Pro-Matrix Metalloproteinase 9 (PRO MMP-9)

Protein Length: Ala20-Asp707. Protein Tag: N terminal containing a HIS tag. Matrix metalloproteinases are a family of zinc- and calcium-dependant 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 collagenhomologous 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. RANDOX recombinant human Pro-MMP-9 comprises a 688aa fragment (20-707) corresponding to the pro form of the protein minus the signal peptide 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