MMP2 Antibody

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Description

Definition and Target Profile

MMP2 antibodies are immunoglobulins that bind specifically to MMP2, an enzyme encoded by the MMP2 gene located on chromosome 16q12.2 . This enzyme cleaves type IV collagen in basement membranes and participates in angiogenesis, tissue repair, and bone remodeling . The antibody targets either the pro-enzyme (72-73 kDa) or active form (62 kDa) of MMP2, depending on its epitope specificity .

Key Applications in Research

MMP2 antibodies are utilized across multiple experimental workflows:

ApplicationExample Use CaseSource
Western Blot (WB)Detects MMP2 in HT1080 fibrosarcoma (72 kDa band) and U-118-MG glioblastoma cells
Immunoprecipitation (IP)Isolates MMP2 from HT1080 lysates for protein interaction studies
Immunohistochemistry (IHC)Identifies MMP2 overexpression in ovarian cancer tissues
Functional InhibitionBlocks MMP2-mediated extracellular matrix degradation in metastasis assays

Oncology

  • Elevated MMP2 correlates with tumor invasion in fibrosarcoma , hepatocellular carcinoma , and glioblastoma .

  • The C-terminal PEX domain exhibits anti-angiogenic properties, suggesting therapeutic potential .

Genetic Disorders

  • Mutations in MMP2 cause Torg-Winchester syndrome and multicentric osteolysis .

  • MMP2-deficient mice show impaired mammary gland development and reduced tumor angiogenesis .

Inflammatory Diseases

  • Regulates GSK3β activity, contributing to myocardial oxidative stress .

  • Exacerbates asthma responses in murine models .

Validation and Quality Control

  • KO validation: CAB19080 demonstrates no cross-reactivity in MMP2-knockout models .

  • Buffer Compatibility: Optimized for 5% NFDM/TBST blocking buffers .

  • Controls: GAPDH (ab181602) used as loading control in WB .

Emerging Therapeutic Directions

MMP2 antibodies are being investigated for:

  1. Anti-cancer therapies: Targeting MMP2 in tumor-associated vasculature .

  2. Biomarker development: Correlating serum MMP2 levels with metastatic progression .

  3. Inflammatory modulation: Blocking MMP2-mediated cleavage of CHUK/IKKA in innate immunity .

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
We typically dispatch orders within 1-3 business days of receipt. Delivery times may vary depending on the purchasing method and location. Please consult your local distributors for specific delivery timeframes.
Synonyms
72 kDa gelatinase antibody; 72kD type IV collagenase antibody; CLG 4 antibody; CLG 4A antibody; CLG4 antibody; CLG4A antibody; Collagenase Type 4 alpha antibody; Collagenase type IV A antibody; Gelatinase A antibody; Gelatinase alpha antibody; Gelatinase neutrophil antibody; Matrix metallopeptidase 2 gelatinase A 72kDa gelatinase 72kDa type IV collagenase antibody; Matrix metalloproteinase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase) antibody; Matrix Metalloproteinase 2 antibody; Matrix metalloproteinase II antibody; Matrix metalloproteinase-2 antibody; MMP 2 antibody; MMP II antibody; MMP-2 antibody; MMP2 antibody; MMP2_HUMAN antibody; MONA antibody; Neutrophil gelatinase antibody; PEX antibody; TBE 1 antibody; TBE-1 antibody
Target Names
Uniprot No.

Target Background

Function
MMP2 is a ubiquitously expressed metalloproteinase involved in a wide range of biological processes, including vascular remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. Beyond degrading extracellular matrix proteins, MMP2 can also cleave non-matrix proteins such as big endothelial 1 and beta-type CGRP, contributing to vasoconstriction. Additionally, MMP2 cleaves KISS at a Gly-|-Leu bond. It is implicated in myocardial cell death pathways and contributes to myocardial oxidative stress by regulating GSK3beta activity. MMP2 cleaves GSK3beta in vitro. MMP2 plays a role in the formation of fibrovascular tissues in association with MMP14. The C-terminal non-catalytic fragment of MMP2, known as PEX, exhibits anti-angiogenic and anti-tumor properties, inhibiting cell migration and adhesion to FGF2 and vitronectin. PEX serves as a ligand for integrin v/beta3 on the surface of blood vessels. MMP2 mediates the proteolysis of CHUK/IKKA, initiating a primary innate immune response by triggering mitochondrial-nuclear stress signaling and activating the pro-inflammatory NF-kappaB, NFAT, and IRF transcriptional pathways.
Gene References Into Functions
  1. No significant associations were observed with either MMP-2(-1306) C/T or MMP-3(-1171) 5A/6A. PMID: 30117779
  2. PROK1 or MMP-2 in the amniotic fluid do not have a role in the prediction of adverse pregnancy outcomes. PMID: 29405963
  3. CDH17 plays a role in altering MMP-2 expression via canonical NF-kappaB signaling in human gastric cancer PMID: 29783070
  4. Study results revealed that CCR2 promotes epithelial-to-mesenchymal transition through MMP2 in liver cancer. PMID: 30132565
  5. results of the study indicate that estradiol influence MMP-2 expression in the endometrium depends on the phase of menstrual cycle PMID: 30187906
  6. Fewer TIMP-2, Hsp70 and TGF-beta1 immunoreactive cells in younger individuals and increased expression of Hsp70 in elderly individuals demonstrated the influence of aging in lung remodeling PMID: 29325453
  7. Melatonin inhibits epithelial-to-mesenchymal transition in gastric cancer cells via attenuation of IL1beta/NFkappaB/MMP2/MMP9 signaling PMID: 30066836
  8. TF-FVIIa/trypsin-mediated PAR2 activation leads to enhanced MMP-2 expression in human breast cancer cells contributing to tumor progression. PMID: 29870887
  9. proteins such as MMP2 and MMP9 as well as P38 expression were also affected by the PKM2 expression changes. These results proved that PKM2 could be involved in the progression of bladder cancer by mitogen-activated protein kinases signaling pathway. PMID: 30249877
  10. High MMP2 expression is associated with colorectal cancer cell migration, invasion and metastasis PMID: 30015978
  11. We conducted a case-control genetic association study, adjusted for known IA risk factors (smoking and hypertension), in a UK Caucasian population of 1409 patients with intracranial aneurysms (IA), and 1290 matched controls, to determine the association of the rs243865 C > T functional MMP-2 gene SNP with IA (overall, and classified as ruptured and unruptured). PMID: 29334797
  12. MMP2 rs243865 and MMP9 rs3918242 polymorphisms are significantly associated with the risk of RSA in Chinese population. PMID: 30290617
  13. findings demonstrate an association between the MMP-2 C-735 T polymorphism with blood pressure and the risk of preeclampsia PMID: 29017408
  14. The role of MMP 2 in asthma remains unclear and no study has been conducted till date, to determine the role of MMP-2 -735C/T gene polymorphism in asthma. This study does not disprove such association. PMID: 28051223
  15. knockdown of TRIM31 reduced the expression of MMP2, MMP9 and phospho-Akt. PMID: 29864908
  16. SB22055 could reduce the expression of BSP, OPN and MMP2 in prostate cancer cells. PMID: 29917166
  17. Therefore, the A allele of MMP2 rs2287074 could be a protective factor for brick tea skeletal fluorosis. PMID: 28079131
  18. MMP-2 genetic variants are an important mediator of stroke risk PMID: 30278505
  19. HMGB1 promoted lung cancer invasion and metastasis by upregulating the expression and activity of MMP-2 in an NF-kappaB-dependent manner. PMID: 29850505
  20. High glucose levels induce MMP-2 expression in Human cardiac fibroblasts , possibly by up-regulation of SGLT1. PMID: 29512713
  21. we have discovered the novel N-72, and it was crucial for EGF-induced migration by targeting MMP2 in Human amnion mesenchymal stem cells (hAMSCs) PMID: 29734654
  22. data indicated that MMP-2/MMP-9 was coordinately targeted by two non-coding RNAs, miR-296-3p and FOXCUT, which were decreased, and tumor-suppressing factors in choroidal malignant melanoma PMID: 29260433
  23. Increased MMP-2 and MMP-9 activities may contribute to the pathogenesis and disease severity of cutaneous lupus erythematosus. PMID: 29349515
  24. No association between the carriage of studied MMP2 polymorphisms and the predisposition to preeclampsia was found. PMID: 29670668
  25. We propose that serum levels of MMP-2 and MMP-9 are not predictive on treatment response and survival in LARC patients. PMID: 29578156
  26. that miR-338-5p has a function in promoting glioma cell invasion by targeting TSHZ3 suppression on MMP2 PMID: 28780604
  27. In dilation cardiomyopathy, expression of MMP-2, MMP-9, and TIMP-1 and their ratios in autopsy material and in cultures was elevated by 1.5-9 times. PMID: 29504111
  28. OSM [oncostatin M]might be involved in the invasiveness of extravillous trophoblasts under hypoxia conditions via increasing MMP-2 and MMP-9 enzymatic activities through STAT3 signaling. Increased MMP-9 activity by OSM seems to be more important in primary trophoblasts. PMID: 30091322
  29. TIMP2 promotes tumor progression and miR2055p directly regulates TIMP2, thereby suppressing proMMP2 activation and inhibiting oral squamous cell carcinoma cell invasiveness. PMID: 29393341
  30. Elevated MMP-2 levels were observed in blood of pancreatic cancer patients which correlated with its tissue expression. However, these levels did not associate with survival or any clinicopathological parameters of patients. PMID: 29355139
  31. Increased urinary concentration of matrix metallopeptidase 2 (MMP-2) at 12 and 16 weeks of gestation predicted an increased risk of developing preeclampsia in the study population. PMID: 28055277
  32. There was no difference found in MMP-2, MMP-9 or TLR-4 levels between non-thrombocytopenic and thrombocytopenic septic donors. PLA formation was increased in thrombocytopenic patients. PMID: 29734352
  33. MMP2 rs243865 was the only single nucleotide polymorphism significantly associated with Floppy Mitral Valve/Mitral Valve Prolapse (FMV/MVP) as compared to the control.The frequency of certain MMP2 polymorphisms is higher in patients with the FMV/MVP syndrome and patients with FMV/MVP without the syndrome. PMID: 28750369
  34. Platelets may contribute to joint degeneration in knee osteoarthritis by favouring the accumulation of MMP-2 in synovial fluid. PMID: 28981555
  35. In pregnancy MMP2 gene expression was significantly higher in preterm than full term. Human papilloma viral load was found to be positively correlated to the rate of MMP2 expression and the gestational age was significantly related to the viral load and the rate of expression of MMP2 gene. Human pabilloma virus especially high-risk genotypes was correlated to spontaneous preterm labor in Egyptian females. PMID: 28264621
  36. We conclude that S1P attenuates the invasion of C643 cells by activating S1P2 and the Rho-ROCK pathway, by decreasing calpain activity, and by decreasing the expression, secretion and activity of MMP2 and, to a lesser extent, MMP9. Our results thus unveil a novel function for the S1P2 receptor in attenuating thyroid cancer cell invasion. PMID: 29734379
  37. High mmp2 expression is associated with ovarian cancer cell migration and invasion. PMID: 28677781
  38. MMP-2 was expressed in high percentage of endometrial cancer and its expression may be associated closely with clinical stage, and tumor invasion and metastasis, indicating that MMP-2 overexpression may serve as a predictive factor for poor prognosis of endometrial cancer. PMID: 30024495
  39. MMP2 single nucleotide polymorphisms association with lymphedema caused by Wuchereria bancrofti. PMID: 29122006
  40. MMP-2 promoted and MMP-13 disrupted vasculogenic mimicry formation in large cell lung cancer by cleaving laminin-5 to influence EGFR signal activation. PMID: 28766880
  41. Data suggest that environmental carcinogen PFOA (perfluorooctanoic acid) stimulates ovarian cancer cell migration, invasion, and MMP2/MMP9 expression by up-regulating ERK/NFkappaB signaling pathway. (MMP = matrix metallopeptidase; NFkappaB = nuclear factor kappa B) PMID: 29753068
  42. Matrix-metalloproteinase-2 is implicated in the pathophysiological mechanism of stenosis development and has a predictive value for arteriovenous fistula failure in hemodialysis patients PMID: 28868755
  43. Fli1 functioned as an oncogene in HCC carcinogenesis and it exerted its promoting metastatic effect primarily by modulating the matrix metalloproteinase (MMP)2 signaling pathway. PMID: 29138848
  44. Rictor regulates the vasculogenic mimicry of melanoma and determines the patients' survival via the AKT-MMP2-MMP9 pathway. PMID: 28699701
  45. Expression of BRM and MMP2 in the thoracic aortic aneurysm and aortic dissection is very high, indicating that BRM and MMP2 may play important roles in the occurrence and development of thoracic aortic aneurysm and aortic dissection. PMID: 28678310
  46. at high endothelial shear stress, PI16 contributes to inhibition of MMP2 protease activity, protection that can be reversed during inflammation PMID: 27996045
  47. MMP-2 serum level and circulating tumor cells show the potential to predict CNS metastases and overall survival in breast cancer patients; CTCs and MMP-9 serum level could be a promising therapy response marker in castration resistant prostate cancer patients PMID: 28529342
  48. RhoGDIbeta overexpression led to downregulation of miR-200c, whereas miR-200c was able directly to target 3'-UTR of jnk2mRNA and attenuated JNK2 protein translation, which resulted in attenuation of Sp1mRNA and protein expression in turn, inhibiting Sp1-dependent MMP-2 transcription. PMID: 28846829
  49. both HBEGF upregulation and apoptosis were rescued by exogenous MMP2 PMID: 28731464
  50. MMP-2 (and MMP-1 and MMP-3) are independently associated with markers of arterial stiffening in patients with type 1 diabetes. PMID: 29070037

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Database Links

HGNC: 7166

OMIM: 120360

KEGG: hsa:4313

STRING: 9606.ENSP00000219070

UniGene: Hs.513617

Involvement In Disease
Multicentric osteolysis, nodulosis, and arthropathy (MONA)
Protein Families
Peptidase M10A family
Subcellular Location
[Isoform 1]: Secreted, extracellular space, extracellular matrix. Membrane. Nucleus. Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes.; [Isoform 2]: Cytoplasm. Mitochondrion.
Tissue Specificity
Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate.

Customer Reviews

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Applications : WB

Sample dilution: 1: 500

Review: MMP-2. ANOVA, Dunnet: control group signif- icantly different from U4w, K4w, and KP4w, *P < .05. ANOVA, Tukey, P< .05: **2-week groups significantly different from 4- week groups. & PPNL-treated groups significantly different from groups without treatment, # P<.05.

Q&A

What is the optimal detection method for MMP-2 in human tissue samples?

Immunohistochemistry (IHC) represents a powerful approach for detecting MMP-2 in human tissue samples, particularly in paraffin-embedded sections. For optimal results, researchers should:

  • Use MMP-2 antibodies at 10-15 µg/mL concentration with overnight incubation at 4°C

  • Consider antibody clone selection based on target specificity (pro-MMP-2 vs. active form)

  • Implement appropriate counterstaining (hematoxylin for contrast)

  • Include positive controls such as ovarian cancer tissue, which shows consistent MMP-2 expression

Research demonstrates successful MMP-2 detection in ovarian cancer tissues using both monoclonal (clone 36006) and polyclonal antibodies, with visualization via HRP-DAB staining systems . When evaluating expression in heterogeneous tissues, consider separate analysis of epithelial and stromal compartments, as they may have distinct prognostic significance .

How can I distinguish between latent and active forms of MMP-2 using antibodies?

Distinguishing between pro-MMP-2 (72 kDa) and active MMP-2 (63-64 kDa) requires careful selection of antibody clones and detection methods:

  • Western blotting remains the gold standard for differentiating the two forms based on molecular weight

  • Clone-specific antibodies like 8B4 are specifically designed to detect activated MMP-2

  • Zymography can complement antibody-based approaches to confirm enzymatic activity

When performing Western blot analysis, use reducing conditions with appropriate molecular weight markers to accurately distinguish the 72 kDa pro-form from the 63-64 kDa active form . The activation status of MMP-2 provides crucial information about tissue remodeling processes and potential disease progression .

What factors influence MMP-2 antibody performance in Western blotting applications?

Several critical factors affect MMP-2 antibody performance in Western blotting:

  • Sample preparation: Cell conditioned medium often yields better results than whole cell lysates for secreted MMP-2

  • Reducing conditions: Most MMP-2 antibodies perform optimally under reducing conditions

  • Antibody concentration: Typically 1-10 μg/mL, with optimal dilution determined empirically

  • Detection systems: HRP-conjugated secondary antibodies with enhanced chemiluminescence provide suitable sensitivity

Researchers report consistent detection of MMP-2 from U-118-MG glioblastoma cell lines, MCF7 breast cancer cells, and HT-1080 fibrosarcoma cells . When troubleshooting, consider using these established positive control cell lines. For detecting both latent and active forms, use antibodies targeting epitopes present in both forms, such as those recognizing the catalytic or hemopexin domains .

How can researchers validate MMP-2 antibody specificity for immunohistochemistry?

Antibody validation for IHC applications is crucial for generating reliable results:

Validation MethodImplementation ApproachExpected Outcome
Positive controlsUse ovarian cancer or glioblastoma tissuesConsistent immunoreactivity
Negative controlsOmit primary antibodyNo significant staining
Knockdown validationUse MMP-2 silenced cell lines or tissuesDecreased or absent staining
Peptide competitionPre-incubate antibody with immunizing peptideAttenuated or blocked signal
Western blot correlationCompare IHC with WB from same samplesConsistent expression patterns

Research demonstrates that MMP-2 knockdown models serve as excellent negative controls for antibody validation, showing significantly reduced staining compared to controls . Additionally, ensure proper antigen retrieval methods, as MMP-2 epitopes may be masked in formalin-fixed tissues.

How does MMP-2 expression correlate with prognosis across different cancer types?

MMP-2 expression exhibits important prognostic significance, but interpretation depends on cancer type and cellular localization:

  • Non-small cell lung cancer: MMP-2 overexpression correlates with shortened cancer-related survival, particularly in lymph node-negative (pN0) patients (relative risk 2.6, P = 0.005)

  • Ovarian cancer: MMP-2 expression in epithelium correlates with poor prognosis (HR: 10.8, 95% CI: 1.36-25.7, p = 0.02), while stromal expression shows a protective effect (HR: 0.15, 95% CI: 0.05-0.42, p < 0.001)

When designing prognostic studies, researchers should:

  • Separately analyze epithelial and stromal compartments

  • Account for tumor stage, histological subtype, and steroid receptor status

  • Correlate with established prognostic markers

  • Apply appropriate multivariate analysis methodologies

The opposing effects of epithelial versus stromal MMP-2 expression in ovarian cancer highlight the complexity of MMP-2 biology and the importance of compartment-specific analysis .

What are the optimal antibody pairs for developing MMP-2 sandwich ELISA assays?

Developing robust sandwich ELISA assays for MMP-2 requires careful selection of capture and detection antibody pairs:

  • Recommended pairs include:

    • Mouse anti-human MMP-2 clone C12-8A3 (capture) with biotinylated clone J08-3B10 (detection)

    • Mouse anti-human MMP-2 MAB9024 (capture) with biotinylated MAB9023 (detection)

Key considerations for ELISA optimization include:

  • Capture antibody concentration (typically 1-10 μg/mL)

  • Detection antibody biotinylation efficiency

  • Blocking buffer composition to minimize background

  • Standard curve preparation using recombinant human MMP-2

  • Sample dilution optimization

For human serum and plasma samples, polyclonal goat antibody AF902 has been successfully used as both capture and detection antibody . Signal amplification with streptavidin-HRP and appropriate substrate solution (such as DY999) enhances sensitivity .

How can MMP-2 antibodies be utilized in developing targeted cancer therapeutics?

MMP-2 antibodies are being leveraged for innovative cancer therapeutic approaches:

  • Antibody-drug conjugates (ADCs): Coupling MMP-2 antibodies to cytotoxic drugs for targeted delivery to MMP-2-expressing tumors

  • Nanobody technology: Development of highly selective MMP-2 inhibitory nanobodies (e.g., VHH-29) that can hinder MMP-2 effects on platelet activation

  • Enzyme-responsive antibody nanoparticle systems: Creating delivery systems that release therapeutic agents upon encountering MMP-2 in the tumor microenvironment

Research demonstrates that enzyme-responsive antibody nanoparticle-loaded drugs (FMSN-Dox-H2-AE01) exhibited 85-90% cancer cell mortality rates while showing favorable safety profiles. These systems offer controlled release efficiency toward cancer cells induced by different levels of MMP-2 and pH .

What role does MMP-2 play in immune modulation, and how can antibodies help elucidate these mechanisms?

Emerging research indicates MMP-2 has previously unrecognized immunomodulatory functions:

  • MMP-2 signals proinflammatory pathways in antigen-presenting cells through interactions with Toll-like receptors (TLRs)

  • Both TLR2 and TLR4 are required for MMP-2-mediated inflammatory responses

  • Immunoprecipitation experiments demonstrate physical association between MMP-2 and TLR2/TLR4

Researchers investigating these pathways should:

  • Use highly specific MMP-2 antibodies for immunoprecipitation studies

  • Employ TLR2/TLR4 knockout models as negative controls

  • Confirm antibody specificity through reverse immunoprecipitation

  • Correlate structural findings with functional immune assays

Understanding these immunomodulatory functions may reveal new therapeutic applications for MMP-2 antibodies in inflammatory diseases and cancer immunotherapy contexts .

What are the methodological considerations when using MMP-2 antibodies for in vivo optical imaging?

In vivo optical imaging using MMP-2 antibodies presents unique methodological challenges:

  • Small immuno protein (SIP) format antibodies specifically targeting the catalytic domain of human MMP-2 (aMMP2-SIP) have been developed for imaging purposes

  • Near-infrared fluorescence imaging (NIRF) using Cy5-labeled aMMP2-SIP allows non-invasive detection of MMP-2 in tumor models

  • Optimal imaging time point is typically 48 hours post-injection, balancing tumor signal with background clearance

When designing in vivo imaging studies:

  • Use MMP-2 knockdown tumor models as negative controls

  • Include low MMP-2 expressing tumors (e.g., HCT116) as additional controls

  • Validate antibody specificity before in vivo application

  • Consider that aMMP2-SIP uptake correlates with MMP-2 activity rather than simply expression levels

This correlation with enzymatic activity makes aMMP2-SIP a potential non-invasive imaging biomarker for evaluating MMP-2 activity in tumors, which may have significant clinical applications for cancer diagnosis and treatment monitoring .

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