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Collagenase 3, EC 3.4.24.-, Matrix metalloproteinase-13, MMP-13, CLG3.
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-a, 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.
Matrix Metalloproteinase-13 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 27 kDa.
The Collagenase 3 is purified by proprietary chromatographic techniques.
Escherichia Coli.
Sterile Filtered clear solution.
The protein Solution (100 µg/ml) in 0.05M Tris-HCl buffer, pH 7.6, containing 0.2M NaCl, 5mM CaCl2, 20µM ZnSO4 and 0.1% BSA and NaN3.
MMP-13 although stable at 14°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze-thaw cycles.
Greater than 90% as determined by SDS-PAGE.
Activity is determined by the cleavage of fluorogenic peptide, 100 ng of enzyme activated with APMA will digest 75-80% (1.5-1.6 nmole) of fluorogenic peptide substrate (0.1ml of 20µM solution) at 35°C for 30 minutes.
Used as a standard for assaying MMP-13 or for screening inhibitors.
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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