Cynomolgus Monkey MMP-9 (XP_005569271.2) VersaClone cDNA

Cynomolgus Monkey MMP-9 (XP_005569271.2) VersaClone cDNA Summary

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Background: MMP-9

The matrix metalloproteinases (MMPs) consist of 24 known human zinc proteases with essential roles in breaking down components of the extracellular matrix (ECM). Additional MMP substrates include cytokines, chemokines, growth factors and binding proteins, cell/cell adhesion molecules, and other proteinases. With a few exceptions, MMPs share common structural motifs including a pro-peptide domain, a catalytic domain, a hinge region, and a hemopexin-like domain. Synthesized as pro-enzymes, most MMPs are secreted before conversion to their active form. MMP activities are modulated on several levels including transcription, pro-enzyme activation, or by their endogenous inhibitors, tissue inhibitors of metalloproteinases (TIMPs). A subset of MMPs are associated with membranes and designated as membrane-type metalloproteinases (MT-MMP).

Related Research Areas

• Airway Inflammation and Remodeling
• Alpha Granule Soluble Molecules
• Cancer Biomarkers
• Cell to Cell Adhesion Disassembly During EMT
• Collagen Modifying Enzymes
• Enzymes Secreted by Endothelial Cells
• Extracellular Matrix Remodeling and Cell Migration During EMT
• Gametes and Fertilization
• Inflammatory Mediators
• Mesenchymal Cells and EMT
• Metalloproteases and Regulators
• Microglia Activation Markers
• Microglia Development
• MMPs, TIMPs and Related Molecules
• Molecules Secreted by VSMC
• Neuroinflammatory Factors
• Preeclampsia
• Proteolytic Degradation of Amyloid beta
• Search Bioprocessing Enzymes