Description
Background: Matrix metalloproteinase-7 (MMP-7) previously called putative metalloproteinase I (PUMP1) or matrilysin. The PUMP1 gene has been identified through studies of collagenase-related connective-tissue-degrading metalloproteinases produced by human tumors. The PUMP I protein has 267 amino acids and is significantly shorter than stromelysin or collagenase (477 and 469 amino acids, respectively). Matrix metalloproteinases play a crucial role in tumor invasion and metastasis. Matrilysin, a member of the matrix metalloproteinase family, is structurally different from the other matrix metalloproteinases by virtue of the absence of a conserved COOH-terminal protein domain. In addition, matrilysin mRNA is regulated in a specific and distinct manner in normal and malignant tissues. Matrilysin has been shown to correlate with nodal or distant metastasis in colorectal carcinomas; however, its implication in early invasive colorectal carcinomas has not been determined. Matrilysin is also a mediator of pulmonary fibrosis and a potential therapeutic target.
Principle of the Assay: The Human MMP7 ELISA (Enzyme-Linked Immunosorbent Assay) kit is an in vitro enzyme-linked immunosorbent assay for the quantitative measurement of Human MMP7 in Cell Culture Supernatants, Serum, Plasma, Urine. This assay employs an antibody specific for Human MMP7 coated on a 96-well plate. Standards and samples are pipetted into the wells and MMP7 present in a sample is bound to the wells by the immobilized antibody. The wells are washed and biotinylated anti-Human MMP7 antibody is added. After washing away unbound biotinylated antibody, HRP-conjugated streptavidin is pipetted to the wells. The wells are again washed, a TMB substrate solution is added to the wells and color develops in proportion to the amount of MMP7 bound. The Stop Solution changes the color from blue to yellow, and the intensity of the color is measured at 450 nm