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).
Amino Acid Sequence
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.
Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.5–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C.