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QuickZyme Human MMP-7 Activity Assay Kit 96-Assays

  • Regulatory status:RUO
  • Type:ELISA
  • Other names:Matrix metalloproteinase-7
  • Species:Human
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New QZMMMP7H 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

ELISA

Description

The QuickZyme human MMP-7 activity assay enables you to specifically measure in biological samples both active human MMP-7, as well as pro-MMP-7, which is activated on the plate by APMA. It can be used for the quantification of MMP-7 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.

Applications

Serum, Urine, Tissue homogenates, Cell culture conditioned medium

Sample Requirements

10 - 100 μl

Shipping

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

Storage/Expiration

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 - 16 ng/ml

Limit of Detection

0.03 ng/ml (3 hr incubation)

0.009 ng/ml (6 hr incubation)

0.004 ng/ml (25 h incubation)

Summary

Research topic

Bone and cartilage metabolism, Extracellular matrix, Immune Response, Infection and Inflammation, Oncology, Others, Pulmonary diseases, Renal disease

Summary

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases responsible for cleaving protein substrates, with the most commonly identified substrates being extracellular matrix (ECM) proteins. MMPs are involved in normal physiological processes, such embryogenesis, organogenesis during development, reproduction tissue resorption, wound healing and tissue remodeling. They also play a role in a number of pathological processes such as inflammation, arthritis, cardiovascular diseases, fibrosis and cancer.

In addition to modulating the components of the extracellular connective tissue, MMPs also regulate cell proliferation, differentiation, migration, apoptosis, and vessel regeneration indirectly by cleaving and activating vital molecules that control cell function, or directly by binding to cell surface molecules that trigger activation of intracellular pathways.

Regulation of MMPs is carried out at various levels. Expression of latent MMPs is regulated at the level of transcription, whereas the proteolytic activity is controlled by specific activation of proMMPs, and by MMP-specific inhibitors, the tissue inhibitors of metalloproteinases (TIMPs), or general circulatory inhibitors, such as α2macroglobulin. The MMPs can be grouped according to their domain structure into collagenases, gelatinases, stromelysins, membrane type MMPs and matrilysins.

MMP-7 (also known as matrilysin, matrilysin 1 or pump 1; EC 3.4.24.23) has a broad range of substrate specificity including collagen type IV, elastin, fibronectin, laminin, nidogen, tenascin, osteonectin, MBP, decorin and versican). Human MMP-7 has a Mw of 29 kDa (pro-form) and 19 kDa (active form). The activity is dependent on Zn2+ and Ca2+ . proMMP-7, can be activated in vitro by organo mercurial compounds such as p-aminophenyl mercuric acetate (APMA). MMP-7 is produced by a variety of cell types including osteoclasts, keratinocytes epithelial cells and macrophages.

MMP-7 plays a crucial role in a diverse array of cellular processes and appears to be a key regulator of fibrosis in several diseases, including pulmonary fibrosis, liver fibrosis, kidney fibrosis, and cystic fibrosis. For example, MMP-7 levels are increased in patients with idiopathic pulmonary fibrosis (IPF), and research suggests that MMP-7 could potentially be a reliable prognostic marker of IPF at time of diagnosis and one that can predict the deterioration of lung function during the follow-up period. Furthermore, research has found that urinary MMP-7 levels are elevated in human chronic kidney disease (CKD) and correlate with kidney fibrosis; thus, MMP-7 could potentially serve as a noninvasive biomarker of kidney fibrosis. It was also discovered that, in mice, pharmacologic inhibition of MMP-7 attenuates renal fibrosis in vivo, suggesting that MMP-7 is a novel therapeutic target as well, and its inhibition confers renal protection against development of kidney fibrosis.

Elevated MMP-7 expression has been observed in numerous cancers. MMP-7 appears to act as an oncogene in cervical cancer cells and is involved in cell proliferation, migration, and invasion. MMP-7 expression has been found to be significantly higher in the tissue and serum of cervical cancer patients compared to healthy individuals and has been correlated with increased pathological grade, clinical stage, and lymph metastasis. This suggests that MMP-7 may be a clinically relevant biomarker for cervical cancer. Similarly, others studies have found that MMP-9 is a potential prognostic factor for ovarian cancer and could be a novel treatment target in ovarian cancer patients.

Summary References (8)

References to MMP-7

  • Bauer Y, White ES, de Bernard S, Cornelisse P, Leconte I, Morganti A, Roux S, Nayler O. MMP-7 is a predictive biomarker of disease progression in patients with idiopathic pulmonary fibrosis. ERJ Open Res. 2017 Mar 22;3(1):00074-2016. doi: 10.1183/23120541.00074-2016. PMID: 28435843; PMCID: PMC5395293. See more on PubMed
  • Clark IM, Swingler TE, Sampieri CL, Edwards DR. The regulation of matrix metalloproteinases and their inhibitors. Int J Biochem Cell Biol. 2008;40(6-7):1362-78. doi: 10.1016/j.biocel.2007.12.006. Epub 2007 Dec 24. PMID: 18258475. See more on PubMed
  • DeCoux A, Lindsey ML, Villarreal F, Garcia RA, Schulz R. Myocardial matrix metalloproteinase-2: inside out and upside down. J Mol Cell Cardiol. 2014 Dec;77:64-72. doi: 10.1016/j.yjmcc.2014.09.016. Epub 2014 Sep 28. PMID: 25261607; PMCID: PMC4312173. See more on PubMed
  • Hu X, Li D, Zhang W, Zhou J, Tang B, Li L. Matrix metalloproteinase-9 expression correlates with prognosis and involved in ovarian cancer cell invasion. Arch Gynecol Obstet. 2012 Dec;286(6):1537-43. doi: 10.1007/s00404-012-2456-6. Epub 2012 Jul 26. PMID: 22832979. See more on PubMed
  • Chen Q, Jin M, Yang F, Zhu J, Xiao Q, Zhang L. Matrix metalloproteinases: inflammatory regulators of cell behaviors in vascular formation and remodeling. Mediators Inflamm. 2013;2013:928315. doi: 10.1155/2013/928315. Epub 2013 Jun 12. PMID: 23840100; PMCID: PMC3694547. See more on PubMed
  • Ke B, Fan C, Yang L, Fang X. Matrix Metalloproteinases-7 and Kidney Fibrosis. Front Physiol. 2017 Feb 10;8:21. doi: 10.3389/fphys.2017.00021. Erratum in: Front Physiol. 2017 Mar 28;8:192. PMID: 28239354; PMCID: PMC5301013. See more on PubMed
  • Zhou D, Tian Y, Sun L, Zhou L, Xiao L, Tan RJ, Tian J, Fu H, Hou FF, Liu Y. Matrix Metalloproteinase-7 Is a Urinary Biomarker and Pathogenic Mediator of Kidney Fibrosis. J Am Soc Nephrol. 2017 Feb;28(2):598-611. doi: 10.1681/ASN.2016030354. Epub 2016 Sep 13. PMID: 27624489; PMCID: PMC5280025. See more on PubMed
  • Zhu L, Zheng X, Du Y, Xing Y, Xu K, Cui L. Matrix metalloproteinase-7 may serve as a novel biomarker for cervical cancer. Onco Targets Ther. 2018 Jul 20;11:4207-4220. doi: 10.2147/OTT.S160998. PMID: 30050312; PMCID: PMC6055895. See more on PubMed
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