SUMO Protease 1 (GST-Tagged) from Yeast, Recombinant Cat

Total Page:16

File Type:pdf, Size:1020Kb

SUMO Protease 1 (GST-Tagged) from Yeast, Recombinant Cat SUMO Protease 1 (GST-tagged) from Yeast, Recombinant Cat. No. NATE-1708 Lot. No. (See product label) Introduction Description SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. The SUMO protease 1 can be used to cleave SUMO protein tag from recombinant SUMO-fusion proteins. The optimal temperature for cleavage is 30°C; however, the enzyme is active over wide ranges of temperature and pH. After the completion of the cleavage reaction, the protease can be easily removed from the reaction by affinity chromatography using the Glutathione resin. Synonyms Ulp1 peptidase; SUMO Protease; SUMO Protease Product Information Species Yeast Source E. coli Form Liquid EC Number EC 3.4.22.68 Molecular Weight 52.6 kDa (403-621 aa + N-terminal GST). Purity > 90% by SDS-PAGE Activity >10,000 units/mg Concentration 1 mg/ml Unit Definition One unit is defined as the amount of SUMO Protease 1 required to cleave >90% of 5 µg a control protein substrate (SUMO-GFP) in 1 h at 37°C. Creative Enzymes. All rights reserved. 45-1 Ramsey Road, Shirley, NY 11967, USA Tel:1-631-562-8517 1-516-512-3133 Fax:1-631-938-8127 E-mail: [email protected] http://www.creative-enzymes.com Notes INTENDED FOR RESEARCH USE ONLY, NOT FOR USE IN HUMAN, THERAPEUTIC OR DIAGNOSTIC APPLICATIONS. Storage and Shipping Information Storage Store at -80°C. Stable for at least 1 year as supplied. It may be further diluted to 0.1-0.5 mg/ml with 50 mM Tris-HCl, 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 and stored at –20°C in aliquots. Avoid repeated freezing and thawing cycles. Creative Enzymes. All rights reserved. 45-1 Ramsey Road, Shirley, NY 11967, USA Tel:1-631-562-8517 1-516-512-3133 Fax:1-631-938-8127 E-mail: [email protected] http://www.creative-enzymes.com.
Recommended publications
  • Babela Massiliensis, a Representative of a Widespread Bacterial
    Babela massiliensis, a representative of a widespread bacterial phylum with unusual adaptations to parasitism in amoebae Isabelle Pagnier, Natalya Yutin, Olivier Croce, Kira S Makarova, Yuri I Wolf, Samia Benamar, Didier Raoult, Eugene V. Koonin, Bernard La Scola To cite this version: Isabelle Pagnier, Natalya Yutin, Olivier Croce, Kira S Makarova, Yuri I Wolf, et al.. Babela mas- siliensis, a representative of a widespread bacterial phylum with unusual adaptations to parasitism in amoebae. Biology Direct, BioMed Central, 2015, 10 (13), 10.1186/s13062-015-0043-z. hal-01217089 HAL Id: hal-01217089 https://hal-amu.archives-ouvertes.fr/hal-01217089 Submitted on 19 Oct 2015 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Pagnier et al. Biology Direct (2015) 10:13 DOI 10.1186/s13062-015-0043-z RESEARCH Open Access Babela massiliensis, a representative of a widespread bacterial phylum with unusual adaptations to parasitism in amoebae Isabelle Pagnier1, Natalya Yutin2, Olivier Croce1, Kira S Makarova2, Yuri I Wolf2, Samia Benamar1, Didier Raoult1, Eugene V Koonin2 and Bernard La Scola1* Abstract Background: Only a small fraction of bacteria and archaea that are identifiable by metagenomics can be grown on standard media.
    [Show full text]
  • WO 2013/185113 Al 12 December 2013 (12.12.2013) P O P C T
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization I International Bureau (10) International Publication Number (43) International Publication Date WO 2013/185113 Al 12 December 2013 (12.12.2013) P O P C T (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every A61K 38/02 (2006.01) A61P 7/02 (2006.01) kind of national protection available): AE, AG, AL, AM, A61K 38/36 (2006.01) AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, (21) Number: International Application DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, PCT/US20 13/044841 HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KN, KP, KR, (22) International Filing Date: KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, 7 June 2013 (07.06.2013) MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SC, (25) Filing Language: English SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, (26) Publication Language: English TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (30) Priority Data: (84) Designated States (unless otherwise indicated, for every 61/657,688 8 June 2012 (08.06.2012) kind of regional protection available): ARIPO (BW, GH, 61/800,626 15 March 2013 (15.03.2013) GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, (71) Applicant: BIOGEN IDEC MA INC.
    [Show full text]
  • Next Generation Sequencing Identifies Five Major Classes of Potentially Therapeutic Enzymes Secreted by Lucilia Sericata Medical Maggots
    Hindawi Publishing Corporation BioMed Research International Volume 2016, Article ID 8285428, 27 pages http://dx.doi.org/10.1155/2016/8285428 Research Article Next Generation Sequencing Identifies Five Major Classes of Potentially Therapeutic Enzymes Secreted by Lucilia sericata Medical Maggots Zdenjk Franta,1 Heiko Vogel,2 Rüdiger Lehmann,1 Oliver Rupp,3 Alexander Goesmann,3 and Andreas Vilcinskas1,4 1 Department of Bioresources, Fraunhofer Institute for Molecular Biology and Applied Ecology, Winchesterstraße 2, 35394 Giessen, Germany 2Department of Entomology, Max Planck Institute for Chemical Ecology, Hans-Knoll-Straße¨ 8, 07745 Jena, Germany 3Justus-Liebig-University of Giessen, Bioinformatics and System Biology, Heinrich-Buff-Ring 58, 35392 Giessen, Germany 4Justus-Liebig-University of Giessen, Institute for Insect Biotechnology, Heinrich-Buff-Ring 26-32, 35392 Giessen, Germany Correspondence should be addressed to Andreas Vilcinskas; [email protected] Received 29 January 2016; Accepted 7 March 2016 Academic Editor: Yudong Cai Copyright © 2016 Zdenekˇ Franta et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Lucilia sericata larvae are used as an alternative treatment for recalcitrant and chronic wounds. Their excretions/secretions contain molecules that facilitate tissue debridement, disinfect, or accelerate wound healing and have therefore
    [Show full text]
  • Biochemical Investigation of the Ubiquitin Carboxyl-Terminal Hydrolase Family" (2015)
    Purdue University Purdue e-Pubs Open Access Dissertations Theses and Dissertations Spring 2015 Biochemical investigation of the ubiquitin carboxyl- terminal hydrolase family Joseph Rashon Chaney Purdue University Follow this and additional works at: https://docs.lib.purdue.edu/open_access_dissertations Part of the Biochemistry Commons, Biophysics Commons, and the Molecular Biology Commons Recommended Citation Chaney, Joseph Rashon, "Biochemical investigation of the ubiquitin carboxyl-terminal hydrolase family" (2015). Open Access Dissertations. 430. https://docs.lib.purdue.edu/open_access_dissertations/430 This document has been made available through Purdue e-Pubs, a service of the Purdue University Libraries. Please contact [email protected] for additional information. *UDGXDWH6FKRRO)RUP 8SGDWHG PURDUE UNIVERSITY GRADUATE SCHOOL Thesis/Dissertation Acceptance 7KLVLVWRFHUWLI\WKDWWKHWKHVLVGLVVHUWDWLRQSUHSDUHG %\ Joseph Rashon Chaney (QWLWOHG BIOCHEMICAL INVESTIGATION OF THE UBIQUITIN CARBOXYL-TERMINAL HYDROLASE FAMILY Doctor of Philosophy )RUWKHGHJUHHRI ,VDSSURYHGE\WKHILQDOH[DPLQLQJFRPPLWWHH Chittaranjan Das Angeline Lyon Christine A. Hrycyna George M. Bodner To the best of my knowledge and as understood by the student in the Thesis/Dissertation Agreement, Publication Delay, and Certification/Disclaimer (Graduate School Form 32), this thesis/dissertation adheres to the provisions of Purdue University’s “Policy on Integrity in Research” and the use of copyrighted material. Chittaranjan Das $SSURYHGE\0DMRU3URIHVVRU V BBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBB BBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBBB $SSURYHGE\R. E. Wild 04/24/2015 +HDGRIWKH'HSDUWPHQW*UDGXDWH3URJUDP 'DWH BIOCHEMICAL INVESTIGATION OF THE UBIQUITIN CARBOXYL-TERMINAL HYDROLASE FAMILY Dissertation Submitted to the Faculty of Purdue University by Joseph Rashon Chaney In Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy May 2015 Purdue University West Lafayette, Indiana ii All of this I dedicate wife, Millicent, to my faithful and beautiful children, Josh and Caleb.
    [Show full text]
  • Babela Massiliensis, a Representative of A
    Pagnier et al. Biology Direct (2015) 10:13 DOI 10.1186/s13062-015-0043-z RESEARCH Open Access Babela massiliensis, a representative of a widespread bacterial phylum with unusual adaptations to parasitism in amoebae Isabelle Pagnier1, Natalya Yutin2, Olivier Croce1, Kira S Makarova2, Yuri I Wolf2, Samia Benamar1, Didier Raoult1, Eugene V Koonin2 and Bernard La Scola1* Abstract Background: Only a small fraction of bacteria and archaea that are identifiable by metagenomics can be grown on standard media. Recent efforts on deep metagenomics sequencing, single-cell genomics and the use of specialized culture conditions (culturomics) increasingly yield novel microbes some of which represent previously uncharacterized phyla and possess unusual biological traits. Results: We report isolation and genome analysis of Babela massiliensis, an obligate intracellular parasite of Acanthamoeba castellanii. B. massiliensis shows an unusual, fission mode of cell multiplication whereby large, polymorphic bodies accumulate in the cytoplasm of infected amoeba and then split into mature bacterial cells. This unique mechanism of cell division is associated with a deep degradation of the cell division machinery and delayed expression of the ftsZ gene. The genome of B. massiliensis consists of a circular chromosome approximately 1.12 megabase in size that encodes, 981 predicted proteins, 38 tRNAs and one typical rRNA operon. Phylogenetic analysis shows that B. massiliensis belongs to the putative bacterial phylum TM6 that so far was represented by the draft genome of the JCVI TM6SC1 bacterium obtained by single cell genomics and numerous environmental sequences. Conclusions: Currently, B. massiliensis is the only cultivated member of the putative TM6 phylum. Phylogenomic analysis shows diverse taxonomic affinities for B.
    [Show full text]
  • Structural Insights Into Inhibitory Mechanisms of Cathepsin K
    STRUCTURAL INSIGHTS INTO INHIBITORY MECHANISMS OF CATHEPSIN K by Simon Sau Yin Law B.Sc., The University of British Columbia, 2013 A THESIS SUBMITTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY in THE FACULTY OF GRADUATE AND POSTDOCTORAL STUDIES (BIOCHEMISTRY AND MOLECULAR BIOLOGY) THE UNIVERSITY OF BRITISH COLUMBIA (Vancouver) December 2018 © Simon Sau Yin Law, 2018 The following individuals certify that they have read, and recommend to the Faculty of Graduate and Postdoctoral Studies for acceptance, the dissertation entitled: Structural Insights into Inhibitory Mechanisms of Cathepsin K submitted by Simon Sau Yin Law in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biochemistry and Molecular Biology Examining Committee: Dieter Bromme, Oral Biological and Medical Sciences Supervisor Chris Overall, Oral Biological and Medical Sciences Supervisory Committee Member Christian Kastrup, Biochemistry and Molecular Biology Supervisory Committee Member Katherine Ryan, Chemistry University Examiner Filip Van Petegem, Biochemistry and Molecular Biology University Examiner ii Abstract Cathepsin K (CatK) is a lysosomal cysteine protease highly expressed in osteoclasts and is responsible for the degradation of bone. Implication of CatK in various musculoskeletal disorders including osteoporosis highlights CatK as an important target for drug development. This thesis aims to identify and characterize different classes of CatK inhibitors, which target the active site and collagenolytically relevant ectosteric sites using X-ray crystallography combined with mutational and kinetic studies. In chapter 2, odanacatib, a specific CatK inhibitor recently abandoned in clinical trials due to adverse side effects, was investigated for its selectivity for mouse CatK over the human counterpart.
    [Show full text]
  • All Enzymes in BRENDA™ the Comprehensive Enzyme Information System
    All enzymes in BRENDA™ The Comprehensive Enzyme Information System http://www.brenda-enzymes.org/index.php4?page=information/all_enzymes.php4 1.1.1.1 alcohol dehydrogenase 1.1.1.B1 D-arabitol-phosphate dehydrogenase 1.1.1.2 alcohol dehydrogenase (NADP+) 1.1.1.B3 (S)-specific secondary alcohol dehydrogenase 1.1.1.3 homoserine dehydrogenase 1.1.1.B4 (R)-specific secondary alcohol dehydrogenase 1.1.1.4 (R,R)-butanediol dehydrogenase 1.1.1.5 acetoin dehydrogenase 1.1.1.B5 NADP-retinol dehydrogenase 1.1.1.6 glycerol dehydrogenase 1.1.1.7 propanediol-phosphate dehydrogenase 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) 1.1.1.9 D-xylulose reductase 1.1.1.10 L-xylulose reductase 1.1.1.11 D-arabinitol 4-dehydrogenase 1.1.1.12 L-arabinitol 4-dehydrogenase 1.1.1.13 L-arabinitol 2-dehydrogenase 1.1.1.14 L-iditol 2-dehydrogenase 1.1.1.15 D-iditol 2-dehydrogenase 1.1.1.16 galactitol 2-dehydrogenase 1.1.1.17 mannitol-1-phosphate 5-dehydrogenase 1.1.1.18 inositol 2-dehydrogenase 1.1.1.19 glucuronate reductase 1.1.1.20 glucuronolactone reductase 1.1.1.21 aldehyde reductase 1.1.1.22 UDP-glucose 6-dehydrogenase 1.1.1.23 histidinol dehydrogenase 1.1.1.24 quinate dehydrogenase 1.1.1.25 shikimate dehydrogenase 1.1.1.26 glyoxylate reductase 1.1.1.27 L-lactate dehydrogenase 1.1.1.28 D-lactate dehydrogenase 1.1.1.29 glycerate dehydrogenase 1.1.1.30 3-hydroxybutyrate dehydrogenase 1.1.1.31 3-hydroxyisobutyrate dehydrogenase 1.1.1.32 mevaldate reductase 1.1.1.33 mevaldate reductase (NADPH) 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH) 1.1.1.35 3-hydroxyacyl-CoA
    [Show full text]
  • Dictionary of DNA and Genome Technology, Second Edition
    Dictionary of DNA and Genome Technology Second Edition Paul Singleton A John Wiley & Sons, Ltd., Publication Dictionary of DNA and Genome Technology Second Edition Dictionary of DNA and Genome Technology Second Edition Paul Singleton A John Wiley & Sons, Ltd., Publication Ó 2010 Paul Singleton First edition 2008 Second edition 2010 Wiley-Blackwell is an imprint of John Wiley & Sons, formed by the merger of Wiley’s global Scientific, Technical and Medical business with Blackwell Publishing. Registered office: John Wiley & Sons Ltd, The Atrium, Southern Gate, Chichester, West Sussex, PO19 8SQ, UK Other Editorial Offices: 9600 Garsington Road, Oxford, OX4 2DQ, UK 111 River Street, Hoboken, NJ 07030-5774, USA For details of our global editorial offices, for customer services and for information about how to apply for permission to reuse the copyright material in this book please see our website at www.wiley.com/wiley-blackwell The right of the author to be identified as the author of this work has been asserted in accordance with the Copyright, Designs and Patents Act 1988. All rights reserved. No part of this publication may be reproduced, stored in a retrieval system, or transmitted, in any form or by any means, electronic, mechanical, photocopying, recording or otherwise, except as permitted by the UK Copyright, Designs and Patents Act 1988, without the prior permission of the publisher. Wiley also publishes its books in a variety of electronic formats. Some content that appears in print may not be available in electronic books. Designations used by companies to distinguish their products are often claimed as trademarks.
    [Show full text]
  • Ezcut™ SUMO Protease 1 (His-Tagged), Yeast Recombinant Rev.05/17 Store at -80°C
    FOR RESEARCH USE ONLY! EZCut™ SUMO Protease 1 (His-tagged), Yeast Recombinant rev.05/17 Store at -80°C. Cat. No.: 7868-500 500 U Cat. No.: 7868-2500 2500 U Cat. No.: 7868-10000 10000 U ALTERNATE NAMES: Ulp1 peptidase, SUMO Protease SOURCE: E. coli FORM: Liquid SDS-PAGE (4-20%) of FORMULATION: 0.1 mg/ml (100 U/µl) solution in 50 mM Tris-HCl, EZCut™ His-SUMO 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 Protease 1: M: Protein Marker PURITY: ≥ 90% by SDS-PAGE 1: His-SUMO 1 (10 μg) 2: His-SUMO 1 (15 μg) MOL. WT.: 28.7 kDa (403-621 aa + N-terminal Poly-His tag). 3: His-SUMO 1 (20 μg) STORAGE CONDITIONS: Store at -80°C. Stable for at least 1 year as supplied. It may be further diluted to 0.01-0.05 mg/ml with 50 mM Tris-HCl, 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 and stored at –20°C in aliquots. Avoid repeated freezing and thawing cycles. BACKGROUND: SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. BioVision’s Recombinant EZCut™ SUMO Protease 1 containing an N-terminal His-tag is expressed in E.
    [Show full text]
  • BMC Genomics Biomed Central
    BMC Genomics BioMed Central Research article Open Access The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes Manuela Tillack1, Laura Biller1, Henriette Irmer1, Michelle Freitas2, Maria A Gomes2, Egbert Tannich1 and Iris Bruchhaus*1 Address: 1Bernhard Nocht Institute for Tropical Medicine, Bernhard Nocht Str. 74, 20359 Hamburg, Germany and 2University of Minas Gerais, Dept. Parasitologia, ICB-UFMG, Laboratorio Amebiase, Av. Antonio Carlos, 6627, 31270-901 Belo Horizonte, Brasil Email: Manuela Tillack - [email protected]; Laura Biller - [email protected]; Henriette Irmer - [email protected]; Michelle Freitas - [email protected]; Maria A Gomes - [email protected]; Egbert Tannich - [email protected]; Iris Bruchhaus* - [email protected] * Corresponding author Published: 14 June 2007 Received: 14 March 2007 Accepted: 14 June 2007 BMC Genomics 2007, 8:170 doi:10.1186/1471-2164-8-170 This article is available from: http://www.biomedcentral.com/1471-2164/8/170 © 2007 Tillack et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract Background: A number of studies have shown that peptidases and in particular cysteine peptidases constitute major pathogenicity factors in Entamoeba histolytica. Recent studies have suggested that a considerable number of genes coding for proteolytic enzymes are present within the E. histolytica genome and questions remain about the mode of expression of the various molecules. Results: By homology search within the recently published amoeba genome, we identified a total of 86 E.
    [Show full text]
  • Springer Handbook of Enzymes
    Dietmar Schomburg Ida Schomburg (Eds.) Springer Handbook of Enzymes Alphabetical Name Index 1 23 © Springer-Verlag Berlin Heidelberg New York 2010 This work is subject to copyright. All rights reserved, whether in whole or part of the material con- cerned, specifically the right of translation, printing and reprinting, reproduction and storage in data- bases. The publisher cannot assume any legal responsibility for given data. Commercial distribution is only permitted with the publishers written consent. Springer Handbook of Enzymes, Vols. 1–39 + Supplements 1–7, Name Index 2.4.1.60 abequosyltransferase, Vol. 31, p. 468 2.7.1.157 N-acetylgalactosamine kinase, Vol. S2, p. 268 4.2.3.18 abietadiene synthase, Vol. S7,p.276 3.1.6.12 N-acetylgalactosamine-4-sulfatase, Vol. 11, p. 300 1.14.13.93 (+)-abscisic acid 8’-hydroxylase, Vol. S1, p. 602 3.1.6.4 N-acetylgalactosamine-6-sulfatase, Vol. 11, p. 267 1.2.3.14 abscisic-aldehyde oxidase, Vol. S1, p. 176 3.2.1.49 a-N-acetylgalactosaminidase, Vol. 13,p.10 1.2.1.10 acetaldehyde dehydrogenase (acetylating), Vol. 20, 3.2.1.53 b-N-acetylgalactosaminidase, Vol. 13,p.91 p. 115 2.4.99.3 a-N-acetylgalactosaminide a-2,6-sialyltransferase, 3.5.1.63 4-acetamidobutyrate deacetylase, Vol. 14,p.528 Vol. 33,p.335 3.5.1.51 4-acetamidobutyryl-CoA deacetylase, Vol. 14, 2.4.1.147 acetylgalactosaminyl-O-glycosyl-glycoprotein b- p. 482 1,3-N-acetylglucosaminyltransferase, Vol. 32, 3.5.1.29 2-(acetamidomethylene)succinate hydrolase, p. 287 Vol.
    [Show full text]
  • Molecular Characterisation of Two Ornithodoros Savignyi Enzyme Isoforms from the 5
    Gene expression profiling of adult female tissues in feeding Rhipicephalus microplus cattle ticks Christian Stutzera, Willem A. van Zyla, Nicholas A. Olivierb, Sabine Richardsc, Christine Maritz-Olivierc,* aDepartment of Biochemistry, Faculty of Natural and Agricultural Sciences, University of Pretoria, South Africa, 0002. bACGT DNA microarray facility, Department of Plant Sciences, Faculty of Natural and Agricultural Sciences, University of Pretoria, South Africa, 0002. cDepartment of Genetics, Faculty of Natural and Agricultural Sciences, University of Pretoria, South Africa, 0002. *Corresponding author:.Tel: +27 012 420 3945; fax: +27 012 362 5327 E-mail address: [email protected] Note: Supplementary data associated with this article. Note: The microarray and sequence data related to this work is available via the NCBI GEO database, GEO accession no. GSE35867. 1 Abstract The southern cattle tick, Rhipicephalus microplus, is an economically important pest, especially for resource-poor countries, both as a highly adaptive invasive species and prominent vector of disease. The increasing prevalence of resistance to chemical acaricides and variable efficacy of current tick vaccine candidates highlight the need for more effective control methods. In the absence of a fully annotated genome, the wealth of available expressed sequence tag (EST) sequence data for this species presents a unique opportunity to study the genes that are expressed in tissues involved in blood meal acquisition, digestion and reproduction during feeding. Utilizing a custom oligonucleotide microarray designed from available singletons (BmiGI Version 2.1) and EST sequences of R. microplus, the expression profiles in feeding adult female midgut, salivary glands and ovarian tissues were compared. From 13,456 assembled transcripts, 588 genes expressed in all three tissues were identified from fed adult females 20 days post infestation.
    [Show full text]