- Created on the 5 May, 2017.
Matrix metalloproteinase-7 (MMP-7, matrilysin, uterine metalloproteinase or pump-1 protease), consists of structural-related zinc-dependent endopeptidases. It is a protein which is bound by 4 metal ions (including catalytic zinc ion), 2 calcium ions and a structural zinc ion. The main function of MMP7 is to break-down extracellular matrix using macromolecules such as casein, proteoglycan, fibronectin and gelatins. The protein itself is usually secreted as zymogen and the prodoamin contains approx. 9 kD of highly conserved cysteine switch that is located near the C-terminal containing cysteine residues.
MMP-7 is identified to be potentially associated with tumor metastasis and a number inflammatory processes. It has be found to be upregulated in many malignant tumors such as stomach, liver, esophagus, pancreas, renal and colon cell carcinomas. MMP7 has the ability to cleave cell surface proteins and to promote the adhesion of cancer cells and therefore increase the likely hood of tumor metastasis.
Human MMP-7 ELISA kit is a method designed for detecting in vitro quantitative amounts of matrix metalloproteinase-7 (matrilysin, pump-1 protease, uterine metalloproteinase, MMP7) in human serum, cell culture supernatant, cell lysates, other biological fluids and plasma. This assay has a minimum sensitivity limit of 0.026 ng/mL.
The minimum detection sensitivity level of human MMP-7 (uterine metalloproteinase, matrilysin, pump-1 protease) using this human matrix metalloproteinase-7 ELISA kit was 0.026 ng/mL. The dynamic assay range for this kit is 0.05 – 15 ng/mL.
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- Full Name: Matrix Metalloproteinase-7 (MMP-7) ELISA Kit
- Reactivity: Human
- Sample Type: Other Biological Fluids, Plasma, Cell Lysates, Cell Culture Supernatant, Serum
- Sensitivity: 0.026 ng/mL