QuickZyme Human MMP-9 Activity Assay principle
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QuickZyme Human MMP-9 Activity Assay

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Quantify both endogenous active MMP-9 and total MMP-9

The QuickZyme Human MMP-9 Activity Assay enables you to specifically measure in biological samples both active human MMP-9, as well as (pro)MMP-9 which is activated on the plate by APMA. It can be used for the measurement of MMP-9 activity in various biological samples, such as conditioned culture media, tissue homogenates, serum, plasma and urine.

This 96-well plate format assay is based on the QuickZyme technology, using a modified pro-enzyme as a substrate, which upon activation is able to release color from a chromogenic peptide substrate. This multiplication step provides a unique assay sensitivity.


  • Measures both endogenous active MMP-9 (naturally occurring) and total active MMP-9 (following activation with APMA).
  • Samples: conditioned cell culture medium, serum, plasma, urine, synovial fluid and tissue homogenates.
  • Quantitative.
  • Range: 0.5 to 16 ng/ml (1 h incubation with detection reagent), 0.01-1 ng/ml (4 h incubation with detection reagent).
  • Sensitivity: 0.005 ng/ml.
  • Ease-of-use: Equivalent to ELISA.


        Enzyme activity immunoassay

        QuickZyme Human MMP-9 Activity Assay principle


        • conditioned cell culture medium, serum, plasma, urine, synovial fluid, tissue homogenates


        • 0.1 ng/ml (1 hr incubation)
        • 0.005 ng/ml (4 hr incubation)

            Quantitative Measurement

            Typical data with 4 hours incubation: QuickZyme Human MMP-9 Activity Assay

            Typical data with 4 hours incubation. The shown data curve is provided for demonstration only.


            Unopened kit: Store at -20°C, except for the standard, this vial should be stored at -70°C. Do not use kit, or individual kit components past kit expiration date.

            Opened kit / reconstituted reagents: Please refer to kit manual.

            Other names

            Matrix metalloproteinase-9, MMP9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB


            Product References

            • Rodríguez-Sánchez, Elena et al. “Prediction of the early response to spironolactone in resistant hypertension by the combination of matrix metalloproteinase-9 activity and arterial stiffness parameters.” European heart journal. Cardiovascular pharmacotherapy vol. 8,1 (2022): 68-76. doi:10.1093/ehjcvp/pvaa086
            • Kim, Michael D et al. “Vegetable glycerin e-cigarette aerosols cause airway inflammation and ion channel dysfunction.” Frontiers in pharmacology vol. 13 1012723. 26 Sep. 2022, doi:10.3389/fphar.2022.1012723
            • Noll, Braxton et al. “Regulation of MMP9 transcription by ETS1 in immortalized salivary gland epithelial cells of patients with salivary hypofunction and primary Sjögren's syndrome.” Scientific reports vol. 12,1 14552. 25 Aug. 2022, doi:10.1038/s41598-022-18576-z
            • Mossa, Abubakr H et al. “Imbalance of nerve growth factor metabolism in aging women with overactive bladder syndrome.” World journal of urology vol. 39,6 (2021): 2055-2063. doi:10.1007/s00345-020-03422-6
            • Lauwen, Susette et al. “Increased pro-MMP9 plasma levels are associated with neovascular age-related macular degeneration and with the risk allele of rs142450006 near MMP9.” Molecular vision vol. 27 142-150. 2 Apr. 2021
            • Shirakawa, Takuhiro et al. “Dose-Dependent Inhibitory Effect of Rosuvastatin in Japanese Patients with Acute Myocardial Infarction on Serum Concentration of Matrix Metalloproteinases-INVITATION Trial.” Journal of atherosclerosis and thrombosis vol. 29,2 (2022): 229-241. doi:10.5551/jat.59477
            • Ringland, Charis et al. “Apolipoprotein E isoforms differentially regulate matrix metallopeptidase 9 function in Alzheimer's disease.” Neurobiology of aging vol. 95 (2020): 56-68. doi:10.1016/j.neurobiolaging.2020.06.018
            • Wu, Wen-Chi et al. “Do different bariatric surgical procedures influence plasma levels of matrix metalloproteinase-2, -7, and -9 among patients with type 2 diabetes mellitus?.” World journal of diabetes vol. 11,6 (2020): 252-260. doi:10.4239/wjd.v11.i6.252
            • Oishi, Masahiro et al. “Aquaporin 1 elicits cell motility and coordinates vascular bed formation by downregulating thrombospondin type-1 domain-containing 7A in glioblastoma.” Cancer medicine vol. 9,11 (2020): 3904-3917. doi:10.1002/cam4.3032
            • Rodríguez-Sánchez, Elena et al. “Variations in Circulating Active MMP-9 Levels During Renal Replacement Therapy.” Biomolecules vol. 10,4 505. 26 Mar. 2020, doi:10.3390/biom10040505
            • García-Prieto, Concha F et al. “Beneficial Effect of Bariatric Surgery on Abnormal MMP-9 and AMPK Activities: Potential Markers of Obesity-Related CV Risk.” Frontiers in physiology vol. 10 553. 8 May. 2019, doi:10.3389/fphys.2019.00553
            • Ruan, Jun Shan et al. “Ursolic Acid Attenuates TGF-β1-Induced Epithelial-Mesenchymal Transition in NSCLC by Targeting Integrin αVβ5/MMPs Signaling.” Oncology research vol. 27,5 (2019): 593-600. doi:10.3727/096504017X15051723858706
            • Kawashima, Keisuke et al. “CD151 confers metastatic potential to clear cell sarcoma of the soft tissue in animal model.” Oncology letters vol. 17,6 (2019): 4811-4818. doi:10.3892/ol.2019.10164
            • Mori, Kazunori et al. “A mitochondrial ROS pathway controls matrix metalloproteinase 9 levels and invasive properties in RAS-activated cancer cells.” The FEBS journal vol. 286,3 (2019): 459-478. doi:10.1111/febs.14671


            Ilex Life Sciences LLC is an official distributor of QuickZyme Biosciences.