Human MMP-7 PE-conjugated Antibody Summary
Leu18-Lys267 (Ala230del)
Accession # NP_002414.1
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.
Scientific Data
Detection of MMP‑7 in A549 Human Cell Line by Flow Cytometry. A549 human lung carcinoma cell line was stained with Mouse Anti-Human MMP-7 PE-conjugated Monoclonal Antibody (Catalog # IC9071P, filled histogram) or isotype control antibody (Catalog # IC0041P, open histogram). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # FC004) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # FC005). View our protocol for Staining Intracellular Molecules.
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Preparation and Storage
Background: MMP-7
Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-7 (matrilysin) is expressed in epithelial cells of normal and diseased tissues, and is capable of digesting a large series of proteins of the extracellular matrix including collagen IV and X, gelatin, casein, laminin, aggrecan, entactin, elastin and versican. MMP-7 is implicated in the activation of other proteinases such as plasminogen, MMP-1, MMP-2, and MMP-9. In addition to its roles in connective tissue remodeling and cancer, MMP-7 also regulates intestinal alpha ‑defensin activation in innate host defense, releases tumor necrosis factor-alpha in a model of herniated disc resorption, and cleaves FasL to generate a soluble form in a model of prostate involution. Structurally, MMP-7 is the smallest of the MMPs and consists of two domains: a pro-domain that is cleaved upon activation and a catalytic domain containing the zinc-binding site.
Product Datasheets
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