• Official Full Name

    matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)

  • 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 type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
  • Synonyms

    MMP2; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); CLG4; MONA; CLG4A; TBE-1; MMP-II; 72 kDa type IV collagenase; MMP-2; gelatinase A; 72 kDa gelatinase; collagenase type IV-A; neutrophil gelatinase; matrix metalloproteinase-2; matrix metalloproteinase-II;

  • Recombinant Proteins
  • Cell & Tissue Lysates
  • Native Proteins
  • Protein Pre-coupled Magnetic Beads
  • Assay Kits
  • Chicken
  • Human
  • Mouse
  • Rat
  • Zebrafish
  • E.coli
  • E.coli Cells
  • HEK293
  • HEK293F
  • HEK293T
  • Human
  • Human Cell
  • Human Fibroblasts
  • Human Synovial Fibroblasts
  • In Vitro Cell Free System
  • Mammalian Cell
  • Mammalian cells
  • Mouse Fibroblast
  • Sf9 Insect Cell
  • Wheat Germ
  • yeast
  • Yeast
  • C
  • His
  • Flag
  • GST
  • His (Fc)
  • Avi
  • His|SUMO
  • Myc
  • DDK
  • Myc|DDK
  • N/A
  • N
  • KSI
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human MMP2-808H Active Recombinant Human Matrix Metallopeptidase 2 Sf9 Insect Cell N/A
Human MMP2-150H Active Recombinant Human MMP2 protein Yeast N/A
Human MMP2-1715H Active Recombinant Human Matrix Metallopeptidase 2 (Gelatinase A, 72 KDa Gelatinase, 72 KDa Type IV Collagenase) Human N/A
Human MMP2-201H Active Recombinant Human MMP2 protein E.coli N/A
Human MMP2-12H Active Recombinant Human MMP2 Protein (115-214, 393-447) E.coli 115-214, 393-447
Human MMP2-408H Recombinant Human MMP2 Mammalian cells N/A
Human MMP2-5051H Recombinant Human MMP2, His-tagged E.coli His
Human MMP2-182H Active Recombinant Human MMP2 Protein, His-tagged HEK293 His Met 1-Cys 660
Human MMP2-29435TH Recombinant Human MMP2, His-tagged E.coli His
Human MMP2-169H Recombinant Human MMP2 yeast N/A
Human MMP2-889H Active Recombinant Human MMP2 protein(Met 1-Cys 660) E.coli N/A Met 1-Cys 660
Human MMP2-8392H Recombinant Human MMP2, GST-tagged E.coli GST 461-660aa
Human MMP2-151H Recombinant Human Matrix Metallopeptidase 2, Hemopexin-like Domain E.coli N/A
Human MMP2-562H Recombinant Human MMP2 Protein, MYC/DDK-tagged HEK293 Myc/DDK
Human MMP2-1716H Recombinant Human Matrix Metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase) Human N/A
Human Mmp2-416M Recombinant Mouse Mmp2, His-tagged Human Cell His
Human MMP2-450H Recombinant Human matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase), His-tagged E.coli His
Human MMP2-244H Recombinant Human MMP2 protein, His-tagged E.coli His
Human MMP2-890H Recombinant Human MMP2 protein, His-tagged HEK293 His 631
Human MMP2-2380HCL Recombinant Human MMP2 cell lysate Human Cell N/A
Human MMP2-5425H Recombinant Human MMP2 Protein, GST-tagged Wheat Germ GST
Human MMP2-8392HA Recombinant Human MMP2 protein, GST-tagged, APC labeled E.coli Cells GST
Human MMP2-6516HF Recombinant Full Length Human MMP2 Protein, GST-tagged In Vitro Cell Free System GST 660 amino acids
Human MMP2-29475TH Native Human MMP2 N/A
Human MMP2-2257H Recombinant Human MMP2 Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293T Myc/DDK
Human MMP2-1120H Recombinant Human MMP2 Protein, His-tagged HEK293F N-His Ala30-Cys660
Human MMP2-1419H-B Recombinant Human MMP2 Protein Pre-coupled Magnetic Beads HEK293
Human MMP2-220H Active Recombinant Human MMP2 Protein (Tyr120-Cys660), C-His tagged, Animal-free, Carrier-free E.coli C-His Tyr120-Cys660
Human MMP2-1872H Recombinant Human MMP2 protein, GST-tagged E.coli GST 110-200 aa
Human MMP2-1121H Recombinant Human MMP2 Protein, His-tagged HEK293F N-His Ala30-Cys660
Human MMP2-4564H Recombinant Human MMP2 Protein (Tyr110-Cys660), N-His tagged E.coli N-His Tyr110-Cys660
Human MMP2-8392HP Recombinant Human MMP2 protein, GST-tagged, R-PE labeled E.coli Cells GST
Human MMP2-46H Native Human MMP-2 Human Synovial Fibroblasts N/A
Human MMP2-1419H Recombinant Human MMP2 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Human MMP2-47H Native Human MMP-2/TIMP-2 Complex Human Fibroblasts N/A
Human MMP2-1611HFL Recombinant Full Length Human MMP2 Protein, C-Flag-tagged Mammalian cells Flag
Human MMP2-03H Active Recombinant Pre-activated Human MMP2 Protein (110-660) HEK293 110-660
Human MMP2-800H Recombinant Human MMP2 Protein, His-tagged HEK293 His
Human MMP2-248H Active Native Human MMP2 protein HEK293 N/A Met1-Cys660
Human MMP2-4562H Recombinant Human MMP2 Protein (Ala30-Cys660), C-His tagged Mammalian cells C-His Ala30-Cys660
Human MMP2-4563H Recombinant Human MMP2 Protein (Tyr110-Gly216 & KGV & Gly394-Asp450), C-His tagged E.coli C-His Tyr110-Gly216 & KGV & Gly394-Asp450
Mouse Mmp2-415M Recombinant Mouse Matrix Metallopeptidase 2 Mammalian cells N/A
Mouse Mmp2-44M Recombinant Mouse MMP-2/TIMP-2 Complex Mouse Fibroblast N/A
Mouse Mmp2-1019M Recombinant Mouse Mmp2 Protein, His-tagged HEK293 His
Mouse Mmp2-245M Recombinant Mouse Mmp2 protein, His-tagged E.coli His
Mouse MMP2-8455M Native Mouse MMP2 Mouse Fibroblast N/A
Mouse Mmp2-10593M-B Recombinant Mouse Mmp2 Protein Pre-coupled Magnetic Beads HEK293
Mouse Mmp2-2164M Recombinant Mouse Mmp2 protein, His-tagged HEK293 His Met409-Cys662
Mouse MMP2-0391M Active Recombinant Mouse MMP2 protein, His-tagged HEK293 His Ala30-Thr460
Mouse Mmp2-1783M Recombinant Mouse Mmp2 Protein, His-tagged E.coli N-His Tyr110-Cys662
Mouse Mmp2-10593M Recombinant Mouse Mmp2 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Mouse Mmp2-1784M Recombinant Mouse Mmp2 Protein, His-tagged E.coli N-His Tyr445-Cys662
Mouse Mmp2-1785M Recombinant Mouse Mmp2 Protein, His-tagged E.coli N-His Tyr110-Cys662
Mouse Mmp2-4100M Recombinant Mouse Mmp2 Protein, Myc/DDK-tagged HEK293T Myc/DDK
Rat MMP2-3715R Recombinant Rat MMP2 Protein Mammalian Cell His
Rat Mmp2-246R Recombinant Rat Mmp2 protein, His-tagged E.coli His
Rat MMP2-28059TR MMP2 protein(Rat) N/A
Rat MMP2-3371R Recombinant Rat MMP2 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Rat MMP2-3371R-B Recombinant Rat MMP2 Protein Pre-coupled Magnetic Beads HEK293
Rat Mmp2-1786R Recombinant Rat Mmp2 Protein, His-tagged E.coli N-His Tyr445-Cys662
Rat Mmp2-2417R Recombinant Rat Mmp2 protein, His-KSI-tagged E.coli N-His-KSI 412-662aa
Rat Mmp2-5467R Recombinant Rat Mmp2 protein, His-tagged Yeast His 110-662aa
Rat MMP2-657R Recombinant Rat MMP2 Protein (110-662 aa), His-SUMO-tagged E.coli His/SUMO 110-662 aa
Zebrafish MMP2-9789Z Recombinant Zebrafish MMP2 Mammalian Cell His
Chicken MMP2-5990C Recombinant Chicken MMP2 Mammalian Cell His
Chicken MMP2-1122C Recombinant Chicken MMP2 Protein, His-tagged E.coli N-His Tyr107-Cys663
Kit-0320C MMP2 Inhibitor Screening Assay Kit N/A
  • Background
  • Quality Guarantee
  • Case Study
  • Involved Pathway
  • Protein Function
  • Interacting Protein
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Fig1. Phosphorylation/dephosphorylation mechanism; MMP-2 activity is enhanced by dephosphorylation and diminished by phosphorylation. (Wesam Bassiouni, 2021)

What is MMP2 protein?

MMP2 (matrix metallopeptidase 2) gene is a protein coding gene which situated on the long arm of chromosome 16 at locus 16q12. This gene is a member of the matrix metalloproteinase (MMP) gene family, that are zinc-dependent enzymes capable of cleaving components of the extracellular matrix and molecules involved in signal transduction. The protein encoded by this gene is a gelatinase A, type IV collagenase, that contains three fibronectin type II repeats in its catalytic site that allow binding of denatured type IV and V collagen and elastin. This enzyme can be activated extracellularly by proteases, or, intracellulary by its S-glutathiolation with no requirement for proteolytical removal of the pro-domain. The MMP2 protein is consisted of 660 amino acids and its molecular mass is approximately 73.9 kDa.

What is the function of MMP2 protein?

The main function of MMP2 is to degrade various proteins in the extracellular matrix (ECM), such as collagen, elastin and fibronectin. Through this degradation, MMP2 plays a key role in many physiological and pathological processes, including tissue development, wound healing, angiogenesis, and tumor invasion and metastasis. In addition, MMP2 is also involved in inflammatory and immune responses, influencing cell migration and proliferation by regulating the activity of cytokines and chemokines.

MMP2 Related Signaling Pathway

MMP2 is involved in a variety of cell signaling pathways, mainly involved in extracellular matrix remodeling, cell proliferation, migration, invasion and apoptosis. During tumorigenesis, angiogenesis, tissue repair, and inflammation, MMP2 influences cellular interactions and signaling by regulating the activity of growth factors, cytokines, and receptors. In addition, MMP2 also interacts with a variety of signaling pathways, such as PI3K/Akt, MAPK/ERK, Wnt/β-catenin and TGF-β, to further regulate cell function and biological behavior.

MMP2 Related Diseases

MMP2 is upregulated in a variety of cancers, such as breast, lung, and prostate cancers, and can help cancer cells penetrate the basement membrane into the blood vessels or lymphatic system to metastasize to other sites. MMP2 plays a role in atherosclerotic plaque formation, causing plaque instability and potentially leading to myocardial infarction or stroke. In rheumatoid arthritis and other inflammatory joint diseases, MMP2 helps destroy articular cartilage. At the same time, it is associated with eye diseases, nervous system diseases and cerebrovascular diseases.


Fig2. Role of intracellular MMP-2 in selected pathological conditions. (Wesam Bassiouni, 2021)

Bioapplications of MMP2

MMP2 is widely used in cancer research as a marker of tumor aggressiveness and metastatic potential due to its ability to degrade the basement membrane and other extracellular matrix components, thereby promoting the migration and invasion of cancer cells. In addition, the detection of MMP2 activity is also used to assess the status of cardiovascular disease, arthritis, and other diseases. In some cases, MMP2 inhibitors are also being investigated as potential therapeutic agents to slow the progression of the disease, particularly in cancer treatment.

Case study 1: Rocío Del Carmen Bravo-Miana, 2022

Extracellular vesicles (EVs) participate in cell-stroma crosstalk within the tumor microenvironment and fibroblasts (Fb) contribute to tumor promotion in thyroid cancer. However, the role of tumor-stroma derived EVs still needs to be deciphered. The researchers hypothesized that the interaction of thyroid tumor cells with Fb would liberate EVs with a specific proteomic profile, which would have an impact on EV-functionality in thyroid tumor progression-related events.

EVs, obtained by ultracentrifugation of conditioned media, were characterized by nanoparticle tracking analysis and western blotting. EV-proteomic analysis was performed by mass-spectrometry, and metalloproteinases (MMPs) were studied by zymography. EVs expressed classical exosome markers, with EVs from thyroid tumor cell-Fb co-cultures showing a proteomic profile related to extracellular matrix (ECM) remodeling. Bidirectional crosstalk between Fb and TPC-1 cells produced significantly more EVs than their isolated cells, and potentiated EV-functionality. In line with this, Fb-TPC-1 derived EVs induced MMP2 activation in NThyOri supernatants, and MMP2 activity could be evidenced in Fb and TPC-1 contact-independent co-cultures. Besides, MMP2 interactors allowed us to discriminate between EVs from thyroid tumoral and non-tumoral milieus.


Fig1. Representative zymogram showing proMMP2 and MMP2 gelatinolytic activity in NThyOri-CM upon stimulation with medium (control) or EVs (CMs of NThyOri + EVs) from isolated Fb, TPC-1, NThyOri and Fb-TPC-1 and Fb-NThyOri co-cultured cells.

Fig2. Densitometric analysis of proMMP2 and MMP2 in TW-CMs from Fb and TPC-1 control and (Fb)-(TPC-1) contact-independent co-culture.

Case study 2: Luciana R Muniz-Bongers, 2021

The presence of an immunosuppressive tumor microenvironment is a major obstacle in the success of cancer immunotherapies. Because extracellular matrix components can shape the microenvironment, the researchers investigated the role of matrix metalloproteinase 2 (MMP2) in melanoma tumorigenesis. They found that MMP2 signals proinflammatory pathways on antigen presenting cells, and this requires both TLR2 and TLR4. B16 melanoma cells that express MMP2 at baseline have slower kinetics in Tlr2-/- Tlr4-/- mice, implicating MMP2 in promoting tumor growth. Indeed, Mmp2 overexpression in B16 cells potentiated rapid tumor growth, which was accompanied by reduced intratumoral cytolytic cells and increased M2 macrophages. In contrast, knockdown of Mmp2 slowed tumor growth and enhanced T cell proliferation and NK cell recruitment. Finally, they found that these effects of MMP2 are mediated through dysfunctional DC-T cell cross-talk as they are lost in Batf3-/- and Rag2-/- mice.


Fig3. Different MMP2 domains were deleted or expressed alone and tested for co-IP with Tlr2-HA.

Fig4. Immunofluorescence (IF) staining for MMP2 (green), CD45 (red), and DAPI (blue).

Fig1. Schematic depiction of potential mechanisms by which ANGPTL4-ERK1/2 signaling regulates OC progression. (Jiaqi Xu, 2024)


Fig2. Schematic representation of different pathways regulation by CLEC19A overexpression. CLEC19A regulates cell migration in this model by targeting VEGFα, RECK, TIMP3, and MMP2. (Fatemeh Mohajerani, 2024)

MMP2 involved in several pathways and played different roles in them. We selected most pathways MMP2 participated on our site, such as Leukocyte transendothelial migration, GnRH signaling pathway, Estrogen signaling pathway, which may be useful for your reference. Also, other proteins which involved in the same pathway with MMP2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

Pathway Name Pathway Related Protein
Leukocyte transendothelial migrationBCAR1;PTK2;PLCG2;CYBB;THY1;RHOH;ITGAM;CLDN2;CLDN22
Estrogen signaling pathwayPIK3CB;HSPA1A;HRAS;FKBP4;GABBR2;SOS1;AKT2;FOS;PIK3CG
Proteoglycans in cancerROCK1;PIK3R2;MAPK12;PPP1R12C;NUDT16L1;GPC1;CAV2;ACTB;PRKACA
Bladder cancerDAPK2;FGFR3;ERBB2;MMP1;MMP9;TP53;RASSF1;MMP2;TRP53

MMP2 has several biochemical functions, for example, metalloendopeptidase activity, metallopeptidase activity, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by MMP2 itself. We selected most functions MMP2 had, and list some proteins which have the same functions with MMP2. You can find most of the proteins on our site.

Function Related Protein
metalloendopeptidase activityMMP8;HE2;OMA1;ADAMTS5;MME;ADAM33;ADAM10;PAPPAB;ADAM30
protein bindingMETTL1;SNX19;KDM6B;ZNF346;TUBGCP2;KRT38;SH3BP4;LUC7L;BTRC
serine-type endopeptidase activityMCPT2;TMPRSS11E;TMPRSS2;KLK1;PRSS45;PRSS8;KLK4;PRSS50;TPSAB1
zinc ion bindingSORD;PHF10;ISL2B;NR3C1;SUV39H1;GFI1AA;PTGR1;TRIM42;CA6

MMP2 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 MMP2 here. Most of them are supplied by our site. Hope this information will be useful for your research of MMP2.

collagen_i_human; PCSK9; collagen_i_pig; TIMP2; Pcsk9; SCUBE3; USP12; A2M; LDLR; TGFB1; HSP90AA1; BACE1

Gene Family


Research Area

Related articles

Ghosh, A; Pechota, A; et al. Cigarette smoke-induced MMP2 and MMP9 secretion from aortic vascular smooth cells is mediated via the Jak/Stat pathway. HUMAN PATHOLOGY 46:284-294(2015).
Ding, XF; Yang, DR; et al. Targeting TR4 nuclear receptor suppresses prostate cancer invasion via reduction of infiltrating macrophages with alteration of the TIMP-1/MMP2/MMP9 signals. MOLECULAR CANCER 14:-(2015).
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Q&As (6)

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How to regulate the activity of MMP2 in tumor therapy? 10/20/2022

The activity of MMP2 is regulated by inhibitors and antibodies against it to inhibit tumor metastasis and invasion.

How is MMP2 related to metastases that promote disease progression? 05/04/2022

MMP2 interacts with some transfer factors, such as VEGF and EGF, to promote tumor metastasis and invasion.

What are the application prospects of MMP2 inhibitors? 02/20/2022

Inhibitors of MMP2 can be used as potential drug targets for the treatment of tumors, cardiovascular diseases and other related diseases.

Does MMP2 interact with the tumor microenvironment? 09/15/2021

MMP2 interacts with tumor cells, immune cells, blood vessels, etc. in the tumor microenvironment to affect tumor progression and treatment effect.

What is the role of MMP2 in embryonic development? 10/18/2020

It is involved in important processes such as morphogenesis, organ development and intraembryonic lymphatic vessel formation during embryonic development.

What are the effects of MMP2 mutations in human disease? 10/13/2020

Mutations in MMP2 may affect its protein structure and function, leading to the occurrence and progression of related diseases.

Customer Reviews (3)

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    The solubility and ion exchange ability are very good, which is convenient for subsequent experimental treatment and purification.


      Kinetic parameters such as enzymatic reaction rate and binding affinity were tested in the early stage, and it was found that the protein performed well.


        MMP2 products undergo strict quality control to ensure the consistency and stability of each batch.

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