Anti-DDX21 Pab
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Not Dicer but Argonaute Is Required for a Microrna Production
Cell Research (2010) 20:735-737. npg © 2010 IBCB, SIBS, CAS All rights reserved 1001-0602/10 $ 32.00 RESEARCH HIGHLIGHT www.nature.com/cr A new twist in the microRNA pathway: Not Dicer but Argonaute is required for a microRNA production Gabriel D Bossé1, Martin J Simard1 1Laval University Cancer Research Centre, Hôtel-Dieu de Québec (CHUQ), Quebec City, Québec G1R 2J6, Canada Cell Research (2010) 20:735-737. doi:10.1038/cr.2010.83; published online 15 June 2010 Found in all metazoans, microRNAs A Canonical pathway B Ago2-dependent pathway or miRNAs are small non-coding RNA Nucleus Cytoplasm Nucleus Cytoplasm of ~22 nucleotides in length that com- Exp.5 Exp.5 pletely reshaped our understanding of gene regulation. This new class of gene pre-miR-451 regulator is mostly transcribed by the pre-miRNA RNA polymerase II producing a long stem-loop structure, called primary- or Ago2 pri-miRNA, that will first be processed Ago2 Dicer in the cell nucleus by a multiprotein TRBP complex called microprocessor to gen- erate a shorter RNA structure called Ago2 RISC precursor- or pre-miRNA. The precisely Ago2 RISC processed pre-miRNA will next be ex- ported into the cytoplasm by Exportin 5 and loaded onto another processing machine containing the ribonuclease III enzyme Dicer, an Argonaute protein Ago2 Ago2 and other accessory cellular factors mRNA mRNA (Figure 1A; [1]). Dicer will mediate the Translation inhibition Translation inhibition cleavage of the pre-miRNA to form the mature miRNA that will then be bound Figure 1 (A) Canonical microRNA biogenesis. In mammals, the pre-miRNA is by the Argonaute protein to form, most loaded onto a multiprotein complex consisting minimally of Dicer, Tar RNA Bind- likely with other cellular factors, the ef- ing Protein (TRBP) and Ago2. -
EIF2C2 Monoclonal Antibody (M01), Clone 2E12-1C9
EIF2C2 monoclonal antibody (M01), clone 2E12-1C9 Catalog # : H00027161-M01 規格 : [ 100 ug ] List All Specification Application Image Product Mouse monoclonal antibody raised against a full length recombinant Western Blot (Cell lysate) Description: EIF2C2. Immunogen: EIF2C2 (AAH07633.1, 483 a.a. ~ 859 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. Sequence: MPIQGQPCFCKYAQGADSVEPMFRHLKNTYAGLQLVVVILPGKTPVYAE VKRVGDTVLGMATQCVQMKNVQRTTPQTLSNLCLKINVKLGGVNNILLP enlarge QGRPPVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPNRYCATV Western Blot (Transfected RVQQHRQEIIQDLAAMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFQQV lysate) LHHELLAIREACIKLEKDYQPGITFIVVQKRHHTRLFCTDKNERVGKSGNIP AGTTVDTKITHPTEFDFYLCSHAGIQGTSRPSHYHVLWDDNRFSSDELQI LTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHTS GQSNGRDHQALAKAVQVHQDTLRTMYFA Host: Mouse enlarge Reactivity: Human Western Blot (Recombinant Isotype: IgG1 Kappa protein) Quality Control Antibody Reactive Against Recombinant Protein. Immunofluorescence Testing: enlarge Immunohistochemistry (Formalin/PFA-fixed paraffin- embedded sections) Western Blot detection against Immunogen (68.03 KDa) . Storage Buffer: In 1x PBS, pH 7.4 enlarge Storage Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. Instruction: Sandwich ELISA (Recombinant protein) MSDS: Download Interspecies Mouse (100); Rat (99) Antigen Sequence: enlarge Datasheet: Download ELISA Publication Reference RNAi Knockdown (Antibody validated) 1. TDP-43 aggregation induced by oxidative stress causes global mitochondrial imbalance -
Mir-125 in Normal and Malignant Hematopoiesis
Leukemia (2012) 26, 2011–2018 & 2012 Macmillan Publishers Limited All rights reserved 0887-6924/12 www.nature.com/leu SPOTLIGHT REVIEW MiR-125 in normal and malignant hematopoiesis L Shaham1,2, V Binder3,4,NGefen1,5, A Borkhardt3 and S Izraeli1,5 MiR-125 is a highly conserved microRNA throughout many different species from nematode to humans. In humans, there are three homologs (hsa-miR-125b-1, hsa-miR-125b-2 and hsa-miR-125a). Here we review a recent research on the role of miR-125 in normal and malignant hematopoietic cells. Its high expression in hematopoietic stem cells (HSCs) enhances self-renewal and survival. Its expression in specific subtypes of myeloid and lymphoid leukemias provides resistance to apoptosis and blocks further differentiation. A direct oncogenic role in the hematopoietic system has recently been demonstrated by several mouse models. Targets of miR-125b include key proteins regulating apoptosis, innate immunity, inflammation and hematopoietic differentiation. Leukemia (2012) 26, 2011–2018; doi:10.1038/leu.2012.90 Keywords: microRNA; hematopoiesis; hematological malignancies; acute myeloid leukemia; acute lymphoblastic leukemia MicroRNAs (miRNAs) are 21–23-nucleotide non-coding RNAs that nucleotides with the seed region of miR-125b (ebv-miR-BART21-5p, have crucial roles in fundamental biological processes by ebv-miR-BART8 and rlcv-miR-rL1-25). In humans, as in most of the regulating the levels of multiple proteins. They are transcribed genomes, there are two paralogs (hsa-miR-125b-1 on chromosome as primary miRNAs and processed in the nucleus by the RNase III 11 and hsa-miR-125b-2 on chromosome 21), coding for the same endonuclease DROSHA to liberate 70-nucleotide stem loops, the mature sequence. -
EIF2C2 Monoclonal Antibody (M01), Clone 2E12-1C9
Produktinformation Diagnostik & molekulare Diagnostik Laborgeräte & Service Zellkultur & Verbrauchsmaterial Forschungsprodukte & Biochemikalien Weitere Information auf den folgenden Seiten! See the following pages for more information! Lieferung & Zahlungsart Lieferung: frei Haus Bestellung auf Rechnung SZABO-SCANDIC Lieferung: € 10,- HandelsgmbH & Co KG Erstbestellung Vorauskassa Quellenstraße 110, A-1100 Wien T. +43(0)1 489 3961-0 Zuschläge F. +43(0)1 489 3961-7 [email protected] • Mindermengenzuschlag www.szabo-scandic.com • Trockeneiszuschlag • Gefahrgutzuschlag linkedin.com/company/szaboscandic • Expressversand facebook.com/szaboscandic EIF2C2 monoclonal antibody (M01), clone 2E12-1C9 Catalog # : H00027161-M01 規格 : [ 100 ug ] List All Specification Application Image Product Mouse monoclonal antibody raised against a full length recombinant Western Blot (Cell lysate) Description: EIF2C2. Immunogen: EIF2C2 (AAH07633.1, 1 a.a. ~ 377 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. Sequence: MPIQGQPCFCKYAQGADSVEPMFRHLKNTYAGLQLVVVILPGKTPVYAE VKRVGDTVLGMATQCVQMKNVQRTTPQTLSNLCLKINVKLGGVNNILLP enlarge QGRPPVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPNRYCATV Western Blot (Transfected RVQQHRQEIIQDLAAMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFQQV lysate) LHHELLAIREACIKLEKDYQPGITFIVVQKRHHTRLFCTDKNERVGKSGNIP AGTTVDTKITHPTEFDFYLCSHAGIQGTSRPSHYHVLWDDNRFSSDELQI LTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHTS GQSNGRDHQALAKAVQVHQDTLRTMYFA Host: Mouse enlarge Reactivity: Human Western Blot (Recombinant Isotype: IgG1 Kappa -
Characterization of a 7.6-Mb Germline Deletion Encompassing the NF1 Locus and About a Hundred Genes in an NF1 Contiguous Gene Syndrome Patient
European Journal of Human Genetics (2008) 16, 1459–1466 & 2008 Macmillan Publishers Limited All rights reserved 1018-4813/08 $32.00 www.nature.com/ejhg ARTICLE Characterization of a 7.6-Mb germline deletion encompassing the NF1 locus and about a hundred genes in an NF1 contiguous gene syndrome patient Eric Pasmant*,1,2, Aure´lie de Saint-Trivier2, Ingrid Laurendeau1, Anne Dieux-Coeslier3, Be´atrice Parfait1,2, Michel Vidaud1,2, Dominique Vidaud1,2 and Ivan Bie`che1,2 1UMR745 INSERM, Universite´ Paris Descartes, Faculte´ des Sciences Pharmaceutiques et Biologiques, Paris, France; 2Service de Biochimie et de Ge´ne´tique Mole´culaire, Hoˆpital Beaujon AP-HP, Clichy, France; 3Service de Ge´ne´tique Clinique, Hoˆpital Jeanne de Flandre, Lille, France We describe a large germline deletion removing the NF1 locus, identified by heterozygosity mapping based on microsatellite markers, in an 8-year-old French girl with a particularly severe NF1 contiguous gene syndrome. We used gene-dose mapping with sequence-tagged site real-time PCR to locate the deletion end points, which were precisely characterized by means of long-range PCR and nucleotide sequencing. The deletion is located on chromosome arm 17q and is exactly 7 586 986 bp long. It encompasses the entire NF1 locus and about 100 other genes, including numerous chemokine genes, an attractive in silico-selected cerebrally expressed candidate gene (designated NUFIP2, for nuclear fragile X mental retardation protein interacting protein 2; NM_020772) and four microRNA genes. Interestingly, the centromeric breakpoint is located in intron 4 of the PIPOX gene (pipecolic acid oxidase; NM_016518) and the telomeric breakpoint in intron 5 of the GGNBP2 gene (gametogenetin binding protein 2; NM_024835) coding a transcription factor. -
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Article in press - uncorrected proof BioMol Concepts, Vol. 2 (2011), pp. 343–352 • Copyright ᮊ by Walter de Gruyter • Berlin • Boston. DOI 10.1515/BMC.2011.033 Review Fragile X family members have important and non-overlapping functions Claudia Winograd2 and Stephanie Ceman1,2,* member, FMR1, was isolated by positional cloning of the X 1 Department of Cell and Developmental Biology, chromosomal region containing the inducible fragile site in University of Illinois, 601 S. Goodwin Avenue, individuals with fragile X syndrome (1). Cloning of the gene Urbana–Champaign, IL 61801, USA revealed the molecular defect to be a trinucleotide (CGG) 2 Neuroscience Program and College of Medicine, repeat expansion in exon 1 (2). Normally, individuals have University of Illinois, 601 S. Goodwin Avenue, less than 45 repeats with an average around 30 repeats; how- Urbana–Champaign, IL 61801, USA ever, expansion to greater than 200 repeats leads to aberrant methylation of the cytosines, leading to recruitment of * Corresponding author histone deacetylases with consequent transcriptional silenc- e-mail: [email protected] ing of the FMR1 locus (3). Thus, individuals with fragile X syndrome do not express transcript from the FMR1 locus. Abstract To identify the Xenopus laevis ortholog of FMR1 for further use in developmental studies, the human FMR1 gene was The fragile X family of genes encodes a small family of used to screen a cDNA library prepared from Xenopus laevis RNA binding proteins including FMRP, FXR1P and FXR2P ovary. In addition to identifying the Xenopus laevis ortholog that were identified in the 1990s. All three members are of FMR1, the first autosomal paralog FXR1 was discovered encoded by 17 exons and show alternative splicing at the 39 because of its sequence similarity to FMR1 (4). -
Relative Contribution of Sequence and Structure Features to the Mrna Binding of Argonaute/ EIF2C–Mirna Complexes and the Degradation of Mirna Targets
Downloaded from genome.cshlp.org on October 2, 2021 - Published by Cold Spring Harbor Laboratory Press Letter Relative contribution of sequence and structure features to the mRNA binding of Argonaute/ EIF2C–miRNA complexes and the degradation of miRNA targets Jean Hausser,1,3 Markus Landthaler,2,3,4 Lukasz Jaskiewicz,1 Dimos Gaidatzis,1,5 and Mihaela Zavolan1,6 1Biozentrum, University of Basel and Swiss Institute of Bioinformatics, CH-4056 Basel, Switzerland; 2Howard Hughes Medical Institute, Laboratory for RNA Biology, The Rockefeller University, New York, New York 10021, USA How miRNAs recognize their target sites is a puzzle that many experimental and computational studies aimed to solve. Several features, such as perfect pairing of the miRNA seed, additional pairing in the 39 region of the miRNA, relative position in the 39 UTR, and the A/Ucontent of the environment of the putative site, have been found to be relevant. Here we have used a large number of previously published data sets to assess the power that various sequence and structure features have in distinguishing between putative sites that do and those that do not appear to be functional. We found that although different data sets give widely different answers when it comes to ranking the relative importance of these features, the sites inferred from most transcriptomics experiments, as well as from comparative genomics, appear similar at this level. This suggests that miRNA target sites have been selected in evolution on their ability to trigger mRNA degradation. To understand at what step in the miRNA-induced response individual features play a role, we transfected human HEK293 cells with miRNAs and analyzed the association of Argonaute/EIF2C–miRNA complexes with target mRNAs and the degradation of these messages. -
Dysregulated RNA-Induced Silencing Complex (RISC) Assembly Within CNS Corresponds with Abnormal Mirna Expression During Autoimmune Demyelination
The Journal of Neuroscience, May 13, 2015 • 35(19):7521–7537 • 7521 Neurobiology of Disease Dysregulated RNA-Induced Silencing Complex (RISC) Assembly within CNS Corresponds with Abnormal miRNA Expression during Autoimmune Demyelination Przemysław Lewkowicz, Hanna Cwiklin´ska, Marcin P. Mycko, Maria Cichalewska, Małgorzata Domowicz, Natalia Lewkowicz, Anna Jurewicz, and Krzysztof W. Selmaj Department of Neurology, Laboratory of Neuroimmunology, Medical University of Lodz, 92-213 Lodz, Poland MicroRNAs (miRNAs) associate with Argonaute (Ago), GW182, and FXR1 proteins to form RNA-induced silencing complexes (RISCs). RISCs represent a critical checkpoint in the regulation and bioavailability of miRNAs. Recent studies have revealed dysregulation of miRNAs in multiple sclerosis (MS) and its animal model, experimental autoimmune encephalomyelitis (EAE); however, the function of RISCs in EAE and MS is largely unknown. Here, we examined the expression of Ago, GW182, and FXR1 in CNS tissue, oligodendrocytes (OLs), brain-infiltrating T lymphocytes, and CD3 ϩsplenocytes (SCs) of EAE mic, and found that global RISC protein levels were signifi- cantly dysregulated. Specifically, Ago2 and FXR1 levels were decreased in OLs and brain-infiltrating T cells in EAE mice. Accordingly, assembly of Ago2/GW182/FXR1 complexes in EAE brain tissues was disrupted, as confirmed by immunoprecipitation experiments. In parallel with alterations in RISC complex content in OLs, we found downregulation of miRNAs essential for differentiation and survival of OLs and myelin synthesis. In brain-infiltrating T lymphocytes, aberrant RISC formation contributed to miRNA-dependent proinflam- matory helper T-cell polarization. In CD3 ϩ SCs, we found increased expression of both Ago2 and FXR1 in EAE compared with nonim- munized mice. -
NIH Public Access Author Manuscript Epigenetics
NIH Public Access Author Manuscript Epigenetics. Author manuscript; available in PMC 2009 June 23. NIH-PA Author ManuscriptPublished NIH-PA Author Manuscript in final edited NIH-PA Author Manuscript form as: Epigenetics. 2007 ; 2(2): 126±134. Epigenetics and Neural Developmental Disorders: Washington DC, September 18 and 19, 2006 Xinyu Zhao1,*, ChangHui Pak2, Richard D. Smrt1, and Peng Jin2,* 1 Department of Neuroscience; University of New Mexico School of Medicine; Albuquerque, New Mexico USA 2 Department of Human Genetics; Emory University School of Medicine; Atlanta, Georgia USA Abstract Neural developmental disorders, such as autism, Rett Syndrome, Fragile X syndrome, and Angelman syndrome manifest during early postnatal neural development. Although the genes responsible for some of these disorders have been identified, how the mutations of these genes affect neural development is currently unclear. Emerging evidence suggest that these disorders share common underlying defects in neuronal morphology, synaptic connectivity and brain plasticity. In particular, alterations in dendritic branching and spine morphology play a central role in the pathophysiology of most mental retardation disorders, suggesting that common pathways regulating neuronal function may be affected. Epigenetic modulations, mediated by DNA methylation, RNA-associated silencing, and histone modification, can serve as an intermediate process that imprints dynamic environmental experiences on the “fixed” genome, resulting in stable alterations in phenotypes. Disturbance in epigenetic regulations can lead to inappropriate expression or silencing of genes, causing an array of multi-system disorders and neoplasias. Rett syndrome, the most common form of mental retardation in young girls, is due to l mutation of MECP2, encoding a methylated DNA binding protein that translates DNA methylation into gene repression. -
A Fragile X Mental Retardation-Like Gene in a Cnidarian
Gene 343 (2004) 231–238 www.elsevier.com/locate/gene A fragile X mental retardation-like gene in a cnidarian Jasenka Guduric-Fuchsa, Frank Mfhrlena, Marcus Frohmeb, Uri Franka,* aInstitute of Zoology, University of Heidelberg, INF 230, Heidelberg 69120, Germany bDepartment of Functional Genome Analysis, German Cancer Research Center, INF 580, 69120 Heidelberg, Germany Received 6 August 2004; received in revised form 9 September 2004; accepted 5 October 2004 Available online 10 November 2004 Received by D.A. Tagle Abstract The fragile X mental retardation syndrome in humans is caused by a mutational loss of function of the fragile X mental retardation gene 1 (FMR1). FMR1 is an RNA-binding protein, involved in the development and function of the nervous system. Despite of its medical significance, the evolutionary origin of FMR1 has been unclear. Here, we report the molecular characterization of HyFMR1, an FMR1 orthologue, from the cnidarian hydroid Hydractinia echinata. Cnidarians are the most basal metazoans possessing neurons. HyFMR1is expressed throughout the life cycle of Hydractinia. Its expression pattern correlates to the position of neurons and their precursor stem cells in the animal. Our data indicate that the origin of the fraxile X related (FXR) protein family dates back at least to the common ancestor of cnidarians and bilaterians. The lack of FXR proteins in other invertebrates may have been due to gene loss in particular lineages. D 2004 Elsevier B.V. All rights reserved. Keywords: FMR1; FMRP; FXR; Hydractinia; Evolution; Hydrozoa 1. Introduction three types of RNA binding motifs: a ribonucleoprotein K homology domain (KH domain; FMR1 has two such The fragile X syndrome is the most common form of domains), an arginine and glycine rich domain (RGG box) inherited mental retardation in humans. -
T Lymphocytes Mrna, and Protein Expression in Activated Networks
MicroRNA Regulation of Molecular Networks Mapped by Global MicroRNA, mRNA, and Protein Expression in Activated T Lymphocytes This information is current as of September 23, 2021. Yevgeniy A. Grigoryev, Sunil M. Kurian, Traver Hart, Aleksey A. Nakorchevsky, Caifu Chen, Daniel Campbell, Steven R. Head, John R. Yates III and Daniel R. Salomon J Immunol 2011; 187:2233-2243; Prepublished online 25 July 2011; Downloaded from doi: 10.4049/jimmunol.1101233 http://www.jimmunol.org/content/187/5/2233 http://www.jimmunol.org/ Supplementary http://www.jimmunol.org/content/suppl/2011/07/25/jimmunol.110123 Material 3.DC1 References This article cites 83 articles, 31 of which you can access for free at: http://www.jimmunol.org/content/187/5/2233.full#ref-list-1 Why The JI? Submit online. by guest on September 23, 2021 • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2011 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology MicroRNA Regulation of Molecular Networks Mapped by Global MicroRNA, mRNA, and Protein Expression in Activated T Lymphocytes Yevgeniy A. -
A Drosophila Fragile X Protein Interacts with Components of Rnai and Ribosomal Proteins
Downloaded from genesdev.cshlp.org on September 25, 2021 - Published by Cold Spring Harbor Laboratory Press A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins Akira Ishizuka,1,2,3 Mikiko C. Siomi,1,3 and Haruhiko Siomi1,4 1Institute for Genome Research, 2Graduate School of Nutrition University of Tokushima, Tokushima 770-8503, Japan Fragile X syndrome is a common form of inherited mental retardation caused by the loss of FMR1 expression. The FMR1 gene encodes an RNA-binding protein that associates with translating ribosomes and acts as a negative translational regulator. In Drosophila, the fly homolog of the FMR1 protein (dFMR1) binds to and represses the translation of an mRNA encoding of the microtuble-associated protein Futsch. We have isolated a dFMR1-associated complex that includes two ribosomal proteins, L5 and L11, along with 5S RNA. The dFMR1 complex also contains Argonaute2 (AGO2) and a Drosophila homolog of p68 RNA helicase (Dmp68). AGO2 is an essential component for the RNA-induced silencing complex (RISC), a sequence-specific nuclease complex that mediates RNA interference (RNAi) in Drosophila. We show that Dmp68 is also required for efficient RNAi. We further show that dFMR1 is associated with Dicer, another essential component of the RNAi pathway, and microRNAs (miRNAs) in vivo, suggesting that dFMR1 is part of the RNAi-related apparatus. Our findings suggest a model in which the RNAi and dFMR1-mediated translational control pathways intersect in Drosophila. Our findings also raise the possibility that defects in an RNAi-related machinery may cause human disease. [Keywords: fragile X syndrome; FMR1; RNAi; RNA helicase; miRNA] Received July 9, 2002; revised version accepted August 22, 2002.