The matrix metalloproteinases (MMPs) constitute a family of zinc-dependent endopeptidases that function within the extracellular matrix. These enzymes are responsible for the breakdown of connective tissues and are important in bone remodeling, menstrual cycle and the repair of tissue damage. MMP-13 (collagenase-3), is a member of the MMP family of extracellular proteases. Targets of MMP-13 include collagen, gelatin, aggracan, plasminogen and CXCL12. The native MMP-13 is secreted as a 60-kDa proenzyme, and activated by cleavage to a mature 48-kDa MMP-13.
The sequence (Accession # 1EUB_A) corresponding to the catalytic domain (aa 104-274 aa) of human MMP-13 was expressed with 6-his tag in E. coli. The molecular weight of the recombinant Human MMP-13 catalytic Domain is 20.5 kDa.