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.