MMP19 Polyclonal Antibody

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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. Mauch S, Kolb C, Kolb B, Sadowski Recommend Usage: ELISA (1:1000) T, Sedlacek R. J Immunol. 2002 Feb 1;168(3):1244-51. Western Blot (1:100-500) Immunohistochemistry (1:50-100) Flow cytometry (1:10-50) The optimal working dilution should be determined by the end user. Storage Buffer: In PBS (0.09% sodium azide) Storage Instruction: Store at 4°C. For long term storage store at -20°C. Aliquot to avoid repeated freezing and thawing. Entrez GeneID: 4327 Gene Symbol: MMP19 Gene Alias: MMP18, RASI-1 Gene Summary: Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological Page 1/1 Powered by TCPDF (www.tcpdf.org).

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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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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?
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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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MIAMI UNIVERSITY The Graduate School Certificate for Approving the Dissertation We hereby approve the Dissertation of Fan Meng Candidate for the Degree DOCTOR OF PHILOSOPHY ______________________________________ Director Dr. Michael W. Crowder ______________________________________ Dr. David L. Tierney ______________________________________ Dr. Carole Dabney-Smith ______________________________________ Dr. Christopher A. Makaroff ______________________________________ Graduate School Representative Dr. Hai-Fei Shi ABSTRACT BIOCHEMICAL CHARACTERIZATION AND ZINC BINDING GROUP (ZBGS) INHIBITION STUDIES ON THE CATALYTIC DOMAINS OF MMP7 (CDMMP7) AND MMP16 (CDMMP16) by Fan Meng Matrix metalloproteinase 7 (MMP7/matrilysin-1) and membrane type matrix metalloproteinase 16 (MMP16/MT3-MMP) have been implicated in the progression of pathological events, such as cancer and inflammatory diseases; therefore, these two MMPs are considered as viable drug targets. In this work, we (a) provide a review of the role(s) of MMPs in biology and of the previous efforts to target MMPs as therapeutics (Chapter 1), (b) describe our efforts at over-expression, purification, and characterization of the catalytic domains of MMP7 (cdMMP7) and MMP16 (cdMMP16) (Chapters 2 and 3), (c) present our efforts at the preparation and initial spectroscopic characterization of Co(II)-substituted analogs of cdMMP7 and cdMMP16 (Chapters 2 and 3), (d) present inhibition data on cdMMP7 and cdMMP16 using zinc binding groups (ZBG) as potential scaffolds for future inhibitors (Chapter 3), and (e) summarize our data in the context of previous results and suggest future directions (Chapter 4). The work described in this dissertation integrates biochemical (kinetic assays, inhibition studies, limited computational methods), spectroscopic (CD, UV-Vis, 1H-NMR, fluorescence, and EXAFS), and analytical (MALDI-TOF mass spectrometry, isothermal calorimetry) methods to provide a detailed structural and mechanistic view of these MMPs.
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