MMP7 Proteins, cDNA Clones Research Reagents

MMP7 (Matrix Metallopeptidase 7, also known as MMP-7; MPSL1; PUMP-1), located on 11q22.2, is conserved in chimpanzee, Rhesus monkey, dog, cow, mouse, rat, chicken, A.thaliana, and rice. The gene produces a 29677 Da protein composed of 267 amino acids. This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). Diseases such as Brain Glioblastoma Multiforme and Rectum Cancer are associated with MMP7. The related pathways of MMP7 include the Degradation of the extracellular matrix and the Wnt signaling pathway.

MMP7 Protein (1)

    MMP7 cDNA Clone (21)

    NM_002423.3

    In lentiviral vector

    NM_010810.4

    MMP7 Lysate (1)

      MMP7 Background

      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 the 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. Besides, matrilysin is also identified as a mediator of pulmonary fibrosis and a potential therapeutic target.

      MMP7 References

      • 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.

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