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 specificities, 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 52-56kD glycosylated proenzyme. Upon cleavage the 22-46kD 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.
Source:Recombinant protein corresponding to human MMP-13, a single, non-glycosylated, polypeptide chain, expressed in E. coli.
Molecular Weight:~27kD
Biological Activity:Determined by the cleavage of fluorogenic peptide, 100ng of enzyme activated with APMA will digest 80% fluorogenic peptide substrate (0.1ml of 20uM solution) at 35°C for 30 minutes, (10ug=100 assays).
Applications:Suitable for use as a standard for assaying MMP-13 or for screening inhibitors. Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
仕様
Size：1ug
Source Antigen：Recombinant, E. coli
Grade：Purified
Purity：~90% (SDS-PAGE)
Form：Supplied as a liquid in 0.05M Tris-HCl buffer, pH 7.5, 0.2M sodium chloride, 5mM calcium chloride, 20uM ZnSO4, 0.1% BSA.
