抗Mouse MMP-7 Phycoerythrin抗体(Anti-Mouse MMP-7 Phycoerythrin antibody)

• 価格
• Product Details
• Applications and Data
• Related Product & Information

価格

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Product Details

Species Reactivity	Mouse
Label	Phycoerythrin
Immunogen	Mouse myeloma cell line NS0-derived recombinant mouse MMP-7Met1-Leu264Accession # Q10738
Source	Monoclonal Rat IgG2B Clone # 704202
Purification	Protein A or G purified from hybridoma culture supernatant
Specificity	Detects mouse MMP-7 in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human MMP-7, recombinant mouse (rm) MMP‑3, or rmMMP-8 is observed.

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Applications and Data

	Recommended Concentration	Sample
Intracellular Staining by Flow Cytometry	10 µL/106 cells	See below

Intracellular Staining by Flow Cytometry

Detection of MMP‑7 in bEnd.3 Mouse Cell Line by Flow Cytometry. bEnd.3 mouse endothelioma cell line treated with Recombinant Mouse FGF basic (Catalog # 3139-FB) was stained with Rat Anti-Mouse MMP‑7 PE‑conjugated Monoclonal Antibody (Catalog # IC7170P, filled histogram) or isotype control antibody (Catalog # IC013P, 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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Related Product & Information

Long Name	Matrix Metalloproteinase 7
Background	MMP-7
background_content	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. Over amino acids (aa) 18-264, mouse MMP-7 shares 69% and 88% aa sequence identity with human and rat MMP-7, respectively.

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