抗MMP-9抗体(Anti-MMP-9, Mouse-Mono, FITC antibody)

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

価格

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Product Details

Species Reactivity	Human
Label	Fluorescein
Immunogen	Chinese hamster ovary cell line CHO-derived recombinant human MMP-9
Source	Monoclonal Mouse IgG2B Clone # 56129
Purification	Protein A or G purified from ascites
Specificity	Detects human MMP-9 in Flow Cytometry.

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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‑9 in NS0 Mouse Cell Line Transfected with Human MMP-9 by Flow Cytometry. NS0 mouse myeloma cell line transfected with human MMP-9 was stained with Mouse Anti-Human MMP‑9 Fluorescein‑conjugated Monoclonal Antibody (Catalog # IC9111F, filled histogram) or isotype control antibody (Catalog # IC0041F, 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 9
Background	MMP-9
background_content	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 maybe 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.

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Citations

1. Differential Expression of Matrix Metalloproteinases 2, 9 and Cytokines by Neutrophils and Monocytes in the Clinical Forms of Chagas Disease
   Authors: NI Medeiros, RC Fares, EP Franco, GR Sousa, RT Mattos, AT Chaves, MD Nunes, WO Dutra, R Correa-Oli, MO Rocha, JA Gomes
   PLoS Negl Trop Dis, 2017;11(1):e0005284.
   Species: Human
   Sample Type: Whole Cells
   Application: Flow


2. MMP9 integrates multiple immunoregulatory pathways that discriminate high suppressive activity of human mesenchymal stem cells
   Authors: C Lavini-Ram, HM Silva, A Soares-Sch, SM Monteiro, LR Ferreira, AP Pacanaro, S Gomes, J Batista, K Faé, J Kalil, V Coelho
   Sci Rep, 2017;7(1):874.
   Species: Human
   Sample Type: Whole Cells
   Application: Flow


3. JAK/STAT regulation of Aspergillus fumigatus corneal infections and IL-6/23-stimulated neutrophil, IL-17, elastase, and MMP9 activity
   Authors: PR Taylor, S Roy, EC Meszaros, Y Sun, SJ Howell, CJ Malemud, E Pearlman
   J Leukoc Biol, 2016;0(0):.
   Species: Human
   Sample Type: Whole Cells
   Application: Flow


4. Development and characterization of a physiologically relevant model of lymphocyte migration in chronic lymphocytic leukemia.
   Authors: Walsby E, Buggins A, Devereux S, Jones C, Pratt G, Brennan P, Fegan C, Pepper C
   Blood, 2014;123(23):3607-17.
   Species: Human
   Sample Type: Whole Cells
   Application: Flow


5. Primary human acute myelogenous leukemia cells release matrix metalloproteases and their inhibitors: release profile and pharmacological modulation.
   Authors: Reikvam H, Hatfield KJ, Oyan AM, Kalland KH, Kittang AO, Bruserud O
   Eur. J. Haematol., 2010;84(3):239-51.
   Species: Human
   Sample Type: Whole Cells
   Application: Flow

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