Latent recombinant human pro-collagenase (MMP-13) also called collagenase-3 truncated from C-terminal. Matrix Metalloproteinase-13 (MMP-13) is an enzyme that is a member of the MMP extracellular protease family. Extracellular protease enzymes, by virtue of their broad substrate specificities1, play a role in both normal and disease states of tissue proliferation. Among the targets of MMP- 13 are collagen, gelatin, entactin, pro-TNF-alpha, and chemokine SDF-11-4. MMP-13 is found in its latent form as a 52-56 kDa glycosylated proenzyme. Upon cleavage the 22-46 kDa5 MMP-1 becomes active in extracellular matrix remodeling. Because of the prominent role that MMP-1 plays in cell migration and metastasis, it is an important target for inhibition screening. Human recombinant Matrix Metalloproteinase-13 produced in E. coli is a single, non- glycosylated, polypeptide chain having a molecular mass of 27 kDa.
Human MMP13 expressed in E.coli
CAT# CSC-CTK0374-25 2.5 μg; CAT# CSC-CTK0374-125 (125 μg)
Greater than 90% as determined by SDS-PAGE analysis.
Activity is determined by the cleavage of a fluorogenic peptide; 100 ng of enzyme activated with APMA will digest 75-80% (1.5-1.6 nmole) of fluorogenic peptide substrate (0.1 ml of 20 μM solution) at 35°C for 30 minutes.
Sterile-filtered, clear solution (100 units/ml) in 0.05 M Tris-HCl buffer (pH 7.6), containing 0.2 M NaCl, 5 mM CaCl , 20 μM ZnSO , 0.0025% NaN and 0.1% BSA.
Please centrifuge product briefly before opening vial. The dissolved protein can be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
Store at 4°C if entire vial will be used within 1 week. Store frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles. Applications Used as a standard for assaying MMP-13 or for screening inhibitors.
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