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.¹ 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.² 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.^3,1,4 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.¹ 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.² Cayman's MMP-9 Q279R Variant (human, recombinant) protein can be used for enzyme activity applications.

WARNING This product is not for human or veterinary use.

1. Yabluchanskiy, A., Ma, Y., Iyer, R.P., et al. Matrix metalloproteinase-9: Many shades of function in cardiovascular disease. Physiology 28(6), 391-403 (2013).

2. Maral, S., Acar, M., Balcik, O.S., et al. Matrix metalloproteinases 2 and 9 polymorphism in patients with myeloproliferative diseases: A STROBE-compliant observational study. Medicine 94(16), e732 (2015).

3. Löffek, S., Schilling, O., and Franzke, C.-W. Series "matrix metalloproteinases in lung health and disease": Biological role of matrix metalloproteinases: a critical balance. Eur. Respir. J. 38(1), 191-208 (2011).

4. Xie, Y., Mustafa, A., Yerzhan, A., et al. Nuclear matrix metalloproteinases: Functions resemble the evolution from the intracellular to the extracellular compartment. Cell Death Discov. 3, 17036 (2017).