Human MMP-3 Alexa Fluor® 350-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: MMP-3

Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-3 (stromelysin-1), can degrade a broad range of substrates including collagen alpha  chains, aggrecan, laminin, fibronectin, elastin, casein, alpha -1 antitrypsin, myelin basic protein, IL-1 beta, IGFBP-3, pro MMP-1, pro MMP-7, pro MMP-8, pro MMP-9 and pro MMP-13. MMP-3 does not cleave the triple helical region of interstitial collagens, a characteristic which distinguishes the stromelysins from the collagenases. The MMP-3 substrate repertoire extends beyond extracellular matrix proteins and implicates MMP-3 in roles other than direct tissue remodelling, for instance, enzyme cascades and cytokine regulation. MMP-3 is expressed by fibroblasts, chrondrocytes, osteoblasts, endothelial cells, smooth muscle cells and macrophages. Structurally, MMP-3 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain.

Product Datasheets

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