Sandwich ELISA quantitative detection kit for Human MMP-7 in cell culture supernates, serum, plasma (heparin), saliva and urine.
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.1 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.2 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.1 Matrilysin is also a mediator of pulmonary fibrosis and a potential therapeutic target.3 The standard product used in this kit is recombinant human MMP-7, consisting of 250 amino acids with the molecular mass of 28kD. The detected MMP-7 includes zymogen and active enzyme.
Assay Range:156pg/ml-10,000pg/ml
Sensitivity:< 6 pg/ml
Crossreactivity:There is no detectable cross-reactivity with other relevant proteins.
