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.
Human MMP1 expressed in E.coli
CAT# CSC-CTK0368-10 (10 μg); CAT# CSC-CTK0368-50 (50 μg)
Greater than 98% as determined by HPLC and SDS-PAGE analysis.
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.
Less than 1 EU/μg.
Lyophilized from a sterile-filtered protein soluti on in 10 mM sodium phosphate (pH 7.5) and 0.1 mM calcium chloride.
Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 0.1 - 1.0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein should be used immediately or stored long-term in undiluted working aliquots at -20°C. Avoid repeated freeze-thaw cycles.
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