Description
Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases, which degrade extracellular matrix proteins. MMP-9 is secreted as a 92kDa zymogen. Cleavage of pro-MMP-9 results in the active enzyme with a molecular weight of ~82kDa. MMP-9 has a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells, and is involved in inflammatory responses, tissue remodelling, wound healing, tumour growth and metastasis. Our recombinant human MMP-9 comprises a 338aa fragment (113-450) corresponding to the catalytic domain of the protein and is expressed in E. coli with an N-terminal 6xHis tag. This product is for research use only and is not intended for diagnostic or therapeutic use