All MMP7 reagents are produced in house and quality controlled, including 16 MMP7 Gene, 1 MMP7 Lysate, 1 MMP7 Protein, 2 MMP7 qPCR. All MMP7 reagents are ready to use.
Recombinant MMP7 proteins are expressed by HEK293 Cells with fusion tags as N-human IgG1-Fc.
MMP7 cDNA clones are full length sequence confirmed and expression validated. There are 13 kinds of tags for each MMP7 of different species, especially GFP tag, OFP tag, FLAG tag and so on. There are three kinds of vectors for choice, cloning vector, expression vector and lentivrial expression vector.
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological and pathological processes such as morphogenesis, differentiation, angiogenesis, tissue remodeling, and tumor invasion. MMPs are synthesized as pro-enzymes and converted to active form by extracellular proteinases. MMP7, also referred to as matrilysin, is the smallest member of the MMP family and differs from other MMP members in that it lacks the C-terminal hemopexin-like domain. MMP7 is produced primarily by mucosal epithelia, and is capable of degrading various ECM proteins including proteoglycans, fibronectin, elastin and casein. This enzyme serves essential functions in both innate defense and wound healing, and appears to be one of the most important MMPs in human colon cancers. It has been reported that MMP7 contributes to tumor malignancy probably by cleaving cell surface proteins such as Fas ligand, degradation of IgG or inducing E-cadherin-mediated cell aggregation. In addition, matrilysin is also identified as a mediator of pulmonary fibrosis and a potential therapeutic target.
Muller D., et al.,(1988), The collagenase gene family in humans consists of at least four members. Biochem. J. 253:187-192.
Marti H.P., et al., (1992), Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1.Biochem. J. 285:899-905.
Gaire M., et al.,(1994), Structure and expression of the human gene for the matrix metalloproteinase matrilysin.J. Biol. Chem. 269:2032-2040.