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Human Matrix metalloproteinase 7,MMP-7 ELISA kit
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Human Matrix metalloproteinase 7,MMP-7 ELISA kit
Sandwich quantitative immunoassay for matrix metallopeptidase 7 (matrilysin, uterine) in human serum, plasma, tissue homogenates available in multiple catalog sizes:
Note: Please send inquiries regarding Trial 24T orders to support@diagnocine.com.
| Target name | matrix metallopeptidase 7 (matrilysin, uterine) |
| Uniprot No. | P09237 |
| Species | Homo sapiens (Human) |
| Sample types | serum, plasma, tissue homogenates |
| Detection range | 78 pg/mL-5000 pg/mL |
| Sensitivity | 19.5 pg/mL |
| Assay time | 1-5h |
| Sample loading volume | 50-100μL |
| Detection wavelength | 450 nm |
| Assay principle | Sandwich (Quantitative) |
| Data analysis | Standard curve + Curve Expert software |
| Research area | Cancer |
| Storage condition | 2-8°C (see protocol for full details) |
| Shipping condition | 4 °C |
| Shelf life | 6 months |
10 business days
Processing + 3-5 days shipping
In Stock : USA
Worldwide shipping available
Antibody capture
450 nm detection
Standard curve
Quantification
In this sandwich ELISA, matrix metallopeptidase 7 (matrilysin, uterine) in the sample is captured between a pre-coated capture antibody and a detection antibody. Signal intensity is proportional to analyte concentration. Quantification uses a standard curve fitted with Curve Expert software, covering 78 pg/mL-5000 pg/mL with a minimum detectable dose of 19.5 pg/mL.
The product CSB-E04679h is a sandwich ELISA kit developed to measure levels of human matrix metalloproteinase 7 (MMP7) in serum, plasma, or tissue homogenates. The enzyme-substrate chromogenic reaction is also used to amplify the signal and quantify the levels of the analyte through the intensity of the colored product. The color intensity positively correlates with the amount of MMP7 bound in the initial step.
MMP7 is a secreted protease that is expressed by glandular and mucosal epithelial cells, keratinocytes, fibroblasts, and macrophages and secretes zinc and calcium endopeptidases. Like other MMPs, MMP7 can act on the extracellular matrix and thereby regulate cell migration, bone growth, wound healing, remodeling, and tissue repair. Additionally, MMP7 plays an important role in the maintenance of innate immunity in organs such as the lungs and intestines where it proteolytically activates anti-bacterial peptides such as pro-defensins. MMP7 has been demonstrated to modulate the occurrence and development of cancers and mediate the proliferation, differentiation, metastasis, and invasion of several types of cancer cells via various mechanisms.
- These findings suggest the usefulness of combining MMP-7 with CA 125 and HE4 in the diagnosis of epithelial ovarian cancer as a new tumor marker panel. PMID: 28662671
- results suggest that MMP-7 might be involved in the pathogenesis of H. pylori; peptic ulcer was associated with cag pathogenicity island-dependent MMP-7 upregulation PMID: 28699830
- Data suggest that the cytoplasmic domain of Sdc2 is involved in regulation of expression of MMP7 in colon carcinoma/adenocarcinoma cells; induction of MMP7 involves protein kinase C gamma-mediated FAK/ERK signaling. (Sdc2 = syndecan-2; MMP7 = matrix metalloproteinase-7; FAK = focal adhesion kinase 1) PMID: 28821612
- Matrix Metalloproteinase-7 Promoter polymorphism is associated with breast Cancer. PMID: 28870920
- The results demonstrate that MMP-7 may play an important role in the defensive mechanism against the aggregation of amyloid beta (1-42), which gives rise to the pathology of Alzheimer's disease. PMID: 28871443
- Results provide evidence that MMP7 expression is regulated by leptin through ERK and JNK pathways to modulate cell invasion of ovarian neoplasm. PMID: 28885729
- Higher serum MMP-7 levels were independently associated with renal fibrosis and poor prognosis in IgA Nephropathy. PMID: 28922659
- Data suggest that HAI1, a protease on the surface of colon carcinoma cells, is an MMP7 substrate; proteolysis by MMP7 releases extracellular region as soluble HAI1 (sHAI1); sHAI1 induces cancer cell aggregation; cholesterol sulfate is required for MMP-7--catalyzed generation of sHAI1. (HAI1 = hepatocyte growth factor activator inhibitor type 1; MMP7 = matrix metalloproteinase-7) PMID: 29046355
- Results indicate that the matrix metallopeptidase 7 (MMP7)A-181G genotype interacts with age and gender and may serve as an early and predictive biomarker for childhood acute lymphoblastic leukemia (ALL). PMID: 29187444
- MMP-7(-181A/G) polymorphisms associate with obesity risk and its severity. PMID: 29317790
- the anti-tumor activity of oleuropein against hepatocellular carcinoma could be attributed to influencing the pro-NGF/NGF balance via affecting MMP-7 activity without affecting the gene expression of NGF PMID: 29476769
- MMP7 promoter genotypes only play an indirect role in determining the personal susceptibility to oral cancer in Taiwan. PMID: 29599326
- CTHRC1 serves as a pro-metastatic gene that contributes to NSCLC invasion and metastasis, which are mediated by upregulated MMP7 and MMP9 expression. Targeting CTHRC1 may be beneficial for inhibiting NSCLC metastasis. PMID: 29631554
- MMP-7 A-181G may play an indirect role in determining personal susceptibility to Colorectal Cancer. PMID: 29695403
- among HPV-positive OPSCC patients, high MMP-7 expression is related to worse 5-year DSS and increased rate of distant recurrences PMID: 29721609
- no difference in the expression of MMP-7 and TIMP-1 in the endometrium in relation to hormone levels and menstrual cycle phases were observed PMID: 30187906
- Absence of MMP-7 Promoter Polymorphisms is associated with Lung Cancer Susceptibility. PMID: 30275186
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. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed. | ||||||||||||
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pg/ml | OD1 | OD2 | Average | Corrected | ||||||||
5000 | 2.715 | 2.625 | 2.670 | 2.526 | ||||||||
2500 | 2.156 | 2.249 | 2.203 | 2.059 | ||||||||
1250 | 1.435 | 1.384 | 1.410 | 1.266 | ||||||||
625 | 0.860 | 0.799 | 0.830 | 0.686 | ||||||||
312 | 0.498 | 0.467 | 0.483 | 0.339 | ||||||||
156 | 0.289 | 0.271 | 0.280 | 0.136 | ||||||||
78 | 0.215 | 0.211 | 0.213 | 0.069 | ||||||||
0 | 0.145 | 0.142 | 0.144 |
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To assess the linearity of the assay, samples were spiked with high concentrations of human MMP-7 in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay. | ||||||||||||
| Sample | Serum(n=4) | ||||||||||
1:1 | Average % | 104 | ||||||||||
Range % | 100-108 | |||||||||||
1:2 | Average % | 88 | ||||||||||
Range % | 84-92 | |||||||||||
1:4 | Average % | 90 | ||||||||||
Range % | 85-98 | |||||||||||
1:8 | Average % | 92 | ||||||||||
Range % | 88-96 | |||||||||||
The recovery of human MMP-7 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 Type | Average % Recovery | Range | ||||||||||
Serum (n=5) | 95 | 90-101 | ||||||||||
Heparin plasma (n=4) | 93 | 89-97 | ||||||||||
