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Recombinant Human MMP-9 Protein, CF

Catalog #: 911-MP
30 Citations 8 Reviews Datasheet
Catalog # Availability Size / Price Qty
911-MP-010
Recombinant Human MMP-9 Protein Enzyme Activity
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Product Details
Citations (30)
FAQs
Supplemental Products
Reviews (8)
Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human MMP-9 Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<1.1 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (Catalog # ES001). The specific activity is >1,300 pmol/min/µg, as measured under the described conditions.
Source
Chinese Hamster Ovary cell line, CHO-derived human MMP-9 protein
Ala20-Asp707 (Gln279Arg)
Accession #
P14780
N-terminal Sequence
Analysis
Ala20
Structure / Form
Pro form
Predicted Molecular Mass
77 kDa
SDS-PAGE
93 kDa, reducing conditions

Product Datasheets

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911-MP

Product Datasheet

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.

911-MP

Formulation Supplied as a 0.2 μm filtered solution in Tris, CaCl2, NaCl and Brij-35.
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

Materials
  • Assay Buffer: 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% Brij-35 (w/v), pH 7.5 (TCNB)
  • Recombinant Human MMP-9 (rhMMP-9) (Catalog # 911-MP)
  • p-aminophenylmercuric acetate (APMA), (Sigma, Catalog # A-9563), prepare a 100 mM stock in DMSO
  • Substrate: MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 (Catalog # ES001)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhMMP-9 to 100 µg/mL in Assay Buffer.
  2. Activate rhMMP-9 by adding APMA to a final concentration of 1 mM.
  3. Incubate at 37 °C for 24 hours.
  4. Dilute activated rhMMP-9 to 0.4 ng/µL in Assay Buffer.
  5. Dilute Substrate to 20 µM in Assay Buffer.
  6. Load 50 µL of the 0.4 ng/µL rhMMP-9 into a plate and start the reaction by adding 50 µL of 20 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 20 µM Substrate.
  7. Read at excitation and emission wavelengths of 320 nm and 405 nm, 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-9: 0.020 µg
  • Substrate: 10 µM

Scientific Data

Enzyme Activity Recombinant Human MMP-9 Protein Enzyme Activity View Larger

Recombinant Human MMP-9 (Catalog # 911-MP) is measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (Catalog # ES001).

Background: MMP-9

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-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 maybe be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin-binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline-rich linker region, and a carboxyl terminal hemopexin-like domain. In addition to the human enzyme, the recombinant mouse MMP-9 is also available (Catalog # 909-MM).

Long Name
Matrix Metalloproteinase 9
Entrez Gene IDs
4318 (Human); 17395 (Mouse); 81687 (Rat); 102117693 (Cynomolgus Monkey)
Alternate Names
92 kDa gelatinase; 92 kDa type IV collagenase; CLG4B; EC 3.4.24; EC 3.4.24.35; Gelatinase B; GELB; macrophage gelatinase; MANDP2; matrix metallopeptidase 9; matrix metalloproteinase 9; matrix metalloproteinase-9; MMP9; MMP-9; type V collagenase

Citations for Recombinant Human MMP-9 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.

30 Citations: Showing 1 - 10
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  1. The Role of Macrophage Inhibitory Factor in TAA-Induced Liver Fibrosis in Mice: Modulatory Effects of Betaine
    Authors: Radosavljevic, T;Vukicevic, D;Djureti?, J;Gopcevic, K;Labudovic Borovic, M;Stankovic, S;Samardzic, J;Radosavljevic, M;Vucevic, D;Jakovljevic, V;
    Biomedicines
    Species: Mouse
    Sample Types: Tissue Homogenates
    Applications: Zymography
  2. Semaphorin 7A promotes endothelial permeability and inflammation via plexin C1 and integrin ?1 in Kawasaki disease
    Authors: Huang, J;Zhao, C;Zhang, S;
    BMC pediatrics
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Metformin Directly Binds to MMP-9 to Improve Plaque Stability
    Authors: X Chen, S Wang, W Xu, M Zhao, Y Zhang, H Xiao
    Journal of cardiovascular development and disease, 2023-01-30;10(2):.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: Bioassay
  4. Dual Functionalized Liposomes for Selective Delivery of Poorly Soluble Drugs to Inflamed Brain Regions
    Authors: S Giofrè, A Renda, S Sesana, B Formicola, B Vergani, BE Leone, V Denti, G Paglia, S Groppuso, V Romeo, L Muzio, A Balboni, A Menegon, A Antoniou, A Amenta, D Passarella, P Seneci, S Pellegrino, F Re
    Pharmaceutics, 2022-11-07;14(11):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Verteporfin-mediated on/off photoswitching functions synergistically to treat choroidal vascular diseases
    Authors: Y Ju, X Dai, Z Tang, Z Ming, N Ni, D Zhu, J Zhang, B Ma, J Wang, R Huang, S Zhao, Y Pang, P Gu
    Bioactive materials, 2022-02-01;14(0):402-415.
    Species: Human
    Sample Types: Small Molecule
    Applications: Bioassay
  6. Loss of mutual protection between human osteoclasts and chondrocytes in damaged joints initiates osteoclast-mediated cartilage degradation by MMPs
    Authors: QC Larrouture, AP Cribbs, SR Rao, M Philpott, SJ Snelling, HJ Knowles
    Scientific Reports, 2021-11-22;11(1):22708.
    Species: Human
    Sample Types: Recombinant Proteins
    Applications: Zymography Control
  7. Predicting Proteolysis in Complex Proteomes Using Deep Learning
    Authors: M Ozols, A Eckersley, CI Platt, C Stewart-Mc, SA Hibbert, J Revote, F Li, CEM Griffiths, REB Watson, J Song, M Bell, MJ Sherratt
    International Journal of Molecular Sciences, 2021-03-17;22(6):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Matrix metalloproteinase-2, -7, and -9 activities in dogs with idiopathic pulmonary fibrosis compared to healthy dogs and dogs with other respiratory diseases
    Authors: M Määttä, HP Laurila, S Holopainen, K Aaltonen, L Lilja-Maul, S Viitanen, MM Rajamäki
    Journal of veterinary internal medicine, 2020-12-04;0(0):.
    Species: Canine
    Sample Types:
    Applications: Zymography Control
  9. Development of a miniaturized 96-Transwell air-liquid interface human small airway epithelial model
    Authors: T Bluhmki, S Bitzer, JA Gindele, E Schruf, T Kiechle, M Webster, J Schymeinsk, R Ries, F Gantner, D Bischoff, J Garnett, R Heilker
    Sci Rep, 2020-08-03;10(1):13022.
    Species: Human
    Sample Types: Cell Culture Supernates, Whole Cells
    Applications: Bioassay, ELISA Capture
  10. Analysis of the inhibiting activity of reversion-inducing cysteine-rich protein with Kazal motifs (RECK) on matrix metalloproteinases
    Authors: SR Mendes, LD Amo-Maestr, L Marino-Pue, I Diego, T Goulas, FX Gomis-Rüth
    Sci Rep, 2020-04-14;10(1):6317.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  11. Wogonin Suppresses the Activity of Matrix Metalloproteinase-9 and Inhibits Migration and Invasion in Human Hepatocellular Carcinoma
    Authors: M Hong, H Cheng, L Song, W Wang, Q Wang, D Xu, W Xing
    Molecules, 2018-02-11;23(2):.
    Applications: Bioassay
  12. Development of matrix metalloproteinase-targeted probes for lung inflammation detection with positron emission tomography
    Authors: N Kondo, T Temma, K Aita, S Shimochi, K Koshino, M Senda, H Iida
    Sci Rep, 2018-01-22;8(1):1347.
    Applications: Bioassay
  13. Downregulation of monocytic differentiation via modulation of CD147 by 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors
    Authors: MV Sasidhar, SK Chevooru, O Eickelberg, HP Hartung, O Neuhaus
    PLoS ONE, 2017-12-18;12(12):e0189701.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Zymography
  14. Nidogen-1 Degraded by Cathepsin S can be Quantified in Serum and is Associated with Non-Small Cell Lung Cancer
    Authors: N Willumsen, CL Bager, DJ Leeming, AC Bay-Jensen, MA Karsdal
    Neoplasia, 2017-03-07;19(4):271-278.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  15. Gelatinases A and B and Antioxidant Enzyme Activity in the Early Phase of Acute Myocardial Infarction
    Authors: K Gopcevic, B Rovcanin, D Kekic, D Milasinovi, G Kocic, I Stojanovic
    Folia Biol. (Praha), 2017-01-01;63(1):20-26.
    Applications: Zymography
  16. IGF1R as a Key Target in High Risk, Metastatic Medulloblastoma
    Authors: Matthew N Svalina
    Sci Rep, 2016-06-03;6(0):27012.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  17. Pathogenic Upregulation of Glial Lipocalin-2 in the Parkinsonian Dopaminergic System
    J Neurosci, 2016-05-18;36(20):5608-22.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  18. GDF15/MIC1 and MMP9 Cerebrospinal Fluid Levels in Parkinson's Disease and Lewy Body Dementia.
    Authors: Walter Maetzler, Willy Deleersni, Valérie Hanssens, Alice Bernard, Kathrin Brockmann, Justus Marquetan, Isabel Wurster, Tim W Rattay, Lorenzo Roncoroni, Eva Schaeffer, Stefanie Lerche, Anja Apel, Christian Deuschle, Daniela Berg
    PLoS ONE, 2016-03-03;0(0):1932-6203.
    Species: Human
    Sample Types: Beads
  19. Plantamajoside, a potential anti-tumor herbal medicine inhibits breast cancer growth and pulmonary metastasis by decreasing the activity of matrix metalloproteinase-9 and -2.
    Authors: Pei S, Yang X, Wang H, Zhang H, Zhou B, Zhang D, Lin D
    BMC Cancer, 2015-12-16;15(0):965.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  20. Plasma levels of the MMP-9:TIMP-1 complex as prognostic biomarker in breast cancer: a retrospective study.
    Authors: Thorsen S, Christensen S, Wurtz S, Lundberg M, Nielsen B, Vinther L, Knowles M, Gee N, Fredriksson S, Moller S, Brunner N, Schrohl A, Stenvang J
    BMC Cancer, 2013-12-13;13(0):598.
  21. Astrocytes directly influence tumor cell invasion and metastasis in vivo.
    Authors: Wang, Ling, Cossette, Stephani, Rarick, Kevin R, Gershan, Jill, Dwinell, Michael, Harder, David R, Ramchandran, Ramani
    PLoS ONE, 2013-12-04;8(12):e80933.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: Bioassay
  22. Fibulin-3, -4, and -5 are highly susceptible to proteolysis, interact with cells and heparin, and form multimers.
    Authors: Djokic J, Fagotto-Kaufmann C, Bartels R, Nelea V, Reinhardt D
    J Biol Chem, 2013-06-19;288(31):22821-35.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  23. 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, 2012-06-11;287(32):26647-56.
    Applications: Enzyme Assay
  24. 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., 2011-01-01;26(0):220.
    Species: Human
    Sample Types:
    Applications: Bioassay
  25. Development and validation of sandwich ELISA microarrays with minimal assay interference.
    Authors: Gonzalez RM, Seurynck-Servoss SL, Crowley SA
    J. Proteome Res., 2008-04-19;7(6):2406-14.
    Applications: ELISA (Standard)
  26. Borrelia burgdorferi-induced monocyte chemoattractant protein-1 production in vivo and in vitro.
    Authors: Zhao Z, McCloud B, Fleming R, Klempner MS
    Biochem. Biophys. Res. Commun., 2007-05-02;358(2):528-33.
    Applications: Zymography
  27. Matrix metalloprotease-9 dysregulation in lower airway secretions of cystic fibrosis patients.
    Authors: Gaggar A, Li Y, Weathington N, Winkler M, Kong M, Jackson P, Blalock JE, Clancy JP
    Am. J. Physiol. Lung Cell Mol. Physiol., 2007-03-23;293(1):L96-L104.
    Applications: Western Blot
  28. Role of platelet-derived growth factor and transforming growth factor beta1 the in the regulation of metalloproteinase expressions.
    Authors: Borrelli V, di Marzo L, Sapienza P, Colasanti M, Moroni E, Cavallaro A
    Surgery, 2006-09-01;140(3):454-63.
    Applications: Western Blot
  29. 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, 2006-07-01;10(1):39-50.
    Species: Human
    Sample Types:
    Applications: Enzyme Assay
  30. Granulocyte colony-stimulating factor induces the release in the bone marrow of proteases that cleave c-KIT receptor (CD117) from the surface of hematopoietic progenitor cells.
    Authors: Levesque JP, Hendy J, Winkler IG, Takamatsu Y, Simmons PJ
    Exp. Hematol., 2003-02-01;31(2):109-17.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay

FAQs

  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 enzyme have a tag?

    • No, this enzyme does not have a tag.  Please refer to the Source section on the product-specific page or product datasheet for sequence information.

  3. If I use this enzyme at a higher concentration, do I need to change the concentration of APMA to activate it?

    • We have only optimized activation conditions for one particular concentration of this MMP enzyme as part of our regular QC testing for enzymatic activity. Activating the enzyme at any different concentration would have to be optimized by the end user.

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

    • Yes, this enzyme requires activation prior to use.

  5. 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.

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Reviews for Recombinant Human MMP-9 Protein, CF

Average Rating: 4.6 (Based on 8 Reviews)

5 Star
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4 Star
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3 Star
12.5%
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Recombinant Human MMP-9 Protein, CF
By Jan Van Deun on 08/04/2023
Application: Enzymatic activity in vitro
Reason for Rating: This enzyme was used to cleave a selection of FRET substrates for different MMPs and clearly cleaved the MMP9-specific peptide at the highest rate.
Enzymatic activity in vitro Recombinant Human MMP-9 Protein, CF 911-MP
Recombinant Human MMP-9 Protein, CF
By Andres Ocampo Carrillo on 03/04/2023
Application: In vitro bioactivity in cell culture
Reason for Rating: The product was easy to dissolve and use in treating human chondrocytes, exhibiting proper enzymatic activity in vitro
In vitro bioactivity in cell culture Recombinant Human MMP-9 Protein, CF 911-MP
Recombinant Human MMP-9 Protein, CF
By Oleg Yerov on 11/06/2020
Application: Enzymatic activity in vitro
Recombinant Human MMP-9 Protein, CF
By Anonymous on 10/09/2019
Application: Enzymatic activity in vitro
Recombinant Human MMP-9 Protein, CF
By Anonymous on 08/14/2018
Application: Enzymatic activity in vitro
Enzymatic activity in vitro Recombinant Human MMP-9 Protein, CF 911-MP
Recombinant Human MMP-9 Protein, CF
By Radhika Mehta on 03/22/2018
Application: Binding assay/Protein-protein interaction
Recombinant Human MMP-9 Protein, CF
By Balaji Mahender on 12/20/2017
Application: Immunoassay Standard
Recombinant Human MMP-9 Protein, CF
By Anonymous on 11/10/2017
Application: Immunoassay Standard
Immunoassay Standard Recombinant Human MMP-9 Protein, CF 911-MP