Mouse MMP-9 Alexa Fluor® 405-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-9

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-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin, and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages, and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin-binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline-rich linker region, and a carboxyl terminal hemopexin-like domain. Compared to the human MMP-9
(Catalog # 911-MP), the mouse enzyme contains extra sequences in the linker region and in the hemopexin-like domain, respectively.

Product Datasheets

Related Research Areas

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• 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
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• Proteolytic Degradation of Amyloid beta
• Search Bioprocessing Enzymes