MMP19 Antibody

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Product Datasheet MMP19 Antibody Catalog No: #35461 Orders: [email protected] Description Support: [email protected] Product Name MMP19 Antibody Host Species Rabbit Clonality Polyclonal Purification Antibodies were purified by antigen-affinity chromatography. Applications WB Species Reactivity Hu Specificity The antibody detects endogenous levels of total MMP19 protein. Immunogen Type Recombinant Protein Immunogen Description Recombinant fragment corresponding to a region within amino acids 210 and 508 of MMP19. Target Name MMP19 Other Names MMP18 antibody; RASI-1 antibody; MMP19 antibody; MMP-19 antibody; matrix metalloproteinase 18 antibody; matrix metalloproteinase RASI antibody; matrix metalloproteinase-19 antibody; MMP-18 antibody; matrix metalloproteinase 19 antibody; matrix metalloprot Accession No. Swiss-Prot#:Q99542;NCBI Gene#:4327 SDS-PAGE MW 57kd Concentration 1mg/ml Formulation Rabbit IgG in 1XPBS, 1%BSA, 20% Glycerol (pH7). 0.01% Thimerosal was added as a preservative. Storage Store at -20°C Application Details Western blotting: 1:500-1:3000 Images Sample (30 ug of whole cell lysate) A: U87-MG 7.5% SDS PAGE #35461 diluted at 1:1000 Background Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 1 secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This protein is expressed in human epidermis and it has a role in cellular proliferation as well as migration and adhesion to type I collagen. Multiple transcript variants encoding distict isoforms have been identified for this gene. [provided by RefSeq] Note: This product is for in vitro research use only and is not intended for use in humans or animals. Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 2.

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Effect of Nanoparticles on the Expression and Activity of Matrix Metalloproteinases
Nanotechnol Rev 2018; 7(6): 541–553 Review Magdalena Matysiak-Kucharek*, Magdalena Czajka, Krzysztof Sawicki, Marcin Kruszewski and Lucyna Kapka-Skrzypczak Effect of nanoparticles on the expression and activity of matrix metalloproteinases https://doi.org/10.1515/ntrev-2018-0110 Received September 14, 2018; accepted October 11, 2018; previously 1 Introduction published online November 15, 2018 Matrix metallopeptidases, commonly known as matrix Abstract: Matrix metallopeptidases, commonly known metalloproteinases (MMPs), are zinc-dependent proteo- as matrix metalloproteinases (MMPs), are a group of pro- lytic enzymes whose primary function is the degradation teolytic enzymes whose main function is the remodeling and remodeling of extracellular matrix (ECM) compo- of the extracellular matrix. Changes in the activity of nents. ECM is a complex, dynamic structure that condi- these enzymes are observed in many pathological states, tions the proper tissue architecture. MMPs by digesting including cancer metastases. An increasing body of evi- ECM proteins eliminate structural barriers and allow dence indicates that nanoparticles (NPs) can lead to the cell migration. Moreover, by hydrolyzing extracellularly deregulation of MMP expression and/or activity both in released proteins, MMPs can change the activity of many vitro and in vivo. In this work, we summarized the current signal peptides, such as growth factors, cytokines, and state of knowledge on the impact of NPs on MMPs. The chemokines. MMPs are involved in many physiological literature analysis showed that the impact of NPs on MMP processes, such as embryogenesis, reproduction cycle, or expression and/or activity is inconclusive. NPs exhibit wound healing; however, their increased activity is also both stimulating and inhibitory effects, which might be associated with a number of pathological conditions, such dependent on multiple factors, such as NP size and coat- as diabetes, cardiovascular diseases and neurodegenera- ing or a cellular model used in the research.
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Supplementary Material DNA Methylation in Inflammatory Pathways Modifies the Association Between BMI and Adult-Onset Non- Atopic
Supplementary Material DNA Methylation in Inflammatory Pathways Modifies the Association between BMI and Adult-Onset Non- Atopic Asthma Ayoung Jeong 1,2, Medea Imboden 1,2, Akram Ghantous 3, Alexei Novoloaca 3, Anne-Elie Carsin 4,5,6, Manolis Kogevinas 4,5,6, Christian Schindler 1,2, Gianfranco Lovison 7, Zdenko Herceg 3, Cyrille Cuenin 3, Roel Vermeulen 8, Deborah Jarvis 9, André F. S. Amaral 9, Florian Kronenberg 10, Paolo Vineis 11,12 and Nicole Probst-Hensch 1,2,* 1 Swiss Tropical and Public Health Institute, 4051 Basel, Switzerland; [email protected] (A.J.); [email protected] (M.I.); [email protected] (C.S.) 2 Department of Public Health, University of Basel, 4001 Basel, Switzerland 3 International Agency for Research on Cancer, 69372 Lyon, France; [email protected] (A.G.); [email protected] (A.N.); [email protected] (Z.H.); [email protected] (C.C.) 4 ISGlobal, Barcelona Institute for Global Health, 08003 Barcelona, Spain; [email protected] (A.-E.C.); [email protected] (M.K.) 5 Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain 6 CIBER Epidemiología y Salud Pública (CIBERESP), 08005 Barcelona, Spain 7 Department of Economics, Business and Statistics, University of Palermo, 90128 Palermo, Italy; [email protected] 8 Environmental Epidemiology Division, Utrecht University, Institute for Risk Assessment Sciences, 3584CM Utrecht, Netherlands; [email protected] 9 Population Health and Occupational Disease, National Heart and Lung Institute, Imperial College, SW3 6LR London, UK; [email protected] (D.J.); [email protected] (A.F.S.A.) 10 Division of Genetic Epidemiology, Medical University of Innsbruck, 6020 Innsbruck, Austria; [email protected] 11 MRC-PHE Centre for Environment and Health, School of Public Health, Imperial College London, W2 1PG London, UK; [email protected] 12 Italian Institute for Genomic Medicine (IIGM), 10126 Turin, Italy * Correspondence: [email protected]; Tel.: +41-61-284-8378 Int.
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MMP19, Matrix Metalloproteinase 19 Polyclonal Antibody
MMP19, Matrix metalloproteinase 19 polyclonal antibody roteins of the matrix metalloproteinase (MMP) fam- or Research Use Only. Not for Pily are involved in the breakdown of extracellular ma- FDiagnostic or Therapeutic Use. trix in normal physiological processes, such as embryonic Purchase does not include or carry development,reproduction, and tissue remodeling, as well any right to resell or transfer this product either as a stand-alone as in disease processes, such as arthritis and metastasis. product or as a component of another Most MMP’s are secreted as inactive proproteins which are product. Any use of this product other activated when cleaved by extracellular proteinases. The than the permitted use without the function of Matrix metalloproteinase 19 (MMP19, formerly express written authorization of Allele called MMP18) has not been determined yet. The MMP19 Biotech is strictly prohibited gene codes for four different protein isoforms (rasi-1, rasi- 3, rasi-6 and rasi-9). Variant rasi-1 encodes the full length protein whereas rasi-3 uses an alternate start codon and Website: www.allelebiotech.com alternate splicing site within the coding sequence resulting Call: 1-800-991-RNAi/858-587-6645 in a much shorter protein which is translated in a different (Pacific Time: 9:00AM~5:00PM) frame. In comparison to rasi-1, rasi-6 is alternatively spliced Email: [email protected] in exon 6 producing a change in frame and a premature stop codon in exon 7. Variant rasi-9 is alternatively spliced in exon 2, producing a different in-frame start codon compared to the full length transcript and encoding a distinct 12 amino Box 1 | Basic Info acid sequence at the N-terminus of the protein, followed by sequence identical to the full length protein.
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A Therapeutic Role for MMP Inhibitors in Lung Diseases?
ERJ Express. Published on June 9, 2011 as doi: 10.1183/09031936.00027411 A therapeutic role for MMP inhibitors in lung diseases? Roosmarijn E. Vandenbroucke1,2, Eline Dejonckheere1,2 and Claude Libert1,2,* 1Department for Molecular Biomedical Research, VIB, Ghent, Belgium 2Department of Biomedical Molecular Biology, Ghent University, Ghent, Belgium *Corresponding author. Mailing address: DBMR, VIB & Ghent University Technologiepark 927 B-9052 Ghent (Zwijnaarde) Belgium Phone: +32-9-3313700 Fax: +32-9-3313609 E-mail: [email protected] 1 Copyright 2011 by the European Respiratory Society. A therapeutic role for MMP inhibitors in lung diseases? Abstract Disruption of the balance between matrix metalloproteinases and their endogenous inhibitors is considered a key event in the development of pulmonary diseases such as chronic obstructive pulmonary disease, asthma, interstitial lung diseases and lung cancer. This imbalance often results in elevated net MMP activity, making MMP inhibition an attractive therapeutic strategy. Although promising results have been obtained, the lack of selective MMP inhibitors together with the limited knowledge about the exact functions of a particular MMP hampers the clinical application. This review discusses the involvement of different MMPs in lung disorders and future opportunities and limitations of therapeutic MMP inhibition. 1. Introduction The family of matrix metalloproteinases (MMPs) is a protein family of zinc dependent endopeptidases. They can be classified into subgroups based on structure (Figure 1), subcellular location and/or function [1, 2]. Although it was originally believed that they are mainly involved in extracellular matrix (ECM) cleavage, MMPs have a much wider substrate repertoire, and their specific processing of bioactive molecules is their most important in vivo role [3, 4].
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Extracellular Matrix Alterations in Metastatic Processes
International Journal of Molecular Sciences Review Extracellular Matrix Alterations in Metastatic Processes Mayra Paolillo * and Sergio Schinelli Department of Drug Sciences, University of Pavia, 27100 Pavia, Italy; [email protected] * Correspondence: [email protected] Received: 17 September 2019; Accepted: 30 September 2019; Published: 7 October 2019 Abstract: The extracellular matrix (ECM) is a complex network of extracellular-secreted macromolecules, such as collagen, enzymes and glycoproteins, whose main functions deal with structural scaffolding and biochemical support of cells and tissues. ECM homeostasis is essential for organ development and functioning under physiological conditions, while its sustained modification or dysregulation can result in pathological conditions. During cancer progression, epithelial tumor cells may undergo epithelial-to-mesenchymal transition (EMT), a morphological and functional remodeling, that deeply alters tumor cell features, leading to loss of epithelial markers (i.e., E-cadherin), changes in cell polarity and intercellular junctions and increase of mesenchymal markers (i.e., N-cadherin, fibronectin and vimentin). This process enhances cancer cell detachment from the original tumor mass and invasiveness, which are necessary for metastasis onset, thus allowing cancer cells to enter the bloodstream or lymphatic flow and colonize distant sites. The mechanisms that lead to development of metastases in specific sites are still largely obscure but modifications occurring in target tissue ECM are being intensively studied. Matrix metalloproteases and several adhesion receptors, among which integrins play a key role, are involved in metastasis-linked ECM modifications. In addition, cells involved in the metastatic niche formation, like cancer associated fibroblasts (CAF) and tumor associated macrophages (TAM), have been found to play crucial roles in ECM alterations aimed at promoting cancer cells adhesion and growth.
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Original Article the Expression of MMP19 and Its Clinical Significance in Glioma
Int J Clin Exp Pathol 2018;11(11):5407-5412 www.ijcep.com /ISSN:1936-2625/IJCEP0085570 Original Article The expression of MMP19 and its clinical significance in glioma Qisheng Luo1,2*, Hongcheng Luo3*, Xiaoping Chen5,6*, Peng Yan2*, Huangde Fu2, Haineng Huang2, Huadong Huang2, Chuanyu Li2, Chengjian Qin2, Chuanhua Zheng2, Lan Chuanliu2, Qianli Tang1,4 1College of Integrated Chinese and Western Medicine, Hunan University of Chinese Medicine, Changsha, Hunan, China; Departments of 2Neurosurgery, 3Laboratory Medicine, 4Surgery, Affiliated Hospital of Youjiang Medical Uni- versity for Nationalities, Baise, Guangxi, China; 5Department of Neurology, Guangxi Zhuang Autonomous Region People’s Hospital, Nanning, Guangxi, China; 6Guangxi Medical University Graduate School, Nanning, Guangxi, China. *Equal contributors. Received September 16, 2018; Accepted September 25, 2018; Epub November 1, 2018; Published November 15, 2018 Abstract: Aims: The expression of phosphoglycerate kinase 1 (MMP19) is elevated in some cancers. However, the clinical features and prognostic value of glioma patients with MMP19 expression are unclear. In this study, the ex- pression level of MMP19 and the correlation between the level of MMP19 expression and the clinicopathologic data in glioma patients including survival were examined. Methods and results: Using real-time PCR, the mRNA expres- sion of MMP19 was examined in 61 fresh glioma tissues and 32 brain samples. The result indicated that MMP19 mRNA was obviously elevated in glioma tissues compared to brain tissues. Further, we observed that MMP19 mRNA was much higher in stage III patients than it was in stage I-II patients. The expression of the MMP19 protein was determined by immunohistochemical analysis in 156 paraffin-embedded glioma samples and 35 normal paraffin- embedded brain samples.
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Molecular Signatures Differentiate Immune States in Type 1 Diabetes Families
Page 1 of 65 Diabetes Molecular signatures differentiate immune states in Type 1 diabetes families Yi-Guang Chen1, Susanne M. Cabrera1, Shuang Jia1, Mary L. Kaldunski1, Joanna Kramer1, Sami Cheong2, Rhonda Geoffrey1, Mark F. Roethle1, Jeffrey E. Woodliff3, Carla J. Greenbaum4, Xujing Wang5, and Martin J. Hessner1 1The Max McGee National Research Center for Juvenile Diabetes, Children's Research Institute of Children's Hospital of Wisconsin, and Department of Pediatrics at the Medical College of Wisconsin Milwaukee, WI 53226, USA. 2The Department of Mathematical Sciences, University of Wisconsin-Milwaukee, Milwaukee, WI 53211, USA. 3Flow Cytometry & Cell Separation Facility, Bindley Bioscience Center, Purdue University, West Lafayette, IN 47907, USA. 4Diabetes Research Program, Benaroya Research Institute, Seattle, WA, 98101, USA. 5Systems Biology Center, the National Heart, Lung, and Blood Institute, the National Institutes of Health, Bethesda, MD 20824, USA. Corresponding author: Martin J. Hessner, Ph.D., The Department of Pediatrics, The Medical College of Wisconsin, Milwaukee, WI 53226, USA Tel: 011-1-414-955-4496; Fax: 011-1-414-955-6663; E-mail: [email protected]. Running title: Innate Inflammation in T1D Families Word count: 3999 Number of Tables: 1 Number of Figures: 7 1 For Peer Review Only Diabetes Publish Ahead of Print, published online April 23, 2014 Diabetes Page 2 of 65 ABSTRACT Mechanisms associated with Type 1 diabetes (T1D) development remain incompletely defined. Employing a sensitive array-based bioassay where patient plasma is used to induce transcriptional responses in healthy leukocytes, we previously reported disease-specific, partially IL-1 dependent, signatures associated with pre and recent onset (RO) T1D relative to unrelated healthy controls (uHC).
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MMP19 Polyclonal Antibody
MMP19 polyclonal antibody processes, such as embryonic development, reproduction, and tissue remodeling, as well as in Catalog Number: PAB4786 disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which Regulatory Status: For research use only (RUO) are activated when cleaved by extracellular proteinases. This protein is expressed in human epidermis and it has Product Description: Rabbit polyclonal antibody raised a role in cellular proliferation as well as migration and against synthetic peptide of MMP19. adhesion to type I collagen. Multiple transcript variants encoding distict isoforms have been identified for this Immunogen: A synthetic peptide (conjugated with KLH) gene. [provided by RefSeq] corresponding to C-terminus of human MMP19. References: Host: Rabbit 1. Matrix metalloproteinase 19 regulates insulin-like growth factor-mediated proliferation, migration, and Reactivity: Human adhesion in human keratinocytes through proteolysis of Applications: ELISA, Flow Cyt, IHC-P, WB-Ce insulin-like growth factor binding protein-3. Sadowski T, (See our web site product page for detailed applications Dietrich S, Koschinsky F, Sedlacek R. Mol Biol Cell. information) 2003 Nov;14(11):4569-80. Epub 2003 Aug 22. 2. Matrix metalloproteinase-19 is expressed by Protocols: See our web site at proliferating epithelium but disappears with neoplastic http://www.abnova.com/support/protocols.asp or product dedifferentiation. Impola U, Toriseva M, Suomela S, page for detailed protocols Jeskanen L, Hieta N, Jahkola T, Grenman R, Kahari VM, Saarialho-Kere U. Int J Cancer. 2003 Mar Form: Liquid 1;103(6):709-16. 3. Matrix metalloproteinase-19 is expressed in myeloid Purification: Protein G purification cells in an adhesion-dependent manner and associates with the cell surface.
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Revealing the Acute Asthma Ignorome: Characterization and Validation of Uninvestigated Gene Networks
www.nature.com/scientificreports OPEN Revealing the acute asthma ignorome: characterization and validation of uninvestigated gene Received: 07 December 2015 Accepted: 01 April 2016 networks Published: 21 April 2016 Michela Riba1,*, Jose Manuel Garcia Manteiga1,*, Berislav Bošnjak2,*, Davide Cittaro1, Pavol Mikolka2,†, Connie Le2,‡, Michelle M. Epstein2,# & Elia Stupka1,# Systems biology provides opportunities to fully understand the genes and pathways in disease pathogenesis. We used literature knowledge and unbiased multiple data meta-analysis paradigms to analyze microarray datasets across different mouse strains and acute allergic asthma models. Our combined gene-driven and pathway-driven strategies generated a stringent signature list totaling 933 genes with 41% (440) asthma-annotated genes and 59% (493) ignorome genes, not previously associated with asthma. Within the list, we identified inflammation, circadian rhythm, lung-specific insult response, stem cell proliferation domains, hubs, peripheral genes, and super-connectors that link the biological domains (Il6, Il1ß, Cd4, Cd44, Stat1, Traf6, Rela, Cadm1, Nr3c1, Prkcd, Vwf, Erbb2). In conclusion, this novel bioinformatics approach will be a powerful strategy for clinical and across species data analysis that allows for the validation of experimental models and might lead to the discovery of novel mechanistic insights in asthma. Allergen exposure causes a complex interaction of cellular and molecular networks leading to allergic asthma in susceptible individuals. Experimental mouse models of allergic asthma are widely used to understand disease pathogenesis and elucidate mechanisms underlying the initiation of allergic asthma1. For example, gene profiling of lung tissue from experimental mice during the initiation of allergic asthma in experiments with different proto- cols2–7 validated well-known genes and identified new genes with roles in disease pathogenesis such as C53, Arg18, Adam89, and Pon17, and dissected pathways activated by Il1310 and Stat611.
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MMP19 Is Upregulated During Melanoma Progression and Increases Invasion of Melanoma Cells
Modern Pathology (2010) 23, 511–521 & 2010 USCAP, Inc. All rights reserved 0893-3952/10 $32.00 511 MMP19 is upregulated during melanoma progression and increases invasion of melanoma cells Matthias Mu¨ ller1,8, Inken M Beck2,3,8, Judith Gadesmann4, Nadine Karschuk1, Annette Paschen5, Ehrhard Proksch6, Valentin Djonov7, Karina Reiss1,6 and Radislav Sedlacek2,3 1Department of Biochemistry, University of Kiel, Kiel, Germany; 2Institute of Biotechnology, Prague, Czech Republic; 3Institute of Molecular Genetics, Prague, Czech Republic; 4Department of Dermatology, Hospital of the German Armed Forces, Ulm, Germany; 5Clinical Cooperation Unit Dermato-Oncology, German Cancer Research Center Heidelberg, University Medical Center Mannheim, Mannheim, Germany; 6Department of Dermatology, University of Kiel, Kiel, Germany; and 7Department of Medicine, Gross Anatomy and Vascular Biology, University of Fribourg, Fribourg, Switzerland During the progression of cutaneous melanomas, matrix metalloproteinases (MMPs) facilitate the tumour cells to traverse the basement membrane and invade the dermis. In this study, we analysed the expression of MMP19 in the course of melanoma progression. Although MMP19 was absent in melanocytes and melanoma cells of early stages of melanoma development, its expression was strongly upregulated in the neighbouring keratinocytes that may facilitate the vertical outgrowth of melanoma cells. In contrast to early stages, MMP19 was upregulated during the vertical growth phase of melanoma and in metastases. The upregulation of MMP19 in melanoma of Clark levels IV and V correlates with that of MMP2 and also simultaneously with ceased expression of E-cadherin. To reveal whether MMP19 facilitates the invasion of melanomas, we examined adhesion and migratory capacity of selected melanoma cell lines.
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Figure S1. GO Analysis of Genes in Glioblastoma Cases That Showed Positive and Negative Correlations with TCIRG1 in the GSE16011 Cohort
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