The Small Gtpases in Fungal Signaling Conservation and Function
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Anti-Rab11 Antibody (ARG41900)
Product datasheet [email protected] ARG41900 Package: 100 μg anti-Rab11 antibody Store at: -20°C Summary Product Description Goat Polyclonal antibody recognizes Rab11 Tested Reactivity Hu, Ms, Rat, Dog, Mk Tested Application IHC-Fr, IHC-P, WB Host Goat Clonality Polyclonal Isotype IgG Target Name Rab11 Antigen Species Mouse Immunogen Purified recombinant peptides within aa. 110 to the C-terminus of Mouse Rab11a, Rab11b and Rab11c (Rab25). Conjugation Un-conjugated Alternate Names RAB11A: Rab-11; Ras-related protein Rab-11A; YL8 RAB11B: GTP-binding protein YPT3; H-YPT3; Ras-related protein Rab-11B RAB25: RAB11C; CATX-8; Ras-related protein Rab-25 Application Instructions Application table Application Dilution IHC-Fr 1:100 - 1:400 IHC-P 1:100 - 1:400 WB 1:250 - 1:2000 Application Note IHC-P: Antigen Retrieval: Heat mediation was recommended. * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control Hepa cell lysate Calculated Mw 24 kDa Observed Size ~ 26 kDa Properties Form Liquid Purification Affinity purification with immunogen. Buffer PBS, 0.05% Sodium azide and 20% Glycerol. Preservative 0.05% Sodium azide www.arigobio.com 1/3 Stabilizer 20% Glycerol Concentration 3 mg/ml Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. -
Endophytic Fungi: Biological Control and Induced Resistance to Phytopathogens and Abiotic Stresses
pathogens Review Endophytic Fungi: Biological Control and Induced Resistance to Phytopathogens and Abiotic Stresses Daniele Cristina Fontana 1,† , Samuel de Paula 2,*,† , Abel Galon Torres 2 , Victor Hugo Moura de Souza 2 , Sérgio Florentino Pascholati 2 , Denise Schmidt 3 and Durval Dourado Neto 1 1 Department of Plant Production, Luiz de Queiroz College of Agriculture, University of São Paulo, Piracicaba 13418900, Brazil; [email protected] (D.C.F.); [email protected] (D.D.N.) 2 Plant Pathology Department, Luiz de Queiroz College of Agriculture, University of São Paulo, Piracicaba 13418900, Brazil; [email protected] (A.G.T.); [email protected] (V.H.M.d.S.); [email protected] (S.F.P.) 3 Department of Agronomy and Environmental Science, Frederico Westphalen Campus, Federal University of Santa Maria, Frederico Westphalen 98400000, Brazil; [email protected] * Correspondence: [email protected]; Tel.: +55-54-99646-9453 † These authors contributed equally to this work. Abstract: Plant diseases cause losses of approximately 16% globally. Thus, management measures must be implemented to mitigate losses and guarantee food production. In addition to traditional management measures, induced resistance and biological control have gained ground in agriculture due to their enormous potential. Endophytic fungi internally colonize plant tissues and have the potential to act as control agents, such as biological agents or elicitors in the process of induced resistance and in attenuating abiotic stresses. In this review, we list the mode of action of this group of Citation: Fontana, D.C.; de Paula, S.; microorganisms which can act in controlling plant diseases and describe several examples in which Torres, A.G.; de Souza, V.H.M.; endophytes were able to reduce the damage caused by pathogens and adverse conditions. -
Genome Scale Metabolic Modeling of the Riboflavin Overproducer Ashbya Gossypii
Chalmers Publication Library Genome Scale Metabolic Modeling of the Riboflavin Overproducer Ashbya gossypii This document has been downloaded from Chalmers Publication Library (CPL). It is the author´s version of a work that was accepted for publication in: Biotechnology and Bioengineering (ISSN: 0006-3592) Citation for the published paper: Ledesma-Amaro, R. ; Kerkhoven, E. ; Revuelta, J. (2014) "Genome Scale Metabolic Modeling of the Riboflavin Overproducer Ashbya gossypii". Biotechnology and Bioengineering, vol. 111(6), pp. 1191-1199. http://dx.doi.org/10.1002/bit.25167 Downloaded from: http://publications.lib.chalmers.se/publication/200098 Notice: Changes introduced as a result of publishing processes such as copy-editing and formatting may not be reflected in this document. For a definitive version of this work, please refer to the published source. Please note that access to the published version might require a subscription. Chalmers Publication Library (CPL) offers the possibility of retrieving research publications produced at Chalmers University of Technology. It covers all types of publications: articles, dissertations, licentiate theses, masters theses, conference papers, reports etc. Since 2006 it is the official tool for Chalmers official publication statistics. To ensure that Chalmers research results are disseminated as widely as possible, an Open Access Policy has been adopted. The CPL service is administrated and maintained by Chalmers Library. (article starts on next page) ARTICLE Genome Scale Metabolic Modeling of the -
Crystal Structure of a Small G Protein in Complex with the Gtpase
letters to nature of apolipoproteins2,12–14. However, our results show that the residues lipoprotein metabolism involving cell surface heparan sulfate proteoglycans. J. Biol. Chem. 269, 2764– 2+ 2772 (1994). in the conserved acidic motif of LR5 are buried to participate in Ca 16. Innerarity, T. L., Pitas, R. E. & Mahley, R. W. Binding of arginine-rich (E) apoprotein after coordination, instead of being exposed on the surface of the domain recombination with phospholipid vesicles to the low density lipoprotein receptors of fibroblasts. J. Biol. Chem. 254, 4186–4190 (1979). (Fig. 4a). Although lipoprotein uptake by members of the LDLR 17. Otwinowski, Z. & Minor, W. Data Collection and Processing (eds Sawyer, L., Isaacs, N. & Bailey, S.) family may involve an electrostatic component, perhaps through 556–562 (SERC Daresbury Laboratory, Warrington, UK, 1993). association of the lipoproteins with cell-surface proteoglycans15, the 18. CCP4. The SERC (UK) Collaborative Computing Project No. 4 A Suite of Programs for Protein Crystallography (SERC Daresbury Laboratory, Warrington, UK, 1979). LR5 structure demonstrates that the primary role for the conserved 19. Cowtan, K. D. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 31, 34–38 (1994). acidic residues in LDL-A modules is structural. It has been noted 20. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110–119 previously that only lipid-associated apolipoproteins bind with (1991). 16 high affinity to the LDLR ; the LR5 structure suggests an alternative 21. -
Protein Prenylation Reactions As Tools for Site-Specific Protein Labeling and Identification of Prenylation Substrates
Protein prenylation reactions as tools for site-specific protein labeling and identification of prenylation substrates Dissertation zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften (Dr. rer. nat.) des Fachbereichs Chemie der Technischen Universität Dortmund Angefertigt am Max-Planck-Institut für molekulare Physiologie in Dortmund Vorgelegt von Dipl.-Chemikerin Thi Thanh Uyen Nguyen aus Jülich Dortmund, April 2009 Die vorliegende Arbeit wurde in der Zeit von Oktober 2005 bis April 2009 am Max-Planck- Institut für molekulare Physiologie in Dortmund unter der Anleitung von Prof. Dr. Roger S. Goody, Prof. Dr. Kirill Alexandrov und Prof. Dr. Herbert Waldmann durchgeführt. 1. Gutachter : Prof. Dr. R. S. Goody 2. Gutachter : Prof. Dr. H. Waldmann The results of this work were published in the following journals: “Exploiting the substrate tolerance of farnesyltransferase for site-selective protein derivatization” U.T.T. Nguyen, J. Cramer, J. Gomis, R. Reents, M. Gutierrez-Rodriguez, R.S. Goody, K. Alexandrov, H. Waldmann, Chembiochem 2007, 8 (4), 408-23. “Development of selective RabGGTase inhibitors and crystal structure of a RabGGTase- inhibitor complex” Z. Guo, Y.W. Wu, K.T. Tan, R.S. Bon, E. Guiu-Rozas, C. Delon, U.T.T. Nguyen, S. Wetzel,S. Arndt, R.S. Goody, W. Blankenfeldt, K. Alexandrov, H. Waldmann, Angew Chem Int Ed Engl 2008, 47 (20), 3747-50. “Analysis of the eukaryotic prenylome by isoprenoid affinity tagging” U.T.T. Nguyen, Z. Guo, C. Delon, Y.W. Wu, C. Deraeve, B. Franzel, R.S. Bon, W. Blankenfeldt, R.S. Goody, H. Waldmann, D. Wolters, K. Alexandrov, Nat Chem Biol 2009, 5 (4), 227-35. -
Ras Gtpase Chemi ELISA Kit Catalog No
Ras GTPase Chemi ELISA Kit Catalog No. 52097 (Version B3) Active Motif North America 1914 Palomar Oaks Way, Suite 150 Carlsbad, California 92008, USA Toll free: 877 222 9543 Telephone: 760 431 1263 Fax: 760 431 1351 Active Motif Europe Waterloo Atrium Drève Richelle 167 – boîte 4 BE-1410 Waterloo, Belgium UK Free Phone: 0800 169 31 47 France Free Phone: 0800 90 99 79 Germany Free Phone: 0800 181 99 10 Telephone: +32 (0)2 653 0001 Fax: +32 (0)2 653 0050 Active Motif Japan Azuma Bldg, 7th Floor 2-21 Ageba-Cho, Shinjuku-Ku Tokyo, 162-0824, Japan Telephone: +81 3 5225 3638 Fax: +81 3 5261 8733 Active Motif China 787 Kangqiao Road Building 10, Suite 202, Pudong District Shanghai, 201315, China Telephone: (86)-21-20926090 Hotline: 400-018-8123 Copyright 2021 Active Motif, Inc. www.activemotif.com Information in this manual is subject to change without notice and does not constitute a commit- ment on the part of Active Motif, Inc. It is supplied on an “as is” basis without any warranty of any kind, either explicit or implied. Information may be changed or updated in this manual at any time. This documentation may not be copied, transferred, reproduced, disclosed, or duplicated, in whole or in part, without the prior written consent of Active Motif, Inc. This documentation is proprietary information and protected by the copyright laws of the United States and interna- tional treaties. The manufacturer of this documentation is Active Motif, Inc. © 2021 Active Motif, Inc., 1914 Palomar Oaks Way, Suite 150; Carlsbad, CA 92008. -
Focus on Cdc42 in Breast Cancer: New Insights, Target Therapy Development and Non-Coding Rnas
Review Focus on Cdc42 in Breast Cancer: New Insights, Target Therapy Development and Non-Coding RNAs Yu Zhang †, Jun Li †, Xing-Ning Lai, Xue-Qiao Jiao, Jun-Ping Xiong and Li-Xia Xiong * Department of Pathophysiology, Jiangxi Province Key Laboratory of Tumor Pathogenesis and Molecular Pathology, Medical College, Nanchang University, 461 Bayi Road, Nanchang 330006, China; [email protected] (Y.Z.); [email protected] (J.L.); [email protected] (X.-N.L.); [email protected] (X.-Q.J.); [email protected] (J.-P.X.) * Correspondence: [email protected]; Tel.: +86-791-8636-0556 † These authors contributed equally to this work. Received: 30 December 2018; Accepted: 8 February 2019; Published: 11 February 2019 Abstract: Breast cancer is the most common malignant tumors in females. Although the conventional treatment has demonstrated a certain effect, some limitations still exist. The Rho guanosine triphosphatase (GTPase) Cdc42 (Cell division control protein 42 homolog) is often upregulated by some cell surface receptors and oncogenes in breast cancer. Cdc42 switches from inactive guanosine diphosphate (GDP)-bound to active GTP-bound though guanine-nucleotide- exchange factors (GEFs), results in activation of signaling cascades that regulate various cellular processes such as cytoskeletal changes, proliferation and polarity establishment. Targeting Cdc42 also provides a strategy for precise breast cancer therapy. In addition, Cdc42 is a potential target for several types of non-coding RNAs including microRNAs and lncRNAs. These non-coding RNAs is extensively involved in Cdc42-induced tumor processes, while many of them are aberrantly expressed. Here, we focus on the role of Cdc42 in cell morphogenesis, proliferation, motility, angiogenesis and survival, introduce the Cdc42-targeted non-coding RNAs, as well as present current development of effective Cdc42-targeted inhibitors in breast cancer. -
Hras Intracellular Trafficking and Signal Transduction Jodi Ho-Jung Mckay Iowa State University
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 2007 HRas intracellular trafficking and signal transduction Jodi Ho-Jung McKay Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biological Phenomena, Cell Phenomena, and Immunity Commons, Cancer Biology Commons, Cell Biology Commons, Genetics and Genomics Commons, and the Medical Cell Biology Commons Recommended Citation McKay, Jodi Ho-Jung, "HRas intracellular trafficking and signal transduction" (2007). Retrospective Theses and Dissertations. 13946. https://lib.dr.iastate.edu/rtd/13946 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. HRas intracellular trafficking and signal transduction by Jodi Ho-Jung McKay A dissertation submitted to the graduate faculty in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Major: Genetics Program of Study Committee: Janice E. Buss, Co-major Professor Linda Ambrosio, Co-major Professor Diane Bassham Drena Dobbs Ted Huiatt Iowa State University Ames, Iowa 2007 Copyright © Jodi Ho-Jung McKay, 2007. All rights reserved. UMI Number: 3274881 Copyright 2007 by McKay, Jodi Ho-Jung All rights reserved. UMI Microform 3274881 Copyright 2008 by ProQuest Information and Learning Company. All rights reserved. This microform edition is protected against unauthorized copying under Title 17, United States Code. ProQuest Information and Learning Company 300 North Zeeb Road P.O. -
Colletotrichum – Names in Current Use
Online advance Fungal Diversity Colletotrichum – names in current use Hyde, K.D.1,7*, Cai, L.2, Cannon, P.F.3, Crouch, J.A.4, Crous, P.W.5, Damm, U. 5, Goodwin, P.H.6, Chen, H.7, Johnston, P.R.8, Jones, E.B.G.9, Liu, Z.Y.10, McKenzie, E.H.C.8, Moriwaki, J.11, Noireung, P.1, Pennycook, S.R.8, Pfenning, L.H.12, Prihastuti, H.1, Sato, T.13, Shivas, R.G.14, Tan, Y.P.14, Taylor, P.W.J.15, Weir, B.S.8, Yang, Y.L.10,16 and Zhang, J.Z.17 1,School of Science, Mae Fah Luang University, Chaing Rai, Thailand 2Research & Development Centre, Novozymes, Beijing 100085, PR China 3CABI, Bakeham Lane, Egham, Surrey TW20 9TY, UK and Royal Botanic Gardens, Kew, Richmond, Surrey TW9 3AB, UK 4Cereal Disease Laboratory, U.S. Department of Agriculture, Agricultural Research Service, 1551 Lindig Street, St. Paul, MN 55108, USA 5CBS-KNAW Fungal Biodiversity Centre, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands 6School of Environmental Sciences, University of Guelph, Guelph, Ontario, N1G 2W1, Canada 7International Fungal Research & Development Centre, The Research Institute of Resource Insects, Chinese Academy of Forestry, Bailongsi, Kunming 650224, PR China 8Landcare Research, Private Bag 92170, Auckland 1142, New Zealand 9BIOTEC Bioresources Technology Unit, National Center for Genetic Engineering and Biotechnology, NSTDA, 113 Thailand Science Park, Paholyothin Road, Khlong 1, Khlong Luang, Pathum Thani, 12120, Thailand 10Guizhou Academy of Agricultural Sciences, Guiyang, Guizhou 550006 PR China 11Hokuriku Research Center, National Agricultural Research Center, -
ADP-Ribosylation Factor, a Small GTP-Binding Protein, Is Required for Binding of the Coatomer Protein Fl-COP to Golgi Membranes JULIE G
Proc. Natl. Acad. Sci. USA Vol. 89, pp. 6408-6412, July 1992 Biochemistry ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein fl-COP to Golgi membranes JULIE G. DONALDSON*, DAN CASSEL*t, RICHARD A. KAHN*, AND RICHARD D. KLAUSNER* *Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, and tLaboratory of Biological Chemistry, Division of Cancer Treatment, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892 Communicated by Marc Kirschner, April 20, 1992 (receivedfor review February 11, 1992) ABSTRACT The coatomer is a cytosolic protein complex localized to the Golgi complex, although their functions have that reversibly associates with Golgi membranes and is Impli- not been defined. Distinct among these proteins is the ADP- cated in modulating Golgi membrane transport. The associa- ribosylation factor (ARF), originally identified as a cofactor tion of 13-COP, a component of coatomer, with Golgi mem- required for in vitro cholera toxin-catalyzed ADP- branes is enhanced by guanosine 5'-[v-thioltriphosphate ribosylation of the a subunit of the trimeric GTP-binding (GTP[yS]), a nonhydrolyzable analogue of GTP, and by a protein G, (G,.) (19). ARF is an abundant cytosolic protein mixture of aluminum and fluoride ions (Al/F). Here we show that reversibly associates with Golgi membranes (20, 21). that the ADP-ribosylation factor (ARF) is required for the ARF has been shown to be present on Golgi coated vesicles binding of (-COP. Thus, 13-COP contained in a coatomer generated in the presence of GTP[yS], but it is not a com- fraction that has been resolved from ARF does not bind to Golgi ponent of the cytosolic coatomer (22). -
Small Rho Gtpase Family Member Cdc42 and Its Role in Neuronal Survival and Apoptosis
University of Denver Digital Commons @ DU Electronic Theses and Dissertations Graduate Studies 1-1-2017 Small Rho GTPase Family Member Cdc42 and Its Role in Neuronal Survival and Apoptosis Noelle Christine Punessen University of Denver Follow this and additional works at: https://digitalcommons.du.edu/etd Part of the Biology Commons, and the Genetics and Genomics Commons Recommended Citation Punessen, Noelle Christine, "Small Rho GTPase Family Member Cdc42 and Its Role in Neuronal Survival and Apoptosis" (2017). Electronic Theses and Dissertations. 1337. https://digitalcommons.du.edu/etd/1337 This Thesis is brought to you for free and open access by the Graduate Studies at Digital Commons @ DU. It has been accepted for inclusion in Electronic Theses and Dissertations by an authorized administrator of Digital Commons @ DU. For more information, please contact [email protected],[email protected]. Small Rho GTPase Family Member Cdc42 and its Role in Neuronal Survival and Apoptosis A Thesis Presented to the Faculty of Natural Sciences and Mathematics University of Denver In Partial Fulfillment of the Requirements for the Degree Master of Science by Noelle C. Punessen August 2017 Advisor: Dr. Daniel A. Linseman Author: Noelle C. Punessen Title: Small Rho GTPase Family Member Cdc42 and its Role in Neuronal Survival and Apoptosis Advisor: Dr. Daniel A. Linseman Degree Date: August 2017 Abstract Neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), Alzheimer’s and Parkinson’s disease are caused by a progressive and aberrant destruction of neurons in the brain and spinal cord. These disorders lack effective long term treatments, and existing options focus primarily on either delaying disease onset or alleviating symptomology. -
Clover Anthracnose Caused by Colletotrichum Trifolii
2 5 2 5 1.0 :; 1111128 1//// . :; 111112 8 11111 . Ww I~ 2.2 : I~ I 2.2 ~ W '"'w Ii£ w ~ ~ ~ ~ ~ 1.1 1.1 ...,a~ ... -- 111111.8 111111.8 '111111. 25 IIIII~ 111111.6 111111.25 111111.4 111111.6 MICROCOPY RESOLUTION TEST CH>XRT (MICROCOPY RESOLUTION TEST CHART NATIONAL BURlAU or SlANO;'RD~·196 H NATiONAL BUREAU OF SlA.NDARDS-1963·A ==========~=~:~========~TECHNICAL BULU'.TIN No. Z8~FEBRUARY. 19Z8 UNITlm:STATES DEPARTMENT OF AGRICULTURE WASHINGTON, D. C. CLOVER ANTHRACNOSE CAUSED BY COLLETOTRICHUM TRIFOLII By JOHN MONTEITH, Jr. ABsociate Pathologist, Office of Vegetable and Forage Diseases, Bureau of Plant Industry 1 CONTENTS Page Page rntroductlon _____________________ 1 The funguR in relntlon to anthrac ElIstol'Y and geogro9hlcal dlstrlbu- ., nos~('ontlnul'd. tlon___________________________ 3- Vlabillty Bnd longe't'lty ot DlY~ flost plnnts______________________ lIum and conidia ___________ 13 SYlI1ptom~ _______________________ 3 Dlsspmluution of conidla_______ 13 Inj lIty produced __________________ II Method of Infection and period The cau~,,1 ol'J~nnlsm--------------, 7 of Incubntlon_______________ 13 Tllxonomy __________.:.________ 7 Source of natural Infl'ctlon____ 14 l~olll t1ous____________________ 8 Environmental factors Influencing oc Spore germlnntlon ____________ 8 currence and progress of the dla- Cull ural characters ___________ 9 ease__________________________ 15 Helu tlon of tpllIpero ture to '.:'em peruture _________________ 15 growth 011 medIa ___________ \l hlolsture ____________________ 17 Errect of I\ght________________