MMP-9 Q279R Variant (human, recombinant)

92 kDa Type IV Collagenase|Gelatinase B|MANDP2|Matrix Metalloproteinase-9

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.{61159} 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.{61160} 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.{61161,61159,61162} 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.{61159} 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.{61160} Cayman's MMP-9 Q279R Variant (human, recombinant) protein can be used for enzyme activity applications.

HEK293 cells

-80

-80

40 mM Tris-HCl buffer, pH 8.0, with 110 mM sodium chloride, 2.2 mM potassium chloride, 200 mM imidazole, and 20% glycerol

180

≥90% estimated by SDS-PAGE