420-01
Scientist.com Supplier
Recombinant Human MMP-1
PeproTech
DESCRIPTION
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.
DETAILS
- 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
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