MMP-13, human, recombinant
Recombinant Human Matrix Metalloproteinase 13
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.
|Molecular Mass||see Description|
|Specific Activity||see below|
|Biological Activity||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.|
|Formulation||Sterile-filtered, clear solution (100 units/ml) in 0.05 M Tris-HCl buffer (pH 7.6), containing 0.2 M NaCl, 5 mM CaCl₂, 20 µM ZnSO₄, 0.0025% NaN₃ and 0.1% BSA.|
|Reconstitution||Please Note: Always centrifuge product briefly before opening vial. The dissolved protein can be diluted into other aqueous buffers and stored at -20°C for future use.|
|Purity||Greater than 90% as determined by SDS-PAGE analysis.|
|Stability & Storage||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.|