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QuickZyme Human MMP-8 Activity Assay Kit 96-Assays

  • Regulatory status:RUO
  • Type:ELISA
  • Other names:Matrix metalloproteinase-8
  • Species:Human
Cat. No. Size Price

Discount QZBMMP8H 96 wells (1 kit) $1242,89
PubMed Product Details
Technical Data




The QuickZyme human MMP-8 activity assay enables you to specifically measure in biological samples both active human MMP-8, as well as (pro) MMP-8 which is activated on the plate by APMA. It can be used for the measurement of MMP-8 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.


Serum, Urine, Saliva, Plasma, Tissue homogenates, Cell culture conditioned medium

Sample Requirements

10 - 100 μl


On dry ice. Upon receipt, store the product at the temperature recommended below.


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.

Calibration Range

0 - 12 ng/ml

Limit of Detection

100 pg/ml (2 hr incubation)

24 pg/ml (6 hr incubation)

4 pg/ml (24 hr incubation)



  • Measures endogenous active MMP-8 ( naturally occurring ) or total active MMP-8 ( following activation with APMA ).

  • Samples: cell culture conditioned medium, serum, plasma, urine, saliva and tissue homogenates.

  • Quantitative.

  • Range: 10 – 24000 pg/ml.

  • Sensitivity: 100 pg/ml for 2 h incubation with detection reagent; 24 pg/ml for 6 h incubation with detection reagent; 4 pg/ml for 24 h incubation with detection reagent.

  • Ease-of-use: Equivalent to ELISA.

  • Marker for neutrophils (PMN)

Research topic

Atherosclerosis, Cardiovascular disease, Extracellular matrix, Immune Response, Infection and Inflammation, Oncology, Pulmonary diseases


Matrix metalloproteinase-8 (MMP-8; called also neutrophil collagenase or collagenase 2) is a member of matrix metalloproteinase family of zinc- and calcium-dependent endo-peptidases responsible for degradation of extracellular matrix. Matrix metalloproteinases (MMPs) possess catalytic properties responsible for tissue remodeling and degradation of structural components of the extracellular matrix (ECM) including collagens, elastins, gelatin, matrix glycoprotein, and proteoglycans.

MMP-8 was first described (as neutrophil collagenase) in 1990 when it was cloned from neutrophils obtained from a patient with granulocytic leukemia. Later observations found MMP-8 mRNA expression in chondrocytes as well as in human rheumatoid synovial fibroblasts, activated macrophages, smooth muscle cells and endothelial cells. The human MMP-8 gene is located on chromosome 11q22.3, residing in a gene cluster that contains several MMP genes. Its expression is inducible and upregulated by various inflammatory cytokines, such as interleukin-1β, tumour necrosis factor-α, and CD40 ligand. The MMP-8 protein consists of a signal peptide, a propeptide, a catalytic domain, a hinge region, and a hemopexin-like C-terminal domain. The mature MMP-8 enzyme is 64 kDa in size, with glycosylation increasing the size to 75 kDa. Autoproteolytic degradation has been described, yielding a 40-kDa fragment, which retains catalytic activity but does not cleave fibrillar collagen. MMP-8 can be proteolytically activated also by stromelysin-1 (MMP-3), stromelysin-2 (MMP-10) and by matrilysin-1 (MMP-7).

PMN-derived MMP-8 is expressed during the myelocyte stage of development of polymorphonuclear (PMN) precursors in the bone marrow, and it is stored as a latent enzyme (pro-MMP-8) within the specific granules of polymorphonuclear cells. Pro-MMP-8 is rapidly released from activated PMN undergoing degranulation, and is then activated via the cysteine switch mechanism to yield the active form of the enzyme to ensure rapid availability at inflammatory sites. The endogenous MMP inhibitors, TIMPs, can inhibit MMP-8. Therefore, the activity of MMP-8 in a tissue at a given time would be dependent on the relative amounts of its transcriptional stimuli, zymogen activators and enzymatic inhibitors that are present in that tissue at the time.

The best-known substrates of MMP-8 are interstitial collagens (types I-III), the major structural components of the extracellular matrix, among which MMP-8 has higher proteolytic activity on types I and III than type II. In addition, MMP-8 can also cleave nonmatrix proteins such as serpins, bradykinin, angiotensin I, fibrinogen and many other. As a result of its known catalytic activities, MMP-8 is believed to be involved in wound healing and tissue remodeling during inflammation. In addition, MMP-8 has been implicated in the pathogenesis of several chronic inflammatory diseases characterized by excessive influx and activation of polymorphonuclear cell (PMN), including cystic fibrosis, rheumatoid arthritis, chronic skin wounds and periodontal disease.
The number of publications investigating the role of MMPs in periodontal disease has been still growing. The imbalance between MMPs and tissue inhibitors of matrix metalloproteinases (TIMPs) is considered to trigger the degradation of extracellular matrix, basement membrane, and alveolar bone, and thus to initiate periodontal disease. MMP-8 was found to be the most prevalent MMP in diseased periodontal tissue, oral fluid, gingival

crevicular fluid (GCF) and saliva. Moreover, MMP-8 activity correlates with disease severity . Reduction of MMP activity was shown to reduce periodontitis progression. MMP-8 is apparently a major mediator of this aggressive tissue destruction, although one report indicates a protective role for MMP-8 during periodontal infection.

Summary References (21)

References to MMP-8

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  • Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL. Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases. J Biol Chem. 1990 Jul;265(20):11421-4.
  • Cole AA, Chubinskaya S, Schumacher B, et al. Chondrocyte matrix metalloproteinase-8. Human articular chondrocytes express neutrophil collagenase. J Biol Chem. 1996 May;271(18):11023-11026.
  • Hanemaaijer R, Sorsa T, Konttinen YT, et al. Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells. Regulation by tumor necrosis factor-alpha and doxycycline. J Biol Chem. Dec 12 1997;272(50):31504-31509.
  • Herman MP, Sukhova GK, Libby P, et al. Expression of neutrophil collagenase (matrix metalloproteinase-8) in human atheroma: a novel collagenolytic pathway suggested by transcriptional profiling. Circulation. Oct 16 2001;104(16):1899-1904.
  • Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol. Mar 2007;8(3):221-233.
  • Knäuper V, Wilhelm SM, Seperack PK, DeClerck YA, Langley KE, Osthues A, Tschesche H. Direct activation of human neutrophil procollagenase by recombinant stromelysin. Biochem J. 1993 Oct 15;295 (Pt 2):581-6.
  • Knäuper V, Murphy G, Tschesche H. Activation of human neutrophil procollagenase by stromelysin 2. Eur J Biochem. 1996 Jan 15;235(1-2):187-91.
  • Dozier S, Escobar GP, Lindsey ML. Matrix metalloproteinase (MMP)-7 activates MMP-8 but not MMP-13. Med Chem. 2006 Sep;2(5):523-6.
  • Owen CA, Hu Z, Lopez-Otin C, Shapiro SD. Membrane-bound matrix metalloproteinase-8 on activated polymorphonuclear cells is a potent, tissue inhibitor of metalloproteinase-resistant collagenase and serpinase. J Immunol. Jun 15 2004;172(12):7791-7803.
  • Nagase H, Visse R, Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res. Feb 15 2006;69(3):562-573.
  • Van Lint P, Libert C. Matrix metalloproteinase-8: cleavage can be decisive. Cytokine Growth Factor Rev. Aug 2006;17(4):217-223.
  • Sorsa T, Tjäderhane L, Salo T. Matrix metalloproteinases (MMPs) in oral diseases. Oral Dis. 2004 Nov;10(6):311-8.
  • Dejonckheere E, Vandenbroucke RE, Libert C. Matrix metalloproteinase8 has a central role in inflammatory disorders and cancer progression. Cytokine Growth Factor Rev. 2011 Apr;22(2):73-81.
  • Kuula H, Salo T, Pirilä E, Tuomainen AM, Jauhiainen M, Uitto VJ, Tjäderhane L, Pussinen PJ, Sorsa T. Local and systemic responses in matrix metalloproteinase 8-deficient mice during Porphyromonas gingivalis-induced periodontitis. Infect Immun. 2009 Feb;77(2):850-9.
  • Kato R, Momiyama Y, Ohmori R, Taniguchi H, Nakamura H, Ohsuzu F. Plasma matrix metalloproteinase-8 concentrations are associated with the presence and severity of coronary artery disease. Circ J. 2005 Sep;69(9):1035-40.
  • Vernooy JH, Lindeman JH, Jacobs JA, Hanemaaijer R, Wouters EF. Increased activity of matrix metalloproteinase-8 and matrix metalloproteinase-9 in induced sputum from patients with COPD. Chest. 2004 Dec;126(6):1802-10.
  • Thrailkill K, Cockrell G, Simpson P, Moreau C, Fowlkes J, Bunn RC. Physiological matrix metalloproteinase (MMP) concentrations: comparison of serum and plasma specimens. Clin Chem Lab Med. 2006;44(4):503-4.
  • Jung K. Matrix metalloproteinase-8 and tissue inhibitor of metalloproteinase-1 in serum do not reflect the analytes circulating in blood. Arterioscler Thromb Vasc Biol. 2008 Mar;28(3):e15-6; author reply e17.
  • Jung K, Lein M. By mistakes we learn: determination of matrix metalloproteinase-8 and tissue inhibitor of matrix metalloproteinase-1 in serum yields doubtful results. J Clin Periodontol. 2009 Jan;36(1):34-5; author reply 36-8.
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