Matrix Metalloproteinases (MMPs)

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CAT# Product Name M.W Molecular Formula Inquiry
M3101 Ac-Pro-Leu-Ala-[(S)-2-mercapto-pentanoyl]-Trp-NH2 642.82 Inquiry
M3102 Abz-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 1110.24 Inquiry
M3104 Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH 992.02 Inquiry
M3106 Mca-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 1093.16 Inquiry
M3107 Dnp-Pro-Leu-Gly-Cys(Me)-His-Ala-D-Arg-NH2 932.03 Inquiry
M3108 Dnp-Pro-β-cyclohexyl-Ala-Abu-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2 1105.29 Inquiry
M3110 Mca-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys(Dnp)-NH2 1656.89 Inquiry
M3111 Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 1675.87 Inquiry
M3112 N-Me-Abz-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 1138.3 Inquiry
M3113 Dnp-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser-OH 1164.29 Inquiry
M3114 Mca-Pro-Lys-Pro-Leu-Ala-Leu-Dap(Dnp)-Ala-Arg-NH2 1332.48 Inquiry
M3116 Mca-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 1221.34 Inquiry
M3120 Mca-Pro-Leu-Ala-Cys(Mob)-Trp-Ala-Arg-Dap(Dnp)-NH2 1403.54 Inquiry
M3121 Mca-Pro-β-cyclohexyl-Ala-Gly-Nva-His-Ala-Dap(Dnp)-NH2 1100.16 Inquiry
M3122 Mca-Pro-Leu-Ala-Nva-Dap(Dnp)-Ala-Arg-NH2 1093.16 Inquiry
M3124 Mca-Pro-Leu-Gly-Leu-Glu-Glu-Ala-Dap(Dnp)-NH2 1195.21 Inquiry
M3125 Elastase Substrate IV, Colorimetric 562.6 Inquiry
M3127 MMP Substrate III, Fluorogenic 1325.6 Inquiry
M3129 MMP Substrate V, Fluorogenic 0 Inquiry
M3131 MMP Substrate, Fluorogenic 977.1 Inquiry


Matrix metalloproteinases (MMPs) are a group of zinc-dependent endopeptidases that are responsible for the degradation of extracellular matrix components, secreted by many cells such as fibroblasts, vascular smooth muscle (VSM), and leukocytesand. They play a crucial role in various physiological and pathologic processes. MMPs consist of a propeptide sequence of about 80 amino acids, a catalytic metalloproteinase domain with catalytic zinc of about 170 amino acids, a hinge region or linker peptide of variable length, and a hemopexin domain of about 200 amino acids. In vertebrates, the MMP family comprises 28 members, at least 23 in human tissues, and 14 of which are expressed in the vasculature. Typically, MMPs are classified according to their substrates and the organization of their structural domains into collagenases, gelatinases, stromelysins, matrilysins, membrane-type (MT)-MMPs, and other MMPs.

Mechanism of action

MMPs are regulated in terms of mRNA expression level and by activation of their latent zymogen form. MMPs are often secreted as inactive form which is cleaved to the active form by various proteinases including other MMPs. MMPs are involved in degradation of ECM proteins such as collagen and elastin, but could influence endothelial cell function as well as VSM cell migration, proliferation, Ca2+ signaling and contraction. MMPs promote cell proliferation, migration, and differentiation, thus playing a role in cell apoptosis, tissue repair, immune response and angiogenesis. MMPs may also affect bioactive molecules on the cell surface and modulate various cellular and signaling pathways.

Application of MMPs

MMPs are associated with different physiological responses, including embryogenesis, vasculogenesis, and cellular remodeling, as well as different disease pathogenesis. MMPs have been proposed as biomarkers for numerous pathological conditions and are potential therapeutic targets in cardiovascular diseases such as atherosclerosis, varicose veins, aneurysms, musculoskeletal disorders such as osteoarthritis and bone resorption, and in various cancers. The imbalance between the expression of MMPs and their inhibitors can be also effective in leukemic cell processes such as migration, angiogenesis, survival, and apoptosis, playing a key role in the progression and prognosis of leukemia.


  1. Kasturi Chatter., jeeSayantan Jana., Preety Choudhary.,&Snehasikta Swarnakar. (2018).Triumph and tumult of matrix metalloproteinases and their crosstalk with eicosanoids in cancer. Cancer and Metastasis Reviews , 37(2-3), 279-288.
  2. Ning Cui., Min Hu., Raouf A. Khalil. (2017). Biochemical and Biological Attributes of Matrix Metalloproteinases. Prog Mol Biol Transl Sci , 147, 1-73.
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