Recombinant Human MMP-1
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
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. |
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BiologicalActivity | 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 μg/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes |
Authenticity | Verified by N-terminal and Mass Spectrometry analyses (when applicable). |
Endotoxin | Endotoxin level is <0.1 ng/ µg of protein (<1EU/ µg). |
Protein Content | Verified by UV Spectroscopy and/or SDS-PAGE gel. |
Storage | -20°C |
Precautions | Recombinant Human MMP-1 is for research use only and not for use in diagnostic or therapeutic procedures. |
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