Recombinant Human MMP-9 Activated Protein, CF

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Recombinant human Active Matrix Metalloproteinase 9 (MMP-9), also known as gelatinase B, is a member of the MMP family of zinc and calcium-dependent endopeptidases. MMP-9 protein is synthesized as a pre-proenzyme in specific cells such as neutrophils, macrophages, fibroblasts and endothelial cells (1). Expressed MMP-9 contains a signal peptide to transport it to the extracellular matrix (ECM), a hinge region, a propeptide region, a catalytic domain, and a hemopexin-like domain that is important for substrate recognition (2, 3).  In addition to having three fibronectin type II domains that contribute to substrate binding and an active site, the catalytic domain of MMP-9 also contains a zinc-binding region that interacts with a cysteine in the propeptide to maintain latency. Consequently, removal of the propeptide through cleavage by proteases in the ECM, such as MMP-3, activates the protein (2, 3). MMP-9 has specificity for targets containing an established preferred consensus sequence (3-5) and has a broad range of substrates within the ECM including gelatin, collagen, elastin that contributes to its role in ECM remodeling and extracellular domain cell surface protein release from the plasma membrane (3). Due to its activity in the ECM, MMP-9 plays a role in many biological processes and can serve as a biomarker in tumor invasion and mestastasis (3, 6) of many cancers including colon, ovarian, breast, osteosarcoma, and lung cancers (7-11) making it a therapeutic target (6, 8, 12). MMP-9 modeling of the ECM also leads to a pivotal role in other inflammation- and autoimmune-related diseases (3, 13, 14).

Array 11602-MP

• MMP-9 Antibodies
• MMP-9 Antibody Pairs
• MMP-9 ELISA Kits
• MMP-9 Lysate
• MMP-9 Proteins
• MMP-9 ELISAs
• MMP-9 Proteins and Enzymes