MMP 13, Human

(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.

Purity: Greater than 90% as determined by SDS-PAGE.

Source: Escherichia Coli.

Physical Appearance: Sterile Filtered clear solution.

Formulation: The MMP-13 protein solution (100 µg/ml) in 0.05M Tris-HCl buffer, pH 7.6, 0.2M NaCl, 5mM CaCl2, 20µM ZnSO4 and 0.1% BSA and 0.0025% NaN3.

MMP 13 General Information

Applications:
Used as a standard for assaying MMP-13 or for screening inhibitors.

Storage:
MMP-13 although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.

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