MMP14

  • Official Full Name

    matrix metallopeptidase 14 (membrane-inserted)

  • Overview

    Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion. [provided by RefSeq, Jul 2008]
  • Synonyms

    MMP14; matrix metallopeptidase 14 (membrane-inserted); MMP-14; MMP-X1; MT-MMP; MT1MMP; MTMMP1; WNCHRS; MT1-MMP; MT-MMP 1; matrix metalloproteinase-14; membrane type 1 metalloprotease; membrane-type-1 matrix metalloproteinase; 1;

  • Recombinant Proteins
  • Cell & Tissue Lysates
  • Protein Pre-coupled Magnetic Beads
  • Assay Kits
  • Homo sapiens (Human)
  • Human
  • Mouse
  • Mus musculus (Mouse)
  • Rat
  • Rhesus Macaque
  • Rhesus monkey
  • E.coli
  • E.coli expression system
  • HEK293
  • HEK293T
  • In Vitro Cell Free System
  • Mammalian Cell
  • Mammalian cells
  • Wheat Germ
  • Flag
  • GST
  • His
  • His (Fc)
  • Avi
  • SUMO
  • Myc
  • DDK
  • Myc|DDK
  • N/A
  • N
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human MMP14-162H Active Recombinant Human MMP14 Mammalian Cell N/A
Human MMP14-161H Active Recombinant Human MMP14, His-tagged Mammalian cells His
Human MMP14-808H Active Recombinant Human MMP14 E.coli N/A
Human MMP14-1837H Active Recombinant Human MMP14 protein E.coli N/A
Human MMP14-38H Active Recombinant Human MMP14, His-tagged Mammalian cells His
Human MMP14-39H Active Recombinant Human MMP14, His-tagged E.coli His
Human MMP14-160H Recombinant Human MMP14(Membrane-inserted), Catalytic Domain E.coli N/A
Human MMP14-812H Recombinant Human MMP14, Hemopexin Domain, His-tagged E.coli His
Human MMP14-571H Recombinant Human MMP14 Protein, MYC/DDK-tagged HEK293 Myc/DDK
Human MMP14-4279HCL Recombinant Human MMP14 293 Cell Lysate HEK293 N/A
Human MMP14-5423H Recombinant Human MMP14 Protein, GST-tagged Wheat Germ GST
Human MMP14-3233H Recombinant Human MMP14 protein, His-SUMO-tagged E.coli His-SUMO 112-582aa
Human MMP14-84H Recombinant Human MMP14 protein E.coli N/A 264
Human MMP14-181H Recombinant Human MMP14 Protein, His-tagged E.coli His Tyr112~Gly321
Human MMP14-6464HF Recombinant Full Length Human MMP14 Protein, GST-tagged In Vitro Cell Free System GST 582 amino acids
Human MMP14-1787HFL Recombinant Full Length Human MMP14 Protein, C-Flag-tagged Mammalian cells Flag
Human MMP14-657H Recombinant Human MMP14 protein, His-tagged E.coli His 520aa
Human MMP14-1418H-B Recombinant Human MMP14 Protein Pre-coupled Magnetic Beads HEK293
Human MMP14-4576H Recombinant Human MMP14 Protein (Pro316-Gly511), N-His tagged E.coli N-His Pro316-Gly511
Human MMP14-1418H Recombinant Human MMP14 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Mouse Mmp14-9911M Recombinant Mouse Mmp14 protein, His-tagged E.coli His aa 112-582
Mouse MMP14-9909M Recombinant Mouse MMP14 Protein Mammalian Cell His
Mouse Mmp14-183M Recombinant Mouse Mmp14 Protein, His-tagged E.coli His His121~Asn487
Mouse MMP14-5599M Recombinant Mouse MMP14 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Mouse MMP14-5599M-B Recombinant Mouse MMP14 Protein Pre-coupled Magnetic Beads HEK293
Mouse Mmp14-4098M Recombinant Mouse Mmp14 Protein, Myc/DDK-tagged HEK293T Myc/DDK
Rat MMP14-3713R Recombinant Rat MMP14 Protein Mammalian Cell His
Rat MMP14-3369R Recombinant Rat MMP14 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Rat MMP14-3369R-B Recombinant Rat MMP14 Protein Pre-coupled Magnetic Beads HEK293
Rhesus monkey MMP14-3296R Recombinant Rhesus monkey MMP14 protein, His-tagged E.coli His Tyr112~Gly321
Homo sapiens (Human) RFL21414HF Recombinant Full Length Human Matrix Metalloproteinase-14(Mmp14) Protein, His-Tagged E.coli expression system His Full Length of Mature Protein (112-582)
Mus musculus (Mouse) RFL2938MF Recombinant Full Length Mouse Matrix Metalloproteinase-14(Mmp14) Protein, His-Tagged E.coli expression system His Full Length of Mature Protein (112-582)
Rhesus Macaque MMP14-2790R Recombinant Rhesus monkey MMP14 Protein, His-tagged Mammalian Cell His
Rhesus Macaque MMP14-2611R Recombinant Rhesus Macaque MMP14 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Rhesus Macaque MMP14-2611R-B Recombinant Rhesus Macaque MMP14 Protein Pre-coupled Magnetic Beads HEK293
Kit-2123 MMP-14 Inhibitor Screening Kit N/A
  • Background
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  • Case Study
  • Involved Pathway
  • Protein Function
  • Interacting Protein
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MMP14-9.jpg

Fig1. The enzymatic activity of MMP-14 is subject to complex regulation.

What is MMP14 protein?

MMP14 (matrix metallopeptidase 14) gene is a protein coding gene which situated on the long arm of chromosome 14 at locus 14q11. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. The MMP14 protein is consisted of 582 amino acids and its molecular mass is approximately 65.9 kDa.

What is the function of MMP14 protein?

MMP14 is also known as membrane matrix metalloproteinase-1 (MT1-MMP). MMP14 is an endopeptidase that degrades various components of the extracellular matrix such as collagen. It is essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. It may be involved in actin cytoskeleton reorganization by cleaving PTK7 and acts as a positive regulator of cell growth and migration via activation of MMP15. And MMP14 is also involved in the formation of the fibrovascular tissues in association with pro-MMP2.

MMP14 Related Signaling Pathway

The biological process involved in MMP14 mainly include extracellular matrix degradation, tumor invasion and development, angiogenesis, and inflammatory response. In addition, MMP14 also plays an important role in the regulation of T cell function, and its expression level is closely related to T cell activation and function. Some signaling pathways are related with MMP14 including TGF-β signaling pathway, Wnt/β-catenin signaling pathway, FAK/PI3K/Akt signaling pathway, etc.

MMP14-10.jpg

Fig2. Probable mechanisms underlying the chloride intracellular channel proteins (CLICs)-mediated suppression of tumor cell invasion and metastasis. In the secretory granules, CLIC2 binds to MMP14 and inhibits the localization of MMP14 in the plasma membrane.

MMP14 Related Diseases

MP14 plays an important role in the development and metastasis of tumors. The abnormal expression of MMP14 may lead to enhanced invasion and metastasis of tumor cells. It also plays a key role in the inflammatory response, participating in the degradation of joint tissues and the inflammatory response. Overactivation of MMP14 is involved in the destruction of artery walls and the formation of atherosclerosis.

Bioapplications of MMP14

MMP14 can be used as a drug target to develop inhibitors against MMP14, and its high expression can be used as a diagnostic marker and prognostic evaluation indicator for some tumors. Some of the inhibitors in development may also be used to treat related diseases.

Case study 1: Chen Xu, 2023

Extracellular vesicles derived from bone marrow mesenchymal stem cells (BMSC-EVs) are emerged as carriers of therapeutic targets against bone disorders, yet its isolation and purification are limited with recent techniques. Magnetic nanoparticles (MNPs) can load EVs with a unique targeted drug delivery system. Gold-coated magnetic nanoparticles (GMNPs) were constructed by decorating the surface of the Fe3O4@SiO2 core and a silica shell with poly(ethylene glycol) (PEG)-aldehyde (CHO) and the researchers examined the role of BMSC-EVs loaded on GMNPs in diabetic osteoporosis (DO). DO models were then established in Sprague-Dawley rats. GMNPE was prepared by combining GMNPs with anti-CD63, after which osteoblasts were co-cultured with the GMNPE-BMSC-EVs. BMSC-EVs delivered miR-150-5p to osteoblasts, where miR-150-5p targeted MMP14 and consequently activated Wnt/β-catenin pathway, resulting in promotion of osteogenesis.

MMP14-3.jpg

Fig1. Immunoblotting of MMP14 protein in the bone tissues of normal and DO rats.

MMP14-4.jpg
Fig2. Osteoblast viability in the presence of with miR-150-5p mimic alone or combined with oe-MMP14 measured by CCK-8 assay.

Case study 2: Ensieh M Poursani, 2023

Metastatic cancer cells exploit Epithelial-mesenchymal-transition (EMT) to enhance their migration, invasion, and resistance to treatments. Clinical trials using copper chelators are associated with improved patient survival; however, the molecular mechanisms by which copper depletion inhibits tumor progression and metastasis are poorly understood. This article proposes that copper chelation inhibits metastasis by reducing TGF-β levels and EMT signaling and hypothesized that copper chelation therapy might be a less toxic alternative to target the TGF-β/EMT axis. To validate this hypothesis, the researchers performed single-cell imaging, protein assays, and in vivo studies. Mechanistically, TEPA significantly downregulated canonical (TGF-β/SMAD2&3) and non-canonical (TGF-β/PI3K/AKT, TGF-β/RAS/RAF/MEK/ERK, and TGF-β/WNT/β-catenin) TGF-β signaling pathways. Additionally, EMT markers of MMP-9, MMP-14, Vimentin, β-catenin, ZEB1, and p-SMAD2 were downregulated. This study suggests that copper chelation therapy represents a potentially effective therapeutic approach for targeting TGF-β and inhibiting EMT in a diverse range of cancers.

MMP14-5.jpg

Fig3. Analysis of MMP-9, MMP-14, and vimentin at protein levels.

MMP14-6.jpg
Fig4. Molecular mechanism of tumor suppression by copper chelator therapy.
MMP14-8.jpg

Fig2. Schematic diagram of the mechanism by which BMSC-EV-loaded GMNPs affect the progression of DO. (Chen Xu, 2023)

MMP14 involved in several pathways and played different roles in them. We selected most pathways MMP14 participated on our site, such as TNF signaling pathway, GnRH signaling pathway, which may be useful for your reference. Also, other proteins which involved in the same pathway with MMP14 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

Pathway Name Pathway Related Protein
TNF signaling pathwayFOS;MAP3K7IP3;MAP2K4;MAPK10;IL1B;MAP2K1;IL6;MMP3;CXCL10
GnRH signaling pathwayPLCB1;GNRHR;MAPK11;ADCY1B;MAPK10;CAMK2D;CALML3;CALM2B;PRKCB

MMP14 has several biochemical functions, for example, calcium ion binding, integrin binding, metalloendopeptidase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by MMP14 itself. We selected most functions MMP14 had, and list some proteins which have the same functions with MMP14. You can find most of the proteins on our site.

Function Related Protein
calcium ion bindingTBC1D8B;EFCAB9;PRSS3;EPDL1;PCDHB12;LALBA;S100A4;TC2N;PLCB1
integrin bindingICAM3;KDR;ILK;LYN;TGFBI;VCAM1;CD9;SFRP2;ECM2
metalloendopeptidase activityADAMTS5;MMP12;ADAM28;ADAM30;MMP3;ADAM10B;MEP1A;ADAMTS20;UQCRC2A
peptidase activator activityMMP14;FBLN1;PSME4;APP;CAV1;FN1;PSME4B;PCOLCE;CLPX
protein bindingTRIM54;BCL6;HDDC3;CTDSP1;NR2F1;SPSB1;C4BP;YES1;ASB3
zinc ion bindingRNF125;RP9;SNCA;ZMIZ2;RABGEF1;MARCH10;BRPF3;APOBEC1;DZIP3

MMP14 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with MMP14 here. Most of them are supplied by our site. Hope this information will be useful for your research of MMP14.

ADI1; Gorasp2; LUM

Gene Family

MMPs

Research Area

Related articles

Oh, G; Yoo, SW; et al. Intravital imaging of mouse colonic adenoma using MMP-based molecular probes with multi-channel fluorescence endoscopy. BIOMEDICAL OPTICS EXPRESS 5:1677-1689(2014).
Ali, G; Borrelli, N; et al. Differential Expression of Extracellular Matrix Constituents and Cell Adhesion Molecules between Malignant Pleural Mesothelioma and Mesothelial Hyperplasia. JOURNAL OF THORACIC ONCOLOGY 8:1389-1395(2013).
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06/06/2018

    The versatility of this reagent is evident in its capacity to cater to a plethora of sample types, offering a broad array of potential applications.

    07/17/2017

      Backed by its user-friendly nature, this protein reagent saves me considerable time and effort, making it highly suitable for fast-paced laboratory work.

      04/26/2017

        Brimming with enchantment, this experimental reagent illuminates your scientific odyssey.

        Q&As (7)

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        What is the cellular source of MMP14 and how is its expression regulated? 06/05/2022

        MMP14, also known as matrix metalloproteinase 14, is primarily expressed by cells of mesenchymal origin, such as fibroblasts and endothelial cells. Its expression is tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms. Transcriptional regulation involves the binding of various transcription factors, such as AP-1 and SP-1, to the MMP14 promoter region. Additionally, microRNAs and RNA-binding proteins can modulate its mRNA stability and translation.

        What is the role of MMP14 in cancer progression and metastasis? 03/29/2021

        MMP14 plays a crucial role in cancer progression and metastasis. It facilitates tumor invasion by degrading components of the extracellular matrix, promoting cancer cell migration, and aiding in angiogenesis. MMP14 also influences tumor cell behavior by interacting with other proteins involved in cell signaling pathways and epithelial-mesenchymal transition. Its overexpression is associated with poor prognosis in various types of cancer.

        How is overexpression of MMP14 associated with tumor progression? 05/24/2020

        Overexpression of MMP14 has been strongly associated with tumor progression and poor prognosis in various types of cancer. Increased levels of MMP14 lead to enhanced degradation of the ECM, promoting tumor cell invasion and metastasis. Additionally, MMP14 can activate other matrix metalloproteinases (MMPs), further amplifying the proteolytic activity and facilitating tumor growth and angiogenesis. Moreover, MMP14 has been implicated in tumor-associated angiogenesis and immunosuppression, contributing to tumor progression and metastasis.

        Can MMP14 be targeted for therapeutic interventions? 12/10/2019

        Targeting MMP14 holds potential for therapeutic interventions in cancer and other diseases. Strategies such as selective inhibition of MMP14 activity, antibody-based therapies, and gene silencing techniques are being explored. However, the development of MMP14-targeted therapies faces challenges, including the need for specificity, avoiding off-target effects, and optimizing delivery methods to reach the tumor microenvironment.

        Are there any known endogenous inhibitors of MMP14? 03/25/2017

        Yes, there are endogenous inhibitors of MMP14, known as tissue inhibitors of metalloproteinases (TIMPs). TIMPs bind to the active site of MMP14 and prevent its activity. TIMP-2 is a specific inhibitor of MMP14 and forms a complex with MMP14, regulating its enzymatic activity. The balance between MMP14 and TIMPs is crucial for maintaining tissue homeostasis and preventing excessive extracellular matrix degradation. Dysregulation of this balance can contribute to pathological conditions, including cancer progression.

        What are the physiological functions of MMP14 in tissue remodeling? 08/29/2016

        MMP14 plays a crucial role in tissue remodeling processes, such as embryogenesis, wound healing, and tissue repair. It is essential for the degradation and turnover of extracellular matrix components during tissue restructuring. MMP14 also influences cell behavior and migration during tissue development and regeneration. Additionally, it participates in the modulation of immune responses and angiogenesis, which are crucial for proper tissue remodeling.

        How does MMP14 interact with its substrates? 07/09/2016

        MMP14 possesses a catalytic domain responsible for substrate cleavage. It predominantly cleaves components of the extracellular matrix, such as collagen type I and type II. The interaction between MMP14 and its substrates occurs through specific binding sites within the substrate proteins. This interaction is facilitated by the hemopexin-like domain of MMP14, which acts as a docking site for substrate recognition and binding.

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