Mouse matrix metalloproteinase 2/Gelatinase A,MMP-2 ELISA kit

Code CSB-E04676m
Size 96T,5×96T,10×96T
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Trial Size 24T ELISA Kit Trial Size (Only USD$150/ kit)
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Product Details

Target Name
matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)
Alternative Names
Mmp2 ELISA Kit; 72 kDa type IV collagenase ELISA Kit; EC ELISA Kit; 72 kDa gelatinase ELISA Kit; Gelatinase A ELISA Kit; Matrix metalloproteinase-2 ELISA Kit; MMP-2) [Cleaved into: PEX] ELISA Kit
Uniprot No.
Mus musculus (Mouse)
Sample Types
serum, plasma, cell culture supernates, tissue homogenates
Detection Range
15.6 pg/mL-1000 pg/mL
3.9 pg/mL
Assay Time
Sample Volume
Detection Wavelength
450 nm
Research Area
Assay Principle
Intra-assay Precision (Precision within an assay): CV%<8%
Three samples of known concentration were tested twenty times on one plate to assess.
Inter-assay Precision (Precision between assays): CV%<10%
Three samples of known concentration were tested in twenty assays to assess.
To assess the linearity of the assay, samples were spiked with high concentrations of mouse MMP-2 in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
1:100Average %90
Range %87-103
1:200Average %96
Range %82-105
1:400Average %89
Range %81-99
1:800Average %95
Range %87-108
The recovery of mouse MMP-2 spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
Sample TypeAverage % RecoveryRange
Serum (n=5) 9689-105
EDTA plasma (n=4)9584-101
Typical Data
These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
10002.754 2.708 2.731 2.608
5001.843 1.911 1.877 1.754
2501.118 1.074 1.096 0.973
1250.679 0.652 0.666 0.543
62.50.375 0.357 0.366 0.243
31.20.292 0.308 0.300 0.177
15.60.195 0.212 0.204 0.081
00.125 0.121 0.123
and FAQs
Store at 2-8°C. Please refer to protocol.
Lead Time
3-5 working days after you place the order, and it takes another 3-5 days for delivery via DHL or FedEx

This mouse MMP2 ELISA Kit is suitable for qualitatively determining mouse concentrations in multiple biological fluids, including mouse serum, plasma, cell culture supernates, and tissue homogenates in vitro.IL27 is a heterodimeric cytokine that plays a role both in innate and adaptive immunity. MMP2 is an enzyme that degrades bone matrix, promotes osteoclastogenesis, and enhances osteolysis in bone metastasis by activating multiple signaling pathways. It plays an essential role in extracellular matrix remodeling and other pathological processes, such as tumor progression and skeletal dysplasia. MMP2 is important for cancer progression, invasion, and metastasis. Excessive activation of MMP2 facilitates osteolytic metastasis and bone destruction in late-stage cancers, while its loss-of-function mutations lead to the declined bone mineralization and generalized osteolysis occurring progressively in skeletal developmental disorders, especially in multicentric osteolysis, nodulosis, and arthropathy (MONA). Either upregulation or downregulation of MMP2 activity can cause the same osteolytic effects.

This kit uses the quantitative sandwich-based enzyme immunoassay technique to measure the amount of mouse MMP2 in the sample. Standards and samples are respectively added to the microplate wells pre-coated with an anti-mouse MMP2 antibody. Biotin-labeled MMP2 antibody, HRP-avidin, and TMB substrate are pipped into the microplate in turn. The capture antibody pre-coated on the plate captures the MMP2 in the mouse samples. MMP2 binds to the biotinylated anti-MMP2 mouse monoclonal antibody. And the biotin on the biotinylated anti-MMP2 mouse monoclonal antibody binds to the avidin on the enzyme label, forming immune complexes. The color renders blue after the addition of the TMB substrate. The addition of the stop solution into the wells immediately turns the blue into yellow. The concentration of MMP2 in the samples is directly proportional to OD (450nm). Each manufactured lot of this ELISA kit was quality tested for criteria such as sensitivity, specificity, precision, linearity, and lot-to-lot consistency.

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Target Background

(From Uniprot)
Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues.; PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrin alpha-v/beta-3 on the surface of blood vessels.; Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.
Gene References into Functions
  1. In obese mice, periodontitis caused the downregulation of MMP2, and upregulation of TIMP1 and TGF-beta1 at transcriptional and translational levels. PMID: 29322806
  2. In the initial periods of AP progression, an increased expression of MMP9 in the TLR2 KO and MyD88 KO mice was observed. In the final periods of AP progression, a reduction of MMP2 expression and an increase of MMP9 expression in the TLR2 KO mice were observed. MMP2 and MMP9 production was modulated for TLR2 and MyD88 during apical periodontitis progression PMID: 29267523
  3. Diet and exercise affect atheromatous MMP2/9 activity by modulating the systemic inflammatory milieu, with sVCAM-1, resistin, and adiponectin closely interacting with each other and with visceral fat. PMID: 28883215
  4. calpains inhibition plays crucial roles in vascular restenosis by preventing neointimal hyperplasia at the early stage via suppression of the MMP2/TGF-beta1 pathway. PMID: 27453531
  5. Aneurysmal-prone factors induced HIF-1alpha can cause overexpression of MMP-2 and MMP-9 and promote aneurysmal progression. PMID: 27363580
  6. These studies illustrated an important role of MMP2 in cognitive and motor behaviors and confirm its importance in NPC activities crucial to brain development, growth and response to and recovery from injury. PMID: 28666838
  7. Secretagogin-dependent MMP2 release from neurons regulates neuroblast migration. PMID: 28223495
  8. This novel mouse model will be a very useful tool for evaluating the mechanistic pathways and for development of novel therapies in cigarette smoke-associated lung emphysema. PMID: 29428733
  9. matrix metalloproteinase 2 (Mmp2) transcript is a target of miR-195a-3p, and that silencing Mmp2 phenocopied the reduced proliferation and migration of MSCs. The therapeutic potential of miR-195a-3p as an angiogenesis inhibitor was also demonstrated in a laser-induced choroidal neovascularization mouse model. PMID: 26989874
  10. developed a novel selective radiolabeled MMP2/9 inhibitor, suitable for single photon emission computed tomography (SPECT) imaging that effectively targets atherosclerotic lesions in mice PMID: 29190653
  11. MMP-2 and MMP-9 have roles in early stages of experimental autoimmune encephalomyelitis induction; MMP-9 from an immune cell source is required in EAE for initial infiltration of leukocytes into the central nervous system PMID: 27831901
  12. This study illustrated that tumour-derived MMP2 has at least two roles in tumour malignancy; to enhance tumour invasiveness by degrading the extracellular matrix and to enhance tumour growth by promoting vessel maturation and function. PMID: 29065106
  13. MMP-2 and -9 expression were suppressed significantly by treatment with SB-3CT. The data demonstrated, for the first time, that SB-3CT strongly reduced corneal lymphangiogenesis and macrophage infiltration during inflammation. PMID: 28669039
  14. animals were submitted to the evaluation of Blood-Brain Barrier permeability and MMP-2 and MMP-9 in striatum, hippocampus and cerebral cortex PMID: 27915985
  15. High MMP2 expression is associated with abdominal aortic aneurysm. PMID: 28179581
  16. Low MMP2 expression is associated with liver fibrosis. PMID: 28118605
  17. Cleavage of beta-DG still occurred when both MMP-2 and MMP-9 were knocked out in gamma - sarcoglycan-deficient mice. The study found that up-regulation of MMP-14 is capable of cleaving beta-DG, and it may be involved in the pathogenesis of sarcoglycanopathy. PMID: 28821434
  18. NH2-terminal truncated MMP-2 "primes" the kidney to enhanced susceptibility to I-R injury via induction of mitochondrial dysfunction. PMID: 28331061
  19. Study demonstrated evidence of beta-dystroglycan cleavage by matrix metalloproteinase-2/-9 in permanent middle cerebral artery occlusion mouse brains; this cleavage was implicated in aquaporin-4 redistribution and brain edema in cerebral ischemia. PMID: 27038751
  20. These results indicate that increased MMP2 and MMP9 activity in the brains of mouse adenovirus type 1-infected susceptible mice may be due to MMP activity produced by endothelial cells, astrocytes, and microglia, which in turn may contribute to blood-brain barrier disruption and encephalitis in susceptible mice. PMID: 28053109
  21. Studies define a novel HMGA1-MMP-2 pathway involved in a subset of human carcinosarcomas and tumor progression in murine models. PMID: 27001612
  22. activation of astrocyte MMP2/JNK1/2 contributes to the pathogenesis of pain hypersensitivity in the complex regional pain syndrome model PMID: 27919822
  23. Ceramide 1-phosphate -stimulated macrophage migration is a receptor mediated effect, and point to MMP-2 and -9 as possible therapeutic targets to control inflammation. PMID: 27164414
  24. MMP-2 potentiates shear-induced platelet activation by enhancing thrombus formation PMID: 26510894
  25. Identify novel MMP-2/cardiac sPLA2 pathway that endows the heart with important endocrine functions, including regulation of inflammation and lipid metabolism in the liver. PMID: 26567374
  26. 129/SvEv mice are more susceptible to abdominal aortic aneurysms compared to C57Bl/6 mice and suggest roles for MMP2/9. PMID: 26546710
  27. Report cross-talk between macrophages, smooth muscle cells, and endothelial cells in response to cigarette smoke alters MMP2/9 levels. PMID: 26318311
  28. MMP-2 silenced hypoxic fibroblasts under hyperglycemic conditions have impaired angiogenic potential. Collagen I/IV secretion is decreased and cell migration is prevented. PMID: 26985676
  29. N-terminal truncated isoform-MMP-2, but not full-length-MMP-2, is the major isoform of MMP-2 involved in skeletal muscle Ischemia-reperfusion injury. PMID: 26213293
  30. These data indicate that oxygen-glucose deprivation-triggered Cav-1 S-nitrosylation interacts with tPA-induced ERK activation to augment MMP2 and 9 secretion and subsequent extracellular matrix degradation. PMID: 26881424
  31. Type IV collagenases, MMP-2 and MMP-9, play important roles in hair cycle, and this could be mediated by induced expression of VEGF, IGF-1, and TGF-beta. PMID: 26451090
  32. Matrix Metalloproteinase-2 Knockout and Heterozygote Mice Are Protected from Hydronephrosis and Kidney Fibrosis after Unilateral Ureteral Obstruction PMID: 26673451
  33. Early MMP-2/MMP-9 activity is not a determinant of long-term recovery after traumatic brain injury in the immature mouse. PMID: 26588471
  34. Taken together, these findings indicate for the first time that AnxA2 phosphorylation and actin remodeling evoked by oxidative stress depend on the sphingolipid pathway, via MMP2 and p38MAPK. PMID: 25574848
  35. Matrix Metalloproteinase-2 (MMP-2) Gene Deletion Enhances MMP-9 Activity, Impairs PARP-1 Degradation, and Exacerbates Hepatic Ischemia and Reperfusion Injury in Mice PMID: 26355684
  36. OPN might be responsible for vascular remodeling diseases associated with hypertension by increasing MMP-2 production in vascluar smooth muscle cells. PMID: 25986148
  37. Further investigation of MMP2 inhibitors of TIMP2/TIMP4 showed an upregulated TIMP2 expression, but not TIMP4. low-dose pre-radiation attenuates the skin inflammation and ROS production induced by medium-dose UV radiation PMID: 26133107
  38. negatively regulates cardiac secreted phospholipase A2 to modulate inflammation and fever PMID: 25820137
  39. Data show that discoidin domain receptor (DDR) 2 siRNA-mediated suppression of extracellular regulated kinase (ERK) 1 and 2 and nuclear factor of kappa B (NF-kappaB) could down-regulate the expressions of matrix metalloproteinase (MMP) 2 and 9. PMID: 25733533
  40. Findings indicate the importance of MMP-2 in central nervous system development and dendritogenesis, and highlight the importance of a correct developmental wiring for adult brain morphology and function. PMID: 24652381
  41. Dietary supplementation with n-3 PUFAs may have protective anti-inflammatory effects mediated through modulation of MMPs and TIMPs PMID: 25512019
  42. Cytokine-induced MMP-2 activity specifically at the inflammatory border collectively act to accelerate leukocyte chemotaxis across the parenchymal border. PMID: 25704809
  43. MMP2/9 expression and activity are elevated in lacrimal glands of two murine models of Sjogren's syndrome, suggesting that manipulation of MMP2/9 activity might be a potential therapeutic target in chronically inflamed lacrimal glands. PMID: 26244298
  44. Data indicate that gelatinase A (MMP-2) deficient embryonic fibroblasts show reduced differentiation into adipocytes. PMID: 25869489
  45. beta-elemene downregulates expression of uPA, uPAR, MMP-2, and MMP-9 in a murine intraocular melanoma model PMID: 25405459
  46. Smoking equivalent levels of nicotine exposure induces VCAM-1, MMP-2, and MMP-9 expression. PMID: 25381636
  47. PDGF-D intensifies fibrogenesis by interfering with the fibrolytic activity of the TIMP-1/MMP-2/MMP-9 system, and PDGF-D signaling is mediated through both PDGF-alpha and -beta receptors. PMID: 25576870
  48. PPARdelta-mediated modulation of MMP-2 secretion and elastin expression may contribute to the maintenance of skin integrity by inhibiting ROS generation PMID: 25149191
  49. Study reveals the dual role of MMP2 in ECM degradation, as well as ECM synthesis in pathogenesis of thoracic aortic aneurysms. PMID: 25657308
  50. In conclusion, ATRA may increase expression of MMP-2 and MMP-9 by the potential signal pathway of RAR-alpha and RAR-gamma in injury podocyte induced by adriamycin, but not RAR-beta. PMID: 24694005

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Subcellular Location
[Isoform 1]: Secreted, extracellular space, extracellular matrix. Membrane. Nucleus.; [Isoform 2]: Cytoplasm. Mitochondrion.
Protein Families
Peptidase M10A family
Database Links
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