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QuickZyme Human MMP-14 Activity Assay Kit 96-Assays

  • Regulatory status:RUO
  • Type:ELISA
  • Other names:Matrix metalloproteinase-14, MMP14, MMP-X1, Membrane-type matrix metalloproteinase 1, MT-MMP 1, MTMMP1, Membrane-type-1 matrix metalloproteinase, MT1-MMP, MT1MMP
  • Species:Human
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New QZBMMP14H 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

ELISA

Description

The QuickZyme human MMP-14 activity assay enables you to specifically measure active human MMP-14. It can be used for the measurement of MMP-14 activity in various biological samples, such as cultured cells and tissue homogenates.

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 amplification step provides a unique assay sensitivity.

Applications

Tissue extract, Tissue homogenates, Cells/cell extracts

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

0.5 ng/ml (2 h incubation)

0.1 ng/ml (5 h incubation)

Summary

Features

  • Measures endogenous active MMP-14 / MT1-MMP (naturally occurring) in complex biological samples.

  • Samples: cell extracts, tissue homogenates, tissue extracts.

  • Quantitative.

  • Range: 0.1 to 16 ng/ml

  • Sensitivity: 0.5 ng/ml (2 h incubation with detection reagent); 0.1 ng/ml (5 h incubation with detection reagent).

  • Ease-of-use: Equivalent to ELISA.

Research topic

Bone and cartilage metabolism, Energy metabolism and body weight regulation, Extracellular matrix, Oncology, Pulmonary diseases

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, matrix metalloproteinases 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- 14 (EC 3.4.24.80), also known as MT- MMP or MT1-MMP, is a membrane type MMP and contains a transmembrane domain. MMP-14 has a role in the activation of the proforms of MMP-2 and MMP-13. MMP-14 is believed to be involved in bone and tooth development, tumor cell invasion and cell migration and also in shedding of a variety of cell surface proteins. Furthermore, MMP-14 is able to directly degrade certain matrix proteins such as laminin, fibronectin, vitronectin and interstitial collagens. Recent work points to an involvement of MMP-14 in plaque vulnerability. Human MMP-14 consists of 562 amino acid residues including a propeptide of 91 residues and is most likely intracellularly activated by furin-like enzymes and transported to the membrane as an active enzyme. MMP-14 is thought to be released from the cell membrane by proteolytic cleavage. The activity is dependent on Zn2+ and Ca2+.

MMP-14 has have been shown to correlate with a variety of physiological functions and tumor-related behaviors such as migration, invasion, metastasis, basement membrane remodeling, and angiogenesis. MMP-14 is overexpressed in most human cancer, and the published studies have demonstrated that overexpression of MMP-14 in various cancers is associated with poor prognosis. It was found that microRNA miR-181a-5p inhibits cancer cell migration and angiogenesis via downregulation of MMP-14, suggesting that miR-181a-5p could serve as a potential prognostic biomarker and molecular target for the prevention of cancer metastasis. Further, it has been demonstrated that interleukin-6 (IL-6) increases MMP-14 levels via down-regulation of p53 to drive cancer progression.

MMP-14 is the predominant pericellular collagenase in adipose tissue. Its mRNA levels are upregulated during obesity, along with many other MMPs. Loss-of-function of MMP14 leads to impaired adipose tissue formation, eventually leading to severe lipodystrophy in mice. A genetic variant in the human MMP14 gene has been found to be linked to obesity and diabetes. Together, these findings demonstrate a key role of MMP14 in physiological/pathological remodeling of adipose tissue.

MMP-14 has a pivotal role in adult collagen homeostasis, and inhibition of its expression and activity may contribute to pathogenesis of fibrosis. The pathogenic role MMP-14 has been investigated with respect to fibrotic disease of the skin, liver, lungs, and others.

Summary References (19)

References to MMP-14

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  • Chun TH, Hotary KB, Sabeh F, Saltiel AR, Allen ED, Weiss SJ. A pericellular collagenase directs the 3-dimensional development of white adipose tissue. Cell. 2006 May 5;125(3):577-91. doi: 10.1016/j.cell.2006.02.050. PMID: 16678100. See more on PubMed
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  • Zhou X, Hovell CJ, Pawley S, Hutchings MI, Arthur MJ, Iredale JP, Benyon RC. Expression of matrix metalloproteinase-2 and -14 persists during early resolution of experimental liver fibrosis and might contribute to fibrolysis. Liver Int. 2004 Oct;24(5):492-501. doi: 10.1111/j.1478-3231.2004.0946.x. PMID: 15482348. See more on PubMed
  • Zigrino P, Brinckmann J, Niehoff A, Lu Y, Giebeler N, Eckes B, Kadler KE, Mauch C. Fibroblast-Derived MMP-14 Regulates Collagen Homeostasis in Adult Skin. J Invest Dermatol. 2016 Aug;136(8):1575-1583. doi: 10.1016/j.jid.2016.03.036. Epub 2016 Apr 9. PMID: 27066886; PMCID: PMC4946792. See more on PubMed
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