Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-9 (92-kDa gelatinase, collagenase-IV) is involved in a number of diseases such as cancer, angiogenesis, alopecia, and metastasis. MMP-9 is secreted as zymogen with prodomain, gelatin-binding domain consisting of three contiguous fibronectin type II units, catalytic domain, proline-rich linker region, and C-terminal hemopexin-like domain. It can degrade a variety of substrates, including gelatin, collagens type IV, V, XIV, a2-macroglobulin, elastin, vitronectin, and proteoglycans.

The sequence (Accession # NP_004985.2) corresponding to the catalytic domain (aa 112-445) of Human MMP-9 was expressed in E. coli. The recombinant human MMP-9 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Human MMP-9 Catalytic Domain is ~40 kDa.

40 kDa.