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MMP

Matrix metalloproteinase (MMP) inhibitors block zinc endopeptidases that degrade collagen and other matrix proteins. The first such activity, a collagenase, was detected in amphibian tissue culture in 1962. MMPs remodel tissue during development and wound repair, and they help tumor cells invade surrounding matrix. Membrane type 1 MMP (MT1-MMP, MMP-14), described in 1994, is anchored on the surface of invasive tumor cells. Batimastat, marimastat and GM 6001 are hydroxamate compounds that chelate the catalytic zinc and inhibit a wide range of MMPs. More selective tools include NSC 405020 for MT1-MMP and T-26c for MMP-13. Metalloproteases of the related ADAM family are listed in the neighboring ADAMs category.

2 Items

  • Hinokiflavone
    Cat. No.
    A24549
    CAS No.
    19202-36-9

    Hinokiflavone

    Hinokiflavone is a naturally occurring biflavonoid isolated from plants, recognized as a novel modulator of pre-mRNA splicing. It exhibits diverse biological activities, including anti-inflammatory, antitumor, and antiviral effects. Mechanistically, Hinokiflavone acts as a potent inhibitor of matrix metalloproteinases (MMPs) and suppresses the virulence of methicillin-resistant Staphylococcus aureus (MRSA) by targeting caseinolytic protease P (ClpP) with an IC₅₀ of 34.36 µg/mL. In cancer models, Hinokiflavone triggers apoptosis through a reactive oxygen species (ROS)-dependent, mitochondria-mediated pathway and suppresses tumor cell migration and invasion. Additionally, it functions as a SUMO protease inhibitor, effectively blocking sentrin-specific protease 1 (SENP1) activity.

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    1 mg
    $23.00
    5 mg
    $68.00
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  • Mca-Pro-Leu-Gly-Leu-Glu-Glu-Ala-Dap(Dnp)-NH2
    Cat. No.
    A76861
    CAS No.
    891198-38-2

    Mca-Pro-Leu-Gly-Leu-Glu-Glu-Ala-Dap(Dnp)-NH2

    Mca-Pro-Leu-Gly-Leu-Glu-Glu-Ala-Dap(Dnp)-NH2 is a highly selective substrate for matrix metalloproteinase 12 (MMP12), exhibiting a kcat/Km value of 1.85 x 10^5 M^-1s^-1. This compound shows limited activity against other matrix metalloproteinases, with notable kcat/Km values of 0.53 x 10^5 M^-1s^-1 for MMP13 and 0.33 x 10^5 M^-1s^-1 for MMP9. This selective profile makes it a useful tool for studying the role of MMP12 in biological processes and for potential therapeutic applications targeting MMP-related pathways.

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