Human MMP-7 Analyte Overview
Also known as MMP-7, MMP7, Matrix Metalloproteinase-7, MPSL1, PUMP-1, Matrilysin, Pump-1 Protease, PUMP-1, Uterine Metalloproteinase
Matrix metalloproteinase 7 (MMP7), also known as matrilysin, pump-1 protease (PUMP-1), or uterine metalloproteinase, is an enzyme that is involved with remodeling tissues. It is a member of the MMP family, a group of structural related zinc-dependent endopeptidases that are involved in breaking down different components of tissue. It is responsible for breaking down extracellular matrixes by degrading macromolecules such as casein, gelatins (type I, II, IV, andV), fibronectin, and proteoglycans. It also generates mature proteases which break down proteoglycans, fibronectin, elastin, and casein. It is critical during processes that require tissue changes, such as embryonic development, reproduction, wound healing, and tissue remodeling, but may also contribute to diseases such as arthritis and tumor metastasis. Upregulation of MMP7 is associated with tumor metastasis in many kinds of cancer, where it promotes the adhesion of cancer cells and facilitates their invasion into other tissues.
Sample Type: Human Serum, EDTA Plasma
Assay Range: 1,800 – 7.41 pg/mL
Volume Required Per Well: Min. 25µL
Detection Method: Chemiluminescent
Singleplex Format: 96-well plate
Features & Requirements
- Sensitive, reproducible, and convenient 96-well format requiring low sample volumes
- Requires the Q-View™ Imaging System for analysis
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