Recombinant Human MMP-9 Protein, CF

Recombinant Human MMP‑9 Protein (Catalog # 911-MP) has a molecular weight (MW) of 88-97 kDa as analyzed by SEC-MALS, suggesting that this protein is a monomer. MW may differ from predicted MW due to post-translational modifications (PTMs) present (i.e. Glycosylation).

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).

• Reactivity: Hu
• Applications: Enzyme Activity
• Format: Carrier-Free

Recombinant Human MMP-9 Protein, CF Summary

• Additional Information: Analyzed by SEC-MALS
• Details of Functionality: 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: Ala20
• Structure / Form: Pro form
• Protein/Peptide Type: Recombinant Enzymes
• Gene: MMP9
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <1.1 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Enzyme Activity
• Theoretical MW: 77 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.
• SDS-PAGE: 93 kDa, reducing conditions

Packaging, Storage & Formulations

• 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.
• Buffer: Supplied as a 0.2 μm filtered solution in Tris, CaCl₂, NaCl and Brij-35.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Assay Procedure:
  • 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

Notes

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

Alternate Names for Recombinant Human MMP-9 Protein, CF

• 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

Background

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).

Publications for MMP-9 (911-MP)(32)

Publications using 911-MP

• Caton, ER;Pan, Y;Kiser, KM;Haddaway, CR;Bryden, WA;McLoughlin, M;Mirski, MA;Christenson, RH;Sevilla, CC;Feng, S;Chen, S;Chen, D; Rapid sepsis diagnosis with protease activity measurement medRxiv : the preprint server for health sciences 2025-07-15 [PMID: 40791693] (Bioassay, Human)
• Levengood, MR;Carosino, CM;Zhang, X;Lucas, S;Ortiz, DJ;Westendorf, L;Chin, AP;Martin, AD;Wong, A;Hengel, SM;Sun, H;Zeng, W;Yumul, R;Dominguez, MM;Chen, Y;Zheng, JH;Karlsson, CAB;Trang, VH;Senter, PD;Gardai, SJ; Preclinical development of SGN-CD47M: Protease-activated antibody technology enables selective tumor targeting of the innate immune checkpoint receptor CD47 Molecular cancer therapeutics 2024-10-28 [PMID: 39463068] (Bioassay, N/A)
• Radosavljevic, T;Vukicevic, D;Djureti?, J;Gopcevic, K;Labudovic Borovic, M;Stankovic, S;Samardzic, J;Radosavljevic, M;Vucevic, D;Jakovljevic, V; The Role of Macrophage Inhibitory Factor in TAA-Induced Liver Fibrosis in Mice: Modulatory Effects of Betaine Biomedicines 2024-06-17 [PMID: 38927544] (Zymography, Mouse)
• Huang, J;Zhao, C;Zhang, S; Semaphorin 7A promotes endothelial permeability and inflammation via plexin C1 and integrin ?1 in Kawasaki disease BMC pediatrics 2024-04-27 [PMID: 38678170] (Bioassay, Human)
• X Chen, S Wang, W Xu, M Zhao, Y Zhang, H Xiao Metformin Directly Binds to MMP-9 to Improve Plaque Stability Journal of cardiovascular development and disease, 2023-01-30;10(2):. 2023-01-30 [PMID: 36826550] (Bioassay, Human)
• 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 Dual Functionalized Liposomes for Selective Delivery of Poorly Soluble Drugs to Inflamed Brain Regions Pharmaceutics, 2022-11-07;14(11):. 2022-11-07 [PMID: 36365220] (Bioassay, Human)
• 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 Verteporfin-mediated on/off photoswitching functions synergistically to treat choroidal vascular diseases Bioactive materials, 2022-02-01;14(0):402-415. 2022-02-01 [PMID: 35386820] (Bioassay, Human)
• QC Larrouture, AP Cribbs, SR Rao, M Philpott, SJ Snelling, HJ Knowles Loss of mutual protection between human osteoclasts and chondrocytes in damaged joints initiates osteoclast-mediated cartilage degradation by MMPs Scientific Reports, 2021-11-22;11(1):22708. 2021-11-22 [PMID: 34811438] (Zymography Control, Human)
• 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 Predicting Proteolysis in Complex Proteomes Using Deep Learning International Journal of Molecular Sciences, 2021-03-17;22(6):. 2021-03-17 [PMID: 33803033] (Bioassay, Human)
• M Määttä, HP Laurila, S Holopainen, K Aaltonen, L Lilja-Maul, S Viitanen, MM Rajamäki Matrix metalloproteinase-2, -7, and -9 activities in dogs with idiopathic pulmonary fibrosis compared to healthy dogs and dogs with other respiratory diseases Journal of veterinary internal medicine, 2020-12-04;0(0):. 2020-12-04 [PMID: 33274549] (Zymography Control, Canine)
• T Bluhmki, S Bitzer, JA Gindele, E Schruf, T Kiechle, M Webster, J Schymeinsk, R Ries, F Gantner, D Bischoff, J Garnett, R Heilker Development of a miniaturized 96-Transwell air-liquid interface human small airway epithelial model Sci Rep, 2020-08-03;10(1):13022. 2020-08-03 [PMID: 32747751] (Bioassay, ELISA Capture, Human)
• SR Mendes, LD Amo-Maestr, L Marino-Pue, I Diego, T Goulas, FX Gomis-Rüth Analysis of the inhibiting activity of reversion-inducing cysteine-rich protein with Kazal motifs (RECK) on matrix metalloproteinases Sci Rep, 2020-04-14;10(1):6317. 2020-04-14 [PMID: 32286475] (Bioassay, Human)
• M Hong, H Cheng, L Song, W Wang, Q Wang, D Xu, W Xing Wogonin Suppresses the Activity of Matrix Metalloproteinase-9 and Inhibits Migration and Invasion in Human Hepatocellular Carcinoma Molecules, 2018-02-11;23(2):. 2018-02-11 [PMID: 29439451] (Bioassay)
• N Kondo, T Temma, K Aita, S Shimochi, K Koshino, M Senda, H Iida Development of matrix metalloproteinase-targeted probes for lung inflammation detection with positron emission tomography Sci Rep, 2018-01-22;8(1):1347. 2018-01-22 [PMID: 29358724] (Bioassay)
• MV Sasidhar, SK Chevooru, O Eickelberg, HP Hartung, O Neuhaus Downregulation of monocytic differentiation via modulation of CD147 by 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors PLoS ONE, 2017-12-18;12(12):e0189701. 2017-12-18 [PMID: 29253870] (Zymography, Human)
• K Gopcevic, B Rovcanin, D Kekic, D Milasinovi, G Kocic, I Stojanovic Gelatinases A and B and Antioxidant Enzyme Activity in the Early Phase of Acute Myocardial Infarction Folia Biol. (Praha), 2017-01-01;63(1):20-26. 2017-01-01 [PMID: 28374671] (Zymography)
• N Willumsen, CL Bager, DJ Leeming, AC Bay-Jensen, MA Karsdal Nidogen-1 Degraded by Cathepsin S can be Quantified in Serum and is Associated with Non-Small Cell Lung Cancer Neoplasia, 2017-03-07;19(4):271-278. 2017-03-07 [PMID: 28282545] (Enzyme Assay, Human)
• Matthew N Svalina IGF1R as a Key Target in High Risk, Metastatic Medulloblastoma Sci Rep, 2016-06-03;6(0):27012. 2016-06-03 [PMID: 27255663] (Bioassay, Human)
• Pathogenic Upregulation of Glial Lipocalin-2 in the Parkinsonian Dopaminergic System J Neurosci, 2016-05-18;36(20):5608-22. 2016-05-18 [PMID: 27194339] (Bioassay, Human)
• 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 GDF15/MIC1 and MMP9 Cerebrospinal Fluid Levels in Parkinson&#039;s Disease and Lewy Body Dementia. PLoS ONE, 2016-03-03;0(0):1932-6203. 2016-03-03 [PMID: 26938614] (Human)
• Pei S, Yang X, Wang H, Zhang H, Zhou B, Zhang D, Lin D Plantamajoside, a potential anti-tumor herbal medicine inhibits breast cancer growth and pulmonary metastasis by decreasing the activity of matrix metalloproteinase-9 and -2. BMC Cancer, 2015-12-16;15(0):965. 2015-12-16 [PMID: 26674531] (Bioassay, Human)
• 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 Plasma levels of the MMP-9:TIMP-1 complex as prognostic biomarker in breast cancer: a retrospective study. BMC Cancer, 2013-12-13;13(0):598. 2013-12-13 [PMID: 24330623] (Standard, Proximity Ligation Assay, Chicken, Human, N/A)
• Wang , Ling, Cossette , Stephani, Rarick , Kevin R, Gershan , Jill, Dwinell , Michael, Harder , David R, Ramchandran , Ramani Astrocytes directly influence tumor cell invasion and metastasis in vivo. PLoS ONE, 2013-12-04;8(12):e80933. 2013-12-04 [PMID: 24324647] (Bioassay, Human)
• Djokic J, Fagotto-Kaufmann C, Bartels R, Nelea V, Reinhardt D Fibulin-3, -4, and -5 are highly susceptible to proteolysis, interact with cells and heparin, and form multimers. J Biol Chem, 2013-06-19;288(31):22821-35. 2013-06-19 [PMID: 23782690] (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, 2012-06-11;287(32):26647-56. 2012-06-11 [PMID: 22689580] (Enzyme Assay)
• 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., 2011-01-01;26(0):220. 2011-01-01 [PMID: 20687161] (Bioassay, Human)
• Gonzalez RM, Seurynck-Servoss SL, Crowley SA Development and validation of sandwich ELISA microarrays with minimal assay interference. J. Proteome Res., 2008-04-19;7(6):2406-14. 2008-04-19 [PMID: 18422355] (ELISA (Standard))
• Zhao Z, McCloud B, Fleming R, Klempner MS Borrelia burgdorferi-induced monocyte chemoattractant protein-1 production in vivo and in vitro. Biochem. Biophys. Res. Commun., 2007-05-02;358(2):528-33. 2007-05-02 [PMID: 17485071] (Zymography)
• Gaggar A, Li Y, Weathington N, Winkler M, Kong M, Jackson P, Blalock JE, Clancy JP Matrix metalloprotease-9 dysregulation in lower airway secretions of cystic fibrosis patients. Am. J. Physiol. Lung Cell Mol. Physiol., 2007-03-23;293(1):L96-L104. 2007-03-23 [PMID: 17384080] (Bioassay, N/A)
• Borrelli V, di Marzo L, Sapienza P, Colasanti M, Moroni E, Cavallaro A Role of platelet-derived growth factor and transforming growth factor beta1 the in the regulation of metalloproteinase expressions. Surgery, 2006-09-01;140(3):454-63. 2006-09-01 [PMID: 16934609] (Western Blot)
• 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, 2006-07-01;10(1):39-50. 2006-07-01 [PMID: 16843264] (Enzyme Assay, Human)
• Levesque JP, Hendy J, Winkler IG, Takamatsu Y, Simmons PJ 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. Exp. Hematol., 2003-02-01;31(2):109-17. 2003-02-01 [PMID: 12591275] (Enzyme Assay, Human)

FAQs for MMP-9 (911-MP). (Showing 1 - 1 of 1 FAQs).

1.  I’m looking for a pair of antibodies to MMP-9 that can be used in a sandwich assay. Do you carry any? 
   • We have 10 primary antibodies for MMP-9 that have been tested in ELISA, seen here.It looks like 2 have been tested for capture (please note the tested species for each of these), seen here.6 have been tested for detection, seen here.

Bioinformatics

• Gene Symbol: MMP9
• Uniprot:
  • P14780()