Matrix Metalloproteinase (MMP) Inhibitors & Substrates

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CAT# Product Name M.W Molecular Formula Inquiry
M3001 Z-Pro-Leu-Gly-NHOH 434.49 Inquiry
M3004 Peptide 74 1558.81 Inquiry
M3005 H-Pro-Leu-Gly-NHOH . HCl 336.82 Inquiry
M3006 Z-Pro-Leu-Ala-NHOH 448.52 Inquiry
M3007 Z-Pro-D-Leu-D-Ala-NHOH 448.52 Inquiry
M3008 4-Abz-Gly-Pro-D-Leu-D-Ala-NHOH 490.56 Inquiry
M3103 Ac-Pro-Leu-Gly-[(S)-2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OEt 655.86 Inquiry
M3109 Dnp-Pro-β-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2 1077.23 Inquiry
M3115 6-(7-Nitro-benzo[2,1,3]oxadiazol-4-ylamino)-hexanoyl-Arg-Pro-Lys-Pro-Leu-Ala-Nva-Trp-Lys((7-dimethylaminocoumarin-4-yl)-acetyl)-NH2 1598.87 Inquiry
M3117 Mca-(Ala7,Lys(Dnp)9)-Bradykinin 1388.46 Inquiry
M3118 DABCYL-γ-Abu-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Glu(EDANS)-Ala-Lys-NH2 2078.48 Inquiry
M3119 DABCYL-γ-Abu-Pro-Gln-Gly-Leu-Glu(EDANS)-Ala-Lys-NH2 1325.56 Inquiry
M3123 Dnp-(Leu421)-Collagen Type VIII α1 Chain (419-426) amide (human, mouse) 965.1 Inquiry
R1311 CTTHWGFTLC, CYCLIC 1166.33 C₅₂H₇₁N₁₃O₁₄S₂ Inquiry

Matrix metalloproteinases (MMPs) is an enzyme that decomposes extracellular matrix (ECM) proteins. They play an important role in both normal and diseased cells. Proteases plays an important role in many diseases. Extracellular protein hydrolase is the material required for the passage of tumor cells. Hydrolyzing ECM protein is necessary for the migration of invasive tumor. In addition, vascular hyperplasia, which supports tumor growth, also hydrolyzes ECM protein by invading epidermal cells. There are four kinds of endopeptidases: serine protease, cystine protease, aspartyl protease, substrate attribute protease, all of which are related to the development and migration of more than one tumor. MMPs is the most important of the four proteases in the development of tumor.

Types of MMPs

  • There are three kinds of gelatinase typeⅠ: interspace zymogenase, neutrophil collagenase and collagenase, all of which can decompose typeⅠ,Ⅱand Ⅲ types of fibrillar collagens.
  • TypeⅡ contains two kinds of 72kDa, 92kDa gelatinases and metalloelastase, which can decompose type Ⅳ andⅤbasal lamina non-maintenance collagen, It can also decompose type VII collagen and fibronectin, X short chained collagen, elastic protein and gold attribute protease .
  • Type Ⅲ is composed of stromelysin-1, lysin-2 and matrilysin, which can decompose proteoglycan, binding protein and laminin in type Ⅳ and type X collagen.
  • MRNA in situ hybridization confirmed that lysin-3 is very important for malignant diseases, and its proteolytic function has been described. Membrane-type metalloproteinases (MT-MMP) have been found, MT-MMP can be combined on the cell membrane is there, MT-MMP is a special activate progelatinase A. Since its initial discovery, the genes of MT-MMP have been identified, and these enzymes are temporarily in type Ⅳ of MMP.

The role of MMPs in tumor

The decomposition ability of MMPs is related to the time of enzyme secretion and inhibitor, which includes general blood protease inhibitors, such as a2-macroglobulin, as well as special inhibitors, such as TIMP-1, TIMP-2, and TIMP-3. A number of diseases, such as inflammation, sclerosis, and cancer, are associated with imbalances between enzymes and inhibitors, which cause extracellular matrix to break down. Studies have shown that the force of MMP in the process of cancer development will be greater than the inhibition of the agent, MMP helps the proliferation and aggression of the first grade tumor, the cells of the tumor to pass through the vascular cell wall, and the growth and invasion of the second stage tumor. In addition, MMP also helps to promote the proliferation and invasion of the first grade tumor, the cell wall of the blood vessel, and the growth and invasion of the second stage tumor.


  1. Morrison, C. J., Butler, G. S., Rodríguez, D., & Overall, C. M. (2009). Matrix metalloproteinase proteomics: substrates, targets, and therapy. Current opinion in cell biology, 21(5), 645-653.
  2. Radisky, E. S., Raeeszadeh‐Sarmazdeh, M., & Radisky, D. C. (2017). Therapeutic potential of matrix metalloproteinase inhibition in breast cancer. Journal of cellular biochemistry, 118(11), 3531-354
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