Human MMP-3 (AAA36321.1) VersaClone cDNA

Human MMP-3 (AAA36321.1) VersaClone cDNA Summary

Specifications

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Background: MMP-3

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

• Cancer Biomarkers
• Cell to Cell Adhesion Disassembly During EMT
• Collagen Modifying Enzymes
• EMT Induction
• Enzymes Secreted by Endothelial Cells
• Extracellular Matrix Remodeling and Cell Migration During EMT
• Mesenchymal Cells and EMT
• Metalloproteases and Regulators
• Microglia Activation Markers
• MMPs, TIMPs and Related Molecules
• Neuroinflammatory Factors
• Proteolytic Degradation of Amyloid beta
• Search Bioprocessing Enzymes