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-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. Recombinant human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).
Catalog #:
420-02
Source :
E.coli
Purity :
Greater than 90% by SDS-PAGE gel and HPLC analyses.
Endotoxin Level :
Endotoxin level is less than 0.1 ng per μg (1EU/μg).
Biological Activity :
MMP-2 activity was measured by its ability to cleave a chromogenic peptide MMP-2 substrate at room temperature. At an MMP-2 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes.