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

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R&D Systems Recombinant Proteins and Enzymes
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Citations (11)
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Recombinant Human MMP-14/MT1-MMP Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
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
Predicted Molecular Mass
31 kDa
31 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl, CaCl2 and Glycerol.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: 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.

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
  • Reconstitution Calculator

    Reconstitution Calculator

    The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.


    Background: MMP-14/MT1-MMP

    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.
    Long Name
    Matrix Metalloproteinase 14/Membrane Type 1 MMP
    Entrez Gene IDs
    4323 (Human)
    Alternate Names
    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; MT1-MMPMTMMP1; MT-MMP 1; MT-MMP1

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

    R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

    11 Citations: Showing 1 - 10
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    1. Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)-A CleavEx Based Analysis
      Authors: K Falkowski, E Bielecka, IB Thøgersen, O Boche?ska, K P?aza, M Kali?ska, L S?siadek, M Magoch, A P?cak, M Wi?niewska, N Gruba, M Wysocka, A Wojtysiak, M Brzezi?ska, K Sychowska, A Pejkovska, M Rehders, G Butler, CM Overall, K Brix, G Dubin, A Lesner, A Kozik, JJ Enghild, J Potempa, T Kantyka
      Int J Mol Sci, 2020;21(12):.
      Species: Human
      Sample Types: Recombinant Protein
      Applications: Bioassay
    2. Glycosaminoglycan Modification of Decorin Depends on MMP14 Activity and Regulates Collagen Assembly
      Authors: AC Daquinag, Z Gao, C Fussell, K Sun, MG Kolonin
      Cells, 2020;9(12):.
      Species: Mouse
      Sample Types: Recombinant Protein
      Applications: Bioassay
    3. Biodistribution of Nanostructured Lipid Carriers in Mice Atherosclerotic Model
      Authors: L Devel, G Almer, C Cabella, F Beau, M Bernes, P Oliva, F Navarro, R Prassl, H Mangge, I Texier
      Molecules, 2019;24(19):.
      Species: Human
      Sample Types: Peptide
      Applications: Bioassay
    4. The interactome of metabolic enzyme carbonic anhydrase IX reveals novel roles in tumor cell migration and invadopodia/MMP14-mediated invasion
      Authors: 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
      Oncogene, 2017;36(45):6244-6261.
      Applications: Bioassay
    5. c-Met-mediated endothelial plasticity drives aberrant vascularization and chemoresistance in glioblastoma
      Authors: 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
      J Clin Invest, 2016;0(0):.
      Species: Human
      Sample Types: Whole Cells
      Applications: Bioassay
    6. ADAM8 as a drug target in pancreatic cancer.
      Authors: 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
      Nat Commun, 2015;6(0):6175.
      Species: Human
      Sample Types: Whole Cells
      Applications: Bioassay
    7. Cellular contractility and extracellular matrix stiffness regulate matrix metalloproteinase activity in pancreatic cancer cells.
      Authors: Haage A, Schneider I
      FASEB J, 2014;28(8):3589-99.
      Species: Human
      Sample Types: Recombinant Protein
      Applications: Enzyme Assay
    8. Activated hepatic stellate cells are dependent on self-collagen, cleaved by membrane type 1 matrix metalloproteinase for their growth.
      Authors: 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
      J Biol Chem, 2014;289(29):20209-21.
      Applications: Enzyme Assay
    9. Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins.
      Authors: Devel L, Beau F, Amoura M, Vera L, Cassar-Lajeunesse E, Garcia S, Czarny B, Stura E, Dive V
      J Biol Chem, 2012;287(32):26647-56.
      Species: N/A
      Sample Types: Fluorogenic Peptide Substrate
      Applications: Enzyme Assay
    10. Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp).
      Authors: Tsuchiya S, Simmer JP, Hu JC, Richardson AS, Yamakoshi F, Yamakoshi Y
      J. Bone Miner. Res., 2010;26(0):220.
      Species: Human
      Sample Types:
      Applications: Bioassay
    11. Targeting ADAM-mediated ligand cleavage to inhibit HER3 and EGFR pathways in non-small cell lung cancer.
      Authors: 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
      Cancer Cell, 2006;10(1):39-50.
      Species: Human
      Sample Types:
      Applications: Enzyme Assay


    1. Can the enzyme be stored after activation, or do I need to use it immediately after activation?

      • We recommend only activating the amount of enzyme needed for your assay, and recommend activating the enzyme immediately prior to use. Any unactivated enzyme should be stored in aliquots at either the stock concentration at which the enzyme was supplied, or the reconstitution concentration, according to the product datasheet.

    2. Does this MMP enzyme need to be activated to work?

      • Yes, this enzyme requires activation prior to use.

    3. What is the activity of this enzyme in units/µg?

      • We supply this enzyme as a mass and calculate its activity relative to mass (pmol/min/µg). We have not calibrated this enzyme to an international standard unit, so we are unable to provide a conversion to units/µg.

    View all Proteins and Enzyme FAQs

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