    Publications using 918-MP Applications Species
    AC Daquinag, Z Gao, C Fussell, K Sun, MG Kolonin Glycosaminoglycan Modification of Decorin Depends on MMP14 Activity and Regulates Collagen Assembly Cells, 2020;9(12):. 2020 [PMID: 33317052] (Bioassay, Mouse) Bioassay Mouse
    L Devel, G Almer, C Cabella, F Beau, M Bernes, P Oliva, F Navarro, R Prassl, H Mangge, I Texier Biodistribution of Nanostructured Lipid Carriers in Mice Atherosclerotic Model Molecules, 2019;24(19):. 2019 [PMID: 31561608] (Bioassay, Human) Bioassay Human
    M Swayampaku, PC McDonald, M Vallejo, E Coyaud, SC Chafe, A Westerback, G Venkateswa, J Shankar, G Gao, EMN Laurent, Y Lou, KL Bennewith, CT Supuran, IR Nabi, B Raught, S Dedhar The interactome of metabolic enzyme carbonic anhydrase IX reveals novel roles in tumor cell migration and invadopodia/MMP14-mediated invasion Oncogene, 2017;36(45):6244-6261. 2017 [PMID: 28692057] (Bioassay) Bioassay
    M Huang, T Liu, P Ma, RA Mitteer, Z Zhang, HJ Kim, E Yeo, D Zhang, P Cai, C Li, L Zhang, B Zhao, L Roccogrand, DM O'Rourke, N Dahmane, Y Gong, C Koumenis, Y Fan c-Met-mediated endothelial plasticity drives aberrant vascularization and chemoresistance in glioblastoma J Clin Invest, 2016;0(0):. 2016 [PMID: 27043280] (Bioassay, Human) Bioassay Human
    Schlomann U, Koller G, Conrad C, Ferdous T, Golfi P, Garcia A, Hofling S, Parsons M, Costa P, Soper R, Bossard M, Hagemann T, Roshani R, Sewald N, Ketchem R, Moss M, Rasmussen F, Miller M, Lauffenburger D, Tuveson D, Nimsky C, Bartsch J ADAM8 as a drug target in pancreatic cancer. Nat Commun, 2015;6(0):6175. 2015 [PMID: 25629724] (Bioassay, Human) Bioassay Human
    Birukawa N, Murase K, Sato Y, Kosaka A, Yoneda A, Nishita H, Fujita R, Nishimura M, Ninomiya T, Kajiwara K, Miyazaki M, Nakashima Y, Ota S, Murakami Y, Tanaka Y, Minomi K, Tamura Y, Niitsu Y Activated hepatic stellate cells are dependent on self-collagen, cleaved by membrane type 1 matrix metalloproteinase for their growth. J Biol Chem, 2014;289(29):20209-21. 2014 [PMID: 24867951] (Enzyme Assay) Enzyme Assay
    Haage A, Schneider I Cellular contractility and extracellular matrix stiffness regulate matrix metalloproteinase activity in pancreatic cancer cells. FASEB J, 2014;28(8):3589-99. 2014 [PMID: 24784579] (Enzyme Assay, Human) Enzyme Assay Human
    Devel L, Beau F, Amoura M, Vera L, Cassar-Lajeunesse E, Garcia S, Czarny B, Stura E, Dive V Simple pseudo-dipeptides with a P2&#039; glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins. J Biol Chem, 2012;287(32):26647-56. 2012 [PMID: 22689580] (Enzyme Assay, N/A) Enzyme Assay N/A
    Tsuchiya S, Simmer JP, Hu JC, Richardson AS, Yamakoshi F, Yamakoshi Y Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp). J. Bone Miner. Res., 2010;26(0):220. 2010 [PMID: 20687161] (Bioassay, Human) Bioassay Human
    Zhou BB, Peyton M, He B, Liu C, Girard L, Caudler E, Lo Y, Baribaud F, Mikami I, Reguart N, Yang G, Li Y, Yao W, Vaddi K, Gazdar AF, Friedman SM, Jablons DM, Newton RC, Fridman JS, Minna JD, Scherle PA Targeting ADAM-mediated ligand cleavage to inhibit HER3 and EGFR pathways in non-small cell lung cancer. Cancer Cell, 2006;10(1):39-50. 2006 [PMID: 16843264] (Enzyme Assay, Human) Enzyme Assay Human

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    Gene Symbol MMP14