Human MMP-9 Quantikine ELISA Kit



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Human MMP-9 Quantikine ELISA Kit Summary

The Quantikine Human MMP-9 Immunoassay is a 3.5 hour solid phase ELISA designed to measure MMP-9 (92 kDa pro- and 82 kDa active forms but not the 65 kDa form) in cell culture supernates, saliva, serum, plasma, and urine. It is calibrated with CHO cell-expressed recombinant human pro-MMP-9 and the antibodies were raised against the recombinant factor. Natural human MMP-9 showed dose-response ...curves that were parallel to the standard curves obtained using the recombinant Quantikine kit standards, indicating that this kit can be used to determine relative mass values of natural human MMP-9.
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Natural and recombinant human 92 kDa Pro-MMP-9 and the 82 kDa active MMP-9
Assay Type
Solid Phase Sandwich ELISA
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Spike Recovery
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Sample Volume
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Application Notes
Interference observed with 1 or more available related molecules.
Read Publications using
DMP900 in the following applications:

Packaging, Storage & Formulations

Store the unopened product at 2 - 8 °C. Do not use past expiration date.


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

Alternate Names for Human MMP-9 Quantikine ELISA Kit

  • 92 kDa gelatinase
  • 92 kDa type IV collagenase
  • CLG4B
  • EC 3.4.24
  • EC
  • Gelatinase B
  • GELB
  • macrophage gelatinase
  • MANDP2
  • matrix metallopeptidase 9
  • matrix metalloproteinase 9
  • matrix metalloproteinase-9
  • MMP9
  • MMP-9
  • type V collagenase


Matrix metalloproteinases (MMPs), also called matrixins, constitute a family of zinc and calcium dependent endopeptidases that function in the breakdown of the extracellular matrix (ECM) and in the processing of a variety of molecules in different subcellular environments. They play an important role in many normal physiological processes such as embryonic development, morphogenesis, reproduction, and tissue remodeling (1, 2). They also participate in inflammatory and autoimmune disorders such as arthritis, cancer, and cardiovascular disease (3-5). While the amounts of newly synthesized MMPs are regulated mainly at the levels of transcription, the proteolytic activities of existing MMPs are controlled through both the activation of proenzymes or zymogens and the inhibition of active enzymes by endogenous inhibitors, alpha 2-Macroglobulin, and tissue inhibitors of metalloproteinases (TIMPs) (6). 
MMP-9 (also referred to as gelatinase B, 92 kDa type IV collagenase, 92 kDa gelatinase, and type V collagenase) is secreted as a glycosylated proenzyme (6-8). Activation of the proenzyme involves proteolytic removal of the N-terminal pro region, resulting in the 82 kDa active enzyme (9, 10). Active human MMP-9 shares 72% and 74% amino acid sequence identity with mouse and rat MMP-9, respectively. In addition to the zinc-binding site, the catalytic domain also contains three contiguous fibronectin type II homology units responsible for binding gelatin (11). A proline-rich hinge region links the catalytic domain to the C-terminal hemopexin-like domain. In vitro treatment of the proenzyme with 4-aminophenylmercuric acetate (APMA) produces not only the active enzyme but also a C-terminal truncated form with activity comparable to that of the active form (12). MMP-9 degrades components of the ECM with high specific activity for denatured collagens (gelatin). It can cleave native collagens of type III, IV, V, and XI, as well as Elastin, Nidogen-1, and Vitronectin (2, 3). MMP-9 can also cleave a variety of chemokines and growth factors (e.g. IL-1 beta , CXCL8/IL-8, CXCL7, CXCL4, CXCL1, Latent TGF-beta , membrane bound TNF-alpha , VEGF, and FGF basic), Amyloid beta peptide, Substance P, and Myelin Basic Protein (3, 13-15). This action can increase or decrease the biological activity of soluble factors and can also liberate them from association with the ECM (16, 17). MMP-9 can also trigger signaling through various transmembrane proteins or inhibit signaling by inducing their shedding from the cell surface (e.g. CD44, E-Cadherin, Integrins, ICAM-1, and IL-2 R alpha ) (3, 18-20). 
MMP-9 is produced by a variety of normal and transformed cells including neutrophils, monocytes, macrophages, astrocytes, fibroblasts, osteoclasts, chondrocytes, keratinocytes, endothelial and epithelial cells. It exerts physiological and pathological angiogenic and remodeling effects on the vasculature (21-25). Activated neutrophils release proMMP-9 which is free of TIMP-1, allowing the liberation of pro-angiogenic FGF-2 from the ECM (17). MMP-9 in complex with TIMP-1 does not induce FGF-2 release (17). Neutrophil-derived MMP-9 exacerbates the inflammatory response, in part by generating collagen-derived peptides that induce the release of additional neutrophil MMP9 (26). MMP-9 also plays a role in bone formation and remodeling (1, 21, 27), methamphetamineinduced behavioral sensitization and reward (28), the regulation of neuronal synapse remodeling (29), trophoblast invasion during implantation (30), and the inactivation of Serpin alpha 1-Proteinase Inhibitor (31). The shedding of adhesion proteins by MMP-9 has a direct effect on tumor cell invasiveness (18-20). 
Circulating levels of MMP-9 are increased in many inflammatory disorders including intraluminal thrombus formation (32), atherosclerosis (33), Crohn's disease (34), hepatitis C virus infection (35), colorectal cancer (36), and Duchenne muscular dystrophy (37). The ratio of MMP-9 to TIMP-1 is also increased in multiple sclerosis serum (38) and cystic fibrosis sputum (39), but it is decreased in the serum during cytomegalovirus infection (40). Levels of free MMP-9 and complexes of MMP-9 with Lipocalin-2/NGAL are elevated in the urine of ovarian cancer and uterine tract infection patients, respectively (41, 42).

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⚠ WARNING: This product can expose you to chemicals including N,N-Dimethylforamide, which is known to the State of California to cause cancer. For more information, go to

Publications for MMP-9 (DMP900)(189)

We have publications tested in 3 confirmed species: Human, Mouse, Primate.

We have publications tested in 1 application: ELISA Capture.

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Showing Publications 1 - 10 of 189. Show All 189 Publications.
Publications using DMP900 Applications Species
J Jarecki, T Ma?ecka-Ma, E Kosior-Jar, W Widuchowsk, P Krasowski, M Gutbier, M Dobrzy?ski, T Blicharski Concentration of Selected Metalloproteinases and Osteocalcin in the Serum and Synovial Fluid of Obese Women with Advanced Knee Osteoarthritis International Journal of Environmental Research and Public Health, 2022;19(6):. 2022 [PMID: 35329213] (Human) Human
C Xie, B Tang, K Wu, Q Meng, F Wang Increased serum LOXL2 concentration in pelvic inflammatory disease with pelvic adhesion Oncogene, 2022;22(1):59. 2022 [PMID: 35246120] (Human) Human
MM Ali, I Mirza, D Naquiallah, C Hassan, M Masrur, FM Bianco, AM Mahmoud CD147 Levels in Blood and Adipose Tissues Correlate with Vascular Dysfunction in Obese Diabetic Adults Journal of cardiovascular development and disease, 2021;9(1):. 2021 [PMID: 35050217] (Human) Human
F Kang, Q Yi, P Gu, Y Dong, Z Zhang, L Zhang, Y Bai Controlled growth factor delivery system with osteogenic-angiogenic coupling effect for bone regeneration Journal of Orthopaedic Translation, 2021;31(0):110-125. 2021 [PMID: 34976731] (Human) Human
D Bakkalci, A Jay, A Rezaei, CA Howard, HJ Haugen, J Pape, S Kishida, M Kishida, G Jell, TR Arnett, S Fedele, U Cheema Bioengineering the ameloblastoma tumour to study its effect on bone nodule formation Scientific Reports, 2021;11(1):24088. 2021 [PMID: 34916549] (Human) Human
S Nawrocka-M, J Biegus, M Hurkacz, M Guzik, M Rosiek-Bie, EA Jankowska, P Ponikowski, R Zymli?ski Differences in the Biomarker Profile of De Novo Acute Heart Failure versus Decompensation of Chronic Heart Failure Biomolecules, 2021;11(11):. 2021 [PMID: 34827701] (Human) Human
A Kuzumi, A Yoshizaki, KM Matsuda, H Kotani, Y Norimatsu, M Fukayama, S Ebata, T Fukasawa, A Yoshizaki-, Y Asano, K Morikawa, Y Kazoe, K Mawatari, T Kitamori, S Sato Interleukin-31 promotes fibrosis and T helper 2 polarization in systemic sclerosis Nature Communications, 2021;12(1):5947. 2021 [PMID: 34642338] (Human) Human
K Wadowska, P B?asiak, A Rzechonek, I Bil-Lula, M ?liwi?ska- New Insights on Old Biomarkers Involved in Tumor Microenvironment Changes and Their Diagnostic Relevance in Non-Small Cell Lung Carcinoma Biomolecules, 2021;11(8):. 2021 [PMID: 34439874] (Human) Human
L Scola, RM Giarratana, V Marinello, V Cancila, C Pisano, G Ruvolo, G Frati, D Lio, CR Balistreri Polymorphisms of Pro-Inflammatory IL-6 and IL-1&beta Cytokines in Ascending Aortic Aneurysms as Genetic Modifiers and Predictive and Prognostic Biomarkers Biomolecules, 2021;11(7):. 2021 [PMID: 34202072] (Human) Human
Y Wu, K Brennan, AB Fernández, MM Mc Gee Cyclophilin A regulates secretion of tumour-derived extracellular vesicles Translational Oncology, 2021;14(8):101112. 2021 [PMID: 33984826] (Human) Human
Show All 189 Publications.

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FAQs for MMP-9 (DMP900). (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. looks like 2 have been tested for capture (please note the tested species for each of these). has been tested for detection.

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Gene Symbol MMP9