MMP7

  • Official Full Name

    matrix metallopeptidase 7 (matrilysin, uterine)

  • 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. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]
  • Synonyms

    MMP7; matrix metallopeptidase 7 (matrilysin, uterine); MMP-7; MPSL1; PUMP-1; matrilysin; matrin; pump-1 protease; uterine matrilysin; uterine metalloproteinase; matrix metalloproteinase-7; matrix metalloproteinase 7 (matrilysin, uterine); MAT;

  • Recombinant Proteins
  • Cell & Tissue Lysates
  • Native Proteins
  • Protein Pre-coupled Magnetic Beads
  • Cattle
  • Chicken
  • Human
  • Mouse
  • Rat
  • 293F
  • CHO
  • E.coli
  • HEK293
  • Human Cell
  • In Vitro Cell Free System
  • Mammalian Cell
  • Mammalian cells
  • Mouse myeloma cell line NS0
  • Wheat Germ
  • Yeast
  • Fc
  • GST
  • His
  • Avi
  • T7
  • Non
  • N
  • SUMO
  • C
  • TG
  • 8H
  • GGQ
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human MMP7-22H Active Recombinant Human MMP7 protein E.coli Non 173
Human MMP7-01H Active Recombinant Human MMP7 Protein Mouse myeloma cell line NS0
Human MMP7-47H Recombinant Human MMP7 protein, His-tagged E.coli His 95-267
Human MMP7-810H Recombinant Human MMP7, Fc tagged Human Cell Fc Tyr95-Lys267
Human MMP7-94 Recombinant ProMatrix Metalloproteinase-7 E.coli Non
Human MMP7-40H Active Recombinant Human MMP7 E.coli Non
Human MMP7-2883HCL Recombinant Human MMP7 cell lysate Human Cell Non
Human MMP7-49H Recombinant Human MMP7 protein, His-tagged 293F His 250
Human MMP7-28205TH Native Human MMP7 Non
Human MMP7-5435H Recombinant Human MMP7 Protein, GST-tagged Wheat Germ GST
Human MMP7-6280HF Recombinant Full Length Human MMP7 Protein, GST-tagged In Vitro Cell Free System GST 267 amino acids
Human MMP7-395H Recombinant Human MMP7 Protein, GST-tagged E.coli GST 1-100 aa
Human MMP7-48H Recombinant Human MMP7 protein, His-tagged E.coli His 267
Human MMP7-50H Active Recombinant Human MMP7 Protein, TG-8H-GGQ-tagged CHO TG-8H-GGQ Leu18-Lys267
Human MMP7-0504H Active Recombinant Human MMP7 protein, His-tagged HEK293 His Leu18-Lys267
Human MMP7-4565H Recombinant Human MMP7 Protein (Tyr95-Lys267), N-His tagged E.coli His Tyr95-Lys267
Human MMP7-221H Active Recombinant Human MMP7 Protein (Tyr95-Lys276), C-His tagged, Animal-free, Carrier-free E.coli His Tyr95-Lys276
Human MMP7-001H Recombinant Human MMP7 Protein, His-tagged E.coli His 18-267
Human MMP7-222H Recombinant Human MMP7 Protein (Met1-Lys276), C-His tagged, Animal-free, Carrier-free E.coli His Met1-Lys276
Human MMP7-3236H Recombinant Human MMP7 protein, GST-tagged E.coli GST 95-267aa
Human MMP7-2612H Recombinant Human MMP7 protein(18-267 aa), N-SUMO & C-His-tagged E.coli N-SUMO & C-His 18-267 aa
Mouse Mmp7-203M Active Recombinant Mouse Mmp7 Mammalian cells Non Met1-Leu264
Mouse Mmp7-748M Recombinant Mouse Mmp7 protein, His-tagged E.coli His Met1~Leu264
Mouse Mmp7-10595M Recombinant Mouse Mmp7 Protein, His (Fc)-Avi-tagged HEK293 His&Fc&Avi
Mouse Mmp7-10595M-B Recombinant Mouse Mmp7 Protein Pre-coupled Magnetic Beads HEK293
Rat MMP7-3718R Recombinant Rat MMP7 Protein Mammalian Cell His
Rat Mmp7-749R Recombinant Rat Mmp7 protein, His & T7-tagged E.coli His&T7 Met1~Leu267
Rat MMP7-659R Recombinant Rat MMP7 Protein (98-267 aa), GST-tagged E.coli GST 98-267 aa
Rat MMP7-1458R Recombinant Rat MMP7 Protein (98-267 aa), His-tagged Yeast His 98-267 aa
Rat MMP7-3374R-B Recombinant Rat MMP7 Protein Pre-coupled Magnetic Beads HEK293
Rat MMP7-3374R Recombinant Rat MMP7 Protein, His (Fc)-Avi-tagged HEK293 His&Fc&Avi
Cattle MMP7-1126C Recombinant Cattle MMP7 Protein, His&GST-tagged E.coli His&GST Asp29-Lys267
Chicken MMP7-1425C Recombinant Chicken MMP7 Mammalian Cell His
Chicken MMP7-1125C Recombinant Chicken MMP7 Protein, His&GST-tagged E.coli His&GST Phe22-Ser267
  • Background
  • Quality Guarantee
  • Case Study
  • Involved Pathway
  • Protein Function
  • Interacting Protein
  • Other Resource
MMP7-7.jpg

Fig1. MMP-7 roles, structure, function, and inhibition. (Steven R Van Doren, 2022)

What is MMP7 protein?

MMP7 gene (matrix metallopeptidase 7) is a protein coding gene which situated on the long arm of chromosome 11 at locus 11q22. This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). The encoded preproprotein is proteolytically processed to generate the mature protease. This secreted protease breaks down proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal hemopexin domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The MMP7 protein is consisted of 267 amino acids and MMP7 molecular weight is approximately 29.7 kDa.

What is the function of MMP7 protein?

MMP7 protein is a secreted zinc-dependent endopeptidase that plays a role in a variety of biological processes. MMP7 is capable of degrading extracellular matrix and through this degradation plays a regulatory role in physiological processes such as tissue repair, wound healing, bone growth and remodeling. In addition, MMP7 also plays an important role in the pathological process, especially in the occurrence and development of cancer, which can promote the proliferation, differentiation, metastasis and invasion of cancer cells. The expression of MMP7 is associated with clinical features in patients with multiple cancers, and its expression pattern can serve as a novel diagnostic and prognostic biomarker for a variety of human diseases.

MMP7 related signaling pathway

Matrix metalloproteinase-7 (MMP7), also known as matrilysin, belongs to the family of zinc-dependent endopeptidases. It cleaves various ECM components, such as type IV collagen, laminin, and elastin, thereby facilitating cell migration, invasion, and tissue remodeling. MMP7 is upregulated by various signaling pathways, including those involving growth factors like epidermal growth factor (EGF) and cytokines such as tumor necrosis factor-alpha (TNF-α). Its activity is tightly regulated by endogenous inhibitors called tissue inhibitors of metalloproteinases (TIMPs).

MMP7 related diseases

The MMP7 protein plays an important role in the occurrence and development of many diseases. The expression level of MMP7 is elevated in many types of cancer, including lung cancer, stomach cancer, colorectal cancer, esophageal cancer, bladder cancer, ovarian cancer, breast cancer, liver cancer, etc., and its expression is closely related to tumor invasiveness, metastasis and prognosis. MMP7 is involved in tumor progression by promoting the proliferation, differentiation, migration and invasion of tumor cells. In addition, MMP7 also plays a role in non-neoplastic diseases such as chronic kidney disease and idiopathic pulmonary fibrosis (IPF), and its abnormal expression may lead to tissue damage and fibrosis.

Bioapplications of MMP7

By harnessing its ability to degrade extracellular matrix (ECM) components, rhMMP7 can facilitate the development of novel treatments for conditions characterized by excessive ECM deposition, such as fibrotic diseases and atherosclerosis. In oncology, rhMMP7 holds potential as a therapeutic agent to enhance drug delivery across biological barriers or as a targeted therapy for cancers overexpressing specific MMP7 receptors. Additionally, due to its role in ECM remodeling, rhMMP7 can be utilized in regenerative medicine to promote wound healing and tissue engineering applications. Furthermore, its specificity for certain ECM proteins makes it a candidate for imaging agents to visualize ECM changes in disease states.

High Purity

SDS-PAGE (MMP7-49H).jpg

Fig1. SDS-PAGE (MMP7-49H)

.

SDS-PAGE (MMP7-5434H).jpg

Fig2. SDS-PAGE (MMP7-5434H)

Case Study 1: Suwen Ou, 2023

Colorectal cancer (CRC), the third most prevalent cancer, often harbors high levels of Fusobacterium nucleatum (F. nucleatum), which may promote metastasis. Researchers conducted a comprehensive analysis to identify key genes and pathways influenced by F. nucleatum. Using 16S rDNA sequencing and q-PCR, they confirmed its overabundance in CRC tissues and stools. The experiments showed that F. nucleatum enhances CRC cell migration by upregulating Matrix metalloproteinase 7 (MMP7), which is linked to poor prognosis. Researchers also identified potential drugs from the HERB database that could target MMP7, suggesting new therapeutic strategies for CRC.

MMP7-1.jpg

Fig1. The protein expression of MMP7 after PBS treatment.

MMP7-2.jpg

Fig2. WB results showed F. nucleatum promotes the migration of CRC cells by upregulating MMP7.

Case Study 2: Yue Yin, 2021

Long-term peritoneal dialysis (PD) can lead to peritoneal membrane dysfunction and ultrafiltration failure. Mesothelial cells are crucial for peritoneal membrane health, and Matrix metalloproteinases (MMPs), particularly MMP-7, are key in maintaining extracellular matrix balance. This study found that MMP-7 levels rise in PD patients, correlating with reduced ultrafiltration. MMP-7 affects cell osmotic pressure and volume in mesothelial cells by activating the MAPKs-ERK pathway, which increases aquaporin-1 (AQP-1) expression. Blocking the ERK pathway can reverse MMP-7's effects on AQP-1 and cell homeostasis.

MMP7-3.jpg

Fig3. The cells were treated with indicated MMP-7 for 12 hours and immunofluorescence assay was used to detect the expression of AQP-1.

MMP7-4.jpg

Fig4. HMrSV5 cells were stimulated with MMP-7 protein for indicated time points, and the phosphorylation level of ERK, JNK and p38 was detected by Western blotting.

MMP7 involved in several pathways and played different roles in them. We selected most pathways MMP7 participated on our site, such as Wnt signaling pathway, which may be useful for your reference. Also, other proteins which involved in the same pathway with MMP7 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

Pathway Name Pathway Related Protein
Wnt signaling pathwayPPARDB;FRAT2;SMAD3;PRICKLE2B;FBXW11;PPP3CCA;SFRP5;TBL1Y;SKP1

MMP7 has several biochemical functions, for example, heparin binding, metalloendopeptidase activity, zinc ion binding. Some of the functions are cooperated with other proteins, some of the functions could acted by MMP7 itself. We selected most functions MMP7 had, and list some proteins which have the same functions with MMP7. You can find most of the proteins on our site.

Function Related Protein
heparin bindingRPL29;MMP7;C6orf25;ADAMTS1;PCOLCE2;SERPINA5;THBS2;COL13A1;PTPRFB
metalloendopeptidase activityMMP1A;ZMPSTE24;ADAMTS2;MBTPS2;ECEL1;ADAM7;OMA1;ADAMTSL5;ADAM1B
zinc ion bindingTRIM22;NR5A2;RNF7;Shh;MT2A;APOBEC3G;XIAP;ZDHHC20A;PRKCBA

MMP7 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 MMP7 here. Most of them are supplied by our site. Hope this information will be useful for your research of MMP7.

ELN; FASLG

Gene Family

MMPs

Research Area

Related articles

Kim, GE; Lee, JS; et al. Expression of matrix metalloproteinases and their inhibitors in different immunohistochemical-based molecular subtypes of breast cancer. BMC CANCER 14:-(2014).
Mitsui, H; Suarez-Farinas, M; et al. Gene Expression Profiling of the Leading Edge of Cutaneous Squamous Cell Carcinoma: IL-24-Driven MMP-7. JOURNAL OF INVESTIGATIVE DERMATOLOGY 134:1418-1427(2014).
  • Reviews
  • Q&As

Customer Reviews (3)

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Reviews
05/01/2023

    This includes rigorous quality control measures to ensure the consistency and purity of the protein, thereby reducing variability in the experimental outcomes.

    05/13/2022

      by utilizing MMP7 protein in trials and collaborating with a supportive manufacturer, researchers can gain access to a versatile tool that can aid in their understanding of angiogenesis and vascular biology.

      05/26/2018

        With expert assistance and reliable product quality, researchers can conduct their experiments with confidence, enabling them to contribute to advancements in the field and potentially improve future therapeutic interventions.

        Q&As (6)

        Ask a question
        What clinical conditions are associated with MMP7 overexpression? 01/31/2023

        MMP7 overexpression has been linked to various diseases, including cancer, inflammatory disorders, and tissue fibrosis.

        In what ways does MMP7 contribute to inflammatory processes? 05/20/2020

        MMP7 is involved in the degradation of extracellular matrix components during inflammation, influencing tissue damage and repair processes.

        How can MMP7 be targeted for therapeutic interventions? 01/20/2020

        Developing specific inhibitors that target MMP7 activity is a potential approach for therapeutic interventions, particularly in diseases where MMP7 plays a detrimental role.

        Are there any inhibitors developed for MMP7? 10/19/2017

        Several MMP inhibitors have been investigated, and some show promise in controlling MMP7 activity. However, their clinical use is still under research.

        How is MMP7 involved in cancer progression? 01/13/2017

        MMP7 facilitates cancer cell invasion and metastasis by degrading the extracellular matrix, allowing cancer cells to invade surrounding tissues and spread to distant organs.

        Can MMP7 be used as a biomarker for cancer diagnosis? 01/09/2016

        Yes, elevated levels of MMP7 have been observed in the serum or tissues of cancer patients, making it a potential biomarker for certain types of cancer.

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