Cayman MMP-9 Q279R Variant (human, recombinant)

Matrix metalloproteinase-9 (MMP-9) is an endopeptidase and a member of the type IV collagenase subfamily of MMPs that has a major role in tissue remodeling. It is composed of an N-terminal prodomain containing a cysteine switch that interacts with the catalytic domain to regulate the proteolytic activity of MMP-9, a fibronectin-like domain that binds various extracellular matrix (ECM) proteins, and a C-terminal hemopexin-like domain that inhibits the proteolytic activity of MMP-9 by binding tissue inhibitor of metalloproteinases (TIMPs). The Q279R variant of MMP-9 possesses a glutamine-to-arginine substitution at Glu279, which is found in the substrate-binding region of the fibronectin-like domain. MMP-9 is synthesized and secreted as an inactive enzyme by a variety of cells, including neutrophils, macrophages, and fibroblasts, and is activated in the extracellular space by proteolytic cleavage of the prodomain by several proteases.^,, MMP9 expression is regulated by the transcription factors NF-κB and AP-1, which can be induced by a variety of biological mediators, including reactive oxygen species (ROS) and inflammatory cytokines. MMP-9 participates in ECM remodeling, a process that is critical for development and wound healing, by degrading a variety of ECM proteins, including collagens and gelatins. Increased MMP-9 activity has been observed in a variety of pathological conditions, including cardiovascular diseases, arthritis, and cancer. The MMP-9 Q279R variant has been found in patients with polycythemia vera, essential thrombocytosis, or idiopathic myelofibrosis. Caymans MMP-9 Q279R Variant (human, recombinant) protein can be used for enzyme activity applications.

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