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Recombinant Human MMP-1



Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-1 is a secreted collagenase with specificity toward Type I, II, III, VII, and X collagens. Recombinant Human MMP-1 is a 42.7 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain, which is involved in substrate specificity, and in binding TIMP-1.


  • Gene Id: 4312
  • Uniprot: P03956
  • Activity: MMP-1 activity was measured by its ability to cleave a chromogenic peptide MMP-1 substrate at room temperature. At an MMP-1 concentration of 2.5 ug/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes.
  • Category: RUO Cytokines
  • Subcategory: Proteases
  • Research Areas: Angiogenesis/Cardiovascular, Bone, Skeletal, Cartilage, Cancer, Immune System, Inflammation, Wound Healing
  • Alternative Names: Matrix Metalloproteinase-1, Fibroblast Collagenase, Interstitial Collagenase
  • Species of Origin: Human
  • Expression System Source: E.coli