MMP3

  • Official Full Name

    matrix metallopeptidase 3 (stromelysin 1, progelatinase)

  • 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. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]
  • Synonyms

    MMP3; matrix metallopeptidase 3 (stromelysin 1, progelatinase); SL-1; STMY; STR1; CHDS6; MMP-3; STMY1; stromelysin-1; transin-1; proteoglycanase; matrix metalloproteinase-3; matrix metalloproteinase 3 (stromelysin 1, progelatinase);

  • Recombinant Proteins
  • Cell & Tissue Lysates
  • Protein Pre-coupled Magnetic Beads
  • Native Proteins
  • Assay Kits
  • Cattle
  • Clostridium histolyticum
  • Human
  • Mouse
  • Pig
  • Rabbit
  • Rat
  • E.coli
  • HEK293
  • HEK293 cells
  • HEK293F
  • HEK293T
  • Human
  • In Vitro Cell Free System
  • Mammalian Cell
  • Mammalian cells
  • Wheat Germ
  • Flag
  • GST
  • His
  • His (Fc)
  • Avi
  • His(C
  • ter)
  • His|T7
  • SUMO
  • Myc
  • DDK
  • Myc|DDK
  • N/A
  • N
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human MMP3-224H Active Recombinant Human MMP3 Protein E.coli N/A
Human MMP3-200H Active Recombinant Human MMP3, His-tagged HEK293 His
Human MMP3-197H Active Recombinant Human MMP3 protein E.coli N/A Tyr18-Thr272
Human MMP3-049H Recombinant Human Matrix Metallopeptidase 3 (stromelysin 1, progelatinase) E.coli N/A
Human MMP3-1383H Recombinant Human Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase), GST-Tagged Human GST
Human MMP3-5080H Recombinant Human MMP3, His-tagged E.coli His
Human MMP3-740H Recombinant Human MMP3 Protein, His-tagged HEK293 His
Human MMP3-163H Recombinant Human MMP3 (Stromelysin 1, Progelatinase), Inactive, Catalytic Domain E.coli N/A
Human MMP3-479H Recombinant Human matrix metallopeptidase 3 (stromelysin 1, progelatinase), His-tagged E.coli His
Human MMP3-28202TH Recombinant Human MMP3, His-tagged His
Human MMP3-39H Recombinant Human MMP3 E.coli N/A
Human MMP3-555H Recombinant Human MMP3 Protein, MYC/DDK-tagged HEK293 Myc/DDK
Human MMP3-152H Recombinant Human Matrix Metallopeptidase 3, Catalytic Domain E.coli N/A
Human MMP3-4273HCL Recombinant Human MMP3 293 Cell Lysate HEK293 N/A
Human MMP3-5433H Recombinant Human MMP3 Protein, GST-tagged Wheat Germ GST
Human MMP3-1420H-B Recombinant Human MMP3 Protein Pre-coupled Magnetic Beads HEK293
Human MMP3-780H Recombinant Human MMP3 Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293T Myc/DDK
Human MMP3-2450H Recombinant Human MMP3 Protein, His-tagged E.coli N-His Arg101-Cys477
Human MMP3-3235H Recombinant Human MMP3 protein, His-SUMO-tagged E.coli His-SUMO 102-477aa
Human MMP3-890HFL Recombinant Full Length Human MMP3 Protein, C-Flag-tagged Mammalian cells Flag
Human MMP3-1123H Recombinant Human MMP3 Protein, His-tagged HEK293F N-His Tyr18-Cys477
Human MMP3-0392H Active Recombinant Human MMP3 protein, His-tagged HEK293 His Tyr18-Thr272
Human MMP3-1420H Recombinant Human MMP3 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Human MMP3-2449H Recombinant Human MMP3 Protein, His-tagged E.coli N-His Tyr18-Cys477
Human MMP3-1238H Active Recombinant Human MMP3 protein, His-tagged HEK293 His Tyr18-Cys477
Human MMP3-6279HF Recombinant Full Length Human MMP3 Protein, GST-tagged In Vitro Cell Free System GST 477 amino acids
Human MMP3-1239H Active Recombinant Human MMP3 protein, His-tagged HEK293 His Tyr18-Cys477
Human MMP3-240H Recombinant Human MMP3 Protein, His-tagged(C-ter) HEK293 His(C-ter) Tyr18-Cys477
Human MMP3-0029H Recombinant Human MMP3 Protein HEK293 cells
Mouse Mmp3-416M Active Recombinant Mouse Mmp3 protein Mammalian cells N/A
Mouse MMP3-9924M Recombinant Mouse MMP3 Protein Mammalian Cell His
Mouse Mmp3-743M Recombinant Mouse Mmp3 protein, His & T7-tagged E.coli His/T7 Phe100~Cys477 (Accession # P28862)
Mouse Mmp3-10594M-B Recombinant Mouse Mmp3 Protein Pre-coupled Magnetic Beads HEK293
Mouse Mmp3-10594M Recombinant Mouse Mmp3 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Mouse Mmp3-5318M Recombinant Mouse Mmp3 protein, His-tagged E.coli His 104-477aa
Rat Mmp3-745R Recombinant Rat Mmp3 protein, His-tagged E.coli His Asn278~Gly450
Rat Mmp3-7422R Recombinant Rat Mmp3 protein, His-tagged E.coli N-His 98-475aa
Rabbit MMP3-1124R Recombinant Rabbit MMP3 Protein, His-tagged E.coli N-His Phe101-Cys478
Cattle MMP3-739C Recombinant Cattle MMP3 protein, His & T7-tagged E.coli His/T7 Tyr18~Cys477
Clostridium histolyticum MMP3-26C Collagenase Type 3 Protein N/A
Pig MMP3-744P Recombinant Pig MMP3 protein, His & T7-tagged E.coli His/T7 Tyr18~Cys477 (Accession# F1SV58)
Pig MMP3-1117P Recombinant Pig MMP3 Protein, His-tagged E.coli N-His Tyr18-Cys477
Kit-0589 MMP-3 Activity Assay Kit N/A
Kit-2213 MMP-3 Activity Fluorometric Assay Kit N/A
  • Background
  • Quality Guarantee
  • Case Study
  • Involved Pathway
  • Protein Function
  • Interacting Protein
  • Other Resource

What is MMP3 protein?

MMP3 (matrix metallopeptidase 3) gene is a protein coding gene which situated on the long arm of chromosome 11 at locus 11q22. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. 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. The MMP3 protein is consisted of 477 amino acids and its molecular mass is approximately 54.0 kDa.

What is the function of MMP3 protein?

MMP3, also known as stromelysin 1, is an enzyme that belongs to the matrix metalloproteinases family. MMP3 has a variety of biological functions, mainly involved in tissue remodeling, cell migration, inflammatory response, wound healing and tumor development. MMP3 can degrade various extracellular matrix (ECM) components, such as fibronectin, laminin and proteoglycan. By degrading ECM components, MMP3 provides pathways for cell migration, which is particularly critical in cell migration during development and in white blood cell migration in inflammatory and immune responses. MMP3 plays a role in the inflammatory process by releasing cytokines and chemokines, which attract immune cells to the site of inflammation and participate in the regulation of inflammatory response.

MMP3 Related Signaling Pathway

MMP3 degrades a variety of extracellular matrix components, such as proteoglycans, fibronectin, and collagen, which are essential for cell migration, inflammatory response, wound healing, and tumor cell invasion and metastasis.

In addition, MMP3 can activate or deactivate other MMPs family members, and through this interaction, MMP3 can regulate a broader range of biological activity. For example, it can enhance its degradation of the extracellular matrix by activating MMP-1 and other MMPs. At the same time, MMP3 can also affect signaling pathways for cell proliferation and differentiation by releasing precursor forms of growth factors and cytokines, such as transforming growth factor-β (TGF-β).

ESM1 may affect the proliferation of CRC cells through the PI3K-Akt-mTOR pathway.jpg

Fig1. ESM1 may affect the proliferation of CRC cells through the PI3K/Akt/mTOR pathway. (Liqun Yang, 2023)

MMP3 Related Diseases

MMP3 is a protease capable of degrading various extracellular matrix components. It plays a role in a variety of physiological processes, such as tissue remodeling, wound healing, and embryonic development. However, abnormal expression or activity of MMP3 has also been associated with a variety of diseases, including but not limited to: elevated levels of MMP3 in osteoarthritis and rheumatoid arthritis; MMP3 is up-regulated in a variety of cancers, and it affects tumor growth and spread by promoting tumor cell invasion and metastasis. In addition, MMP3 is also associated with liver diseases, skin diseases, cardiovascular diseases, etc. MMP3 may be involved in the reduction of bone density and the destruction of bone structure in osteoporosis.

Bioapplications of MMP3

MMP3 is considered to be an important biomarker for the early diagnosis of RA, and its concentration in the serum of RA patients is significantly higher than that of normal people. The concentration of MMP3 is closely associated with cartilage damage and bone erosion, so it can be used to monitor the progression of RA. Drug development targeting MMP3 is ongoing, particularly those aimed at inhibiting MMP3 activity to treat related diseases. These drugs may be potentially valuable in the treatment of rheumatoid arthritis and other MMP3-related conditions.

High Purity

SDS-PAGE (MMP3-5433H).jpg

Fig1. SDS-PAGE (MMP3-5433H)

.

SDS-PAGE (MMP3-780H).jpg

Fig2. SDS-PAGE (MMP3-780H)

Case Study 1: Szymon W Manka, 2019

Matrix metalloproteinase-3 (MMP-3) participates in normal extracellular matrix turnover during embryonic development, organ morphogenesis and wound healing, and in tissue-destruction associated with aneurysm, cancer, arthritis and heart failure. Despite its inability to cleave triple-helical collagens, MMP-3 can still bind to them, but the mechanism, location and role of binding are not known. The researchers used the Collagen Toolkits, libraries of triple-helical peptides that embrace the entire helical domains of collagens II and III, to map MMP-3 interaction sites. The enzyme recognises five sites on collagen II and three sites on collagen III. They share a glycine-phenylalanine-hydroxyproline/alanine (GFO/A) motif that is recognised by the enzyme in a context-dependent manner. Neither MMP-3 zymogen (proMMP-3) nor the individual catalytic (Cat) and hemopexin (Hpx) domains of MMP-3 interact with the peptides, revealing cooperative binding of both domains to the triple helix.

Two modelled frontal-binding MMP-3.jpg

Fig1. Two modelled frontal-binding MMP-3:III-40d complexes shown as ribbons in the standard MMP-3 orientation.

Temperature-dependent binding of biotinylated MMP-3.jpg

Fig2. Temperature-dependent binding of biotinylated MMP-3(EA) to collagens I, II and III.

Case Study 2: Chia-Ling Hsieh, 2017

Studies on the aberrant control of extracellular matrices (ECMs) have mainly focused on the role of malignant cells but less on that of stromal fibroblasts during cancer development. Herein, by using paired normal and prostate cancer-associated stromal fibroblasts (CAFs) derived from a coculture cell model and clinical patient samples, demonstrating that although CAFs promoted prostate cancer growth, matrix metalloproteinase-3 (MMP-3) was lower in CAFs but elevated in prostate cancer cells relative to their normal counterparts. Furthermore, hydrogen peroxide was characterized as the central modulator for altered MMP-3 expression in prostate cancer cells and CAFs, but through different regulatory mechanisms. Treatment of CAFs but not prostate cancer cells with hydrogen peroxide directly inhibited mmp-3 promoter activity with concomitant nuclear translocation of nuclear factor-κB (NF-κB), indicating that NF-κB is the downstream pathway for the transcriptional repression of MMP-3 in CAFs. Hydrogen peroxide reduced thrombospondin 2 (an MMP-3 suppressor) expression in prostate cancer cells by upregulating microRNA-128.

Representative digital images of IHC staining of MMP-3.jpg

Fig3. Representative digital images of IHC staining of MMP-3.

Real-time RT-PCR of THBS2 mRNA expression level and ELISA of MMP-3 levels.jpg

Fig4. Real-time RT-PCR of THBS2 mRNA expression level and ELISA of MMP-3 levels in conditioned media of PC3 transfected with miRNA mimics or inhibitors.

MMP3 involved in several pathways and played different roles in them. We selected most pathways MMP3 participated on our site, such as TNF signaling pathway, Transcriptional misregulation in cancer, Rheumatoid arthritis, which may be useful for your reference. Also, other proteins which involved in the same pathway with MMP3 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 pathwayMAP3K14;MAGI2;TRAF2;CXCL10;MAPK12;PIK3R5;MLKL;SOCS3;CXCL1
Transcriptional misregulation in cancerCD86;HIST1H3G;KDM6A;TLX3;RXRB;IGF1;EWSR1;IL3;RUNX2
Rheumatoid arthritisTLR4;TGFB2;ATP6V1D;ATP6V0A1;H2-AA;HLA-DQA1;HLA-DPB1;CCL5;HLA-DQA2

MMP3 has several biochemical functions, for example, calcium ion binding, endopeptidase activity, metalloendopeptidase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by MMP3 itself. We selected most functions MMP3 had, and list some proteins which have the same functions with MMP3. You can find most of the proteins on our site.

Function Related Protein
calcium ion bindingMYLZ3;AIF1;EPDL1;CDH24;PCDH1G11;RCN2;ASPH;CABP1;ANXA13
endopeptidase activityFAP;PSMB1;P4HB;SENP3B;F9;HTRA4;PSEN1;PSMA6B;PSMA3
metalloendopeptidase activityUQCRC1;ADAMTS15;ADAMTS20;MMP13A;ADAM2;ADAM12;ADAM17A;ADAM19;OMA1
protein bindingGAS1;PDHX;PEG10;DNAJB11;PDHB;NR1H4;FAM129A;CST5;TAB1
zinc ion bindingAFG3L2;FAM90A1;GCH2;CPA3;ADAM33;ZDHHC1;SF1;LMO4;TRIM59

MMP3 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 MMP3 here. Most of them are supplied by our site. Hope this information will be useful for your research of MMP3.

MEOX2; TIMP1

Gene Family

MMPs

Research Area

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        Q&As (7)

        Ask a question
        How does MMP3 (Matrix Metalloproteinase 3) facilitate extracellular matrix remodeling? 10/21/2022

        MMP3 breaks down extracellular matrix components, aiding in tissue remodeling and repair.

        What is the impact of MMP3 on cancer metastasis and tumor microenvironment modulation? 07/04/2022

        MMP3 facilitates cancer metastasis by altering the tumor microenvironment and promoting invasion.

        How do alterations in MMP3 expression or activity affect skin aging and the development of dermatological conditions? 10/19/2021

        Changes in MMP3 activity can accelerate skin aging and contribute to dermatological conditions.

        How does MMP3 influence cardiovascular diseases, particularly in atherosclerosis and aneurysm formation? 07/01/2021

        MMP3 influences cardiovascular health by affecting arterial wall remodeling and stability.

        What role does MMP3 play in the progression of arthritis and joint degeneration? 09/03/2019

        MMP3 contributes to arthritis progression by degrading joint cartilage and connective tissues.

        What are the mechanisms by which MMP3 modulates inflammatory responses? 06/13/2019

        MMP3 modulates inflammation, impacting tissue inflammation and repair processes.

        How does MMP3 contribute to wound healing and tissue repair processes? 12/31/2018

        MMP3 plays a role in wound healing by remodeling damaged tissues and aiding in repair.

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