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SensoLyte® 520 MMP-3 Assay Kit

FRET Fluorometric
Catalog No. ABIN1882522
  • Target See all MMP3 Kits
    MMP3 (Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) (MMP3))
    Detection Method
    Fluorometric
    Application
    Fluorescence Resonance Energy Transfer Microscopy (FRET)
    Brand
    SensoLyte®
    Characteristics
    SensoLyte® 520 MMP-3 Assay Kit uses a 5-FAM (fluorophore) and QXL520™ (quencher) labeled FRET peptide substrates for continuous measurement of the enzyme activities. This substrate showed excellent specificity to MMP-3 with minimal cross-reaction with MMP-1, 2, 7, 8, 9, 13 and 14. In an intact FRET peptide, the fluorescence of 5-FAM is quenched by QXL520™. Upon the cleavage of the FRET peptide by MMP-3, the fluorescence of 5-FAM is recovered, and can be continuously monitored at excitation/emission = 490 nm/520 nm. With superior fluorescence quantum yield and longer emission wavelength, 5-FAM/QXL520™ based FRET peptide is less interfered by the autofluorescence of test compounds and cellular components and provides better assay sensitivity.
    Top Product
    Discover our top product MMP3 ELISA Kit
  • Comment

    FRET-based Assay Kit

    Restrictions
    For Research Use only
  • Handling Advice
    Protect Components A and B from light.
    Storage
    -20 °C
    Storage Comment
    Store all components at -20 °C. Components D and E can be stored at 4 °C for convenience.
  • Ozeki, Hase, Hiyama, Yamaguchi, Kawai, Kondo, Nakata, Mogi: "IL-1?-induced, matrix metalloproteinase-3-regulated proliferation of embryonic stem cell-derived odontoblastic cells is mediated by the Wnt5 signaling pathway." in: Experimental cell research, Vol. 328, Issue 1, pp. 69-86, (2014) (PubMed).

    Pifer, Maerz, Baker, Anderson et al.: "Matrix metalloproteinase content and activity in low-platelet, low-leukocyte and high-platelet, high-leukocyte platelet rich plasma (PRP) and the biologic response to PRP by human ligament ..." in: The American journal of sports medicine, Vol. 42, Issue 5, pp. 1211-8, (2014) (PubMed).

    Yamaguchi, Ozeki, Kawai, Tanaka, Hiyama, Nakata, Mogi, Nakamura: "Proinflammatory cytokines induce stromelysin-1-mediated cell proliferation in dental pulp fibroblast-like cells." in: Journal of endodontics, Vol. 40, Issue 1, pp. 89-94, (2013) (PubMed).

    Shin, Kim, Lee, Rhim, Hwang: "Matrix metalloproteinase-3 is activated by HtrA2/Omi in dopaminergic cells: relevance to Parkinson's disease." in: Neurochemistry international, Vol. 60, Issue 3, pp. 249-56, (2012) (PubMed).

    Dayoub, Wagner, Bataille, Stöltzing, Spruss, Buechler, Schlitt, Weiss: "Liver regeneration associated protein (ALR) exhibits antimetastatic potential in hepatocellular carcinoma." in: Molecular medicine (Cambridge, Mass.), Vol. 17, Issue 3-4, pp. 221-8, (2011) (PubMed).

    Koyama, Tanaka: "Endothelins stimulate the production of stromelysin-1 in cultured rat astrocytes." in: Biochemical and biophysical research communications, Vol. 371, Issue 4, pp. 659-63, (2008) (PubMed).

    Woo, Park, Choi, Kim, Kim: "Inhibition of MMP-3 or -9 suppresses lipopolysaccharide-induced expression of proinflammatory cytokines and iNOS in microglia." in: Journal of neurochemistry, Vol. 106, Issue 2, pp. 770-80, (2008) (PubMed).

  • Target
    MMP3 (Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) (MMP3))
    Alternative Name
    MMP-3 (MMP3 Products)
    Background
    Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated proteins capable of digesting extracellular matrix components. The importance of MMPs in tumor development and invasion and other diseases is well known. MMP-3 (stromelysin-1, transin-1) is proposed as a potential therapeutic target.
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