DOCSLIB.ORG

DNA Polymerase Lambda (POLL) (NM 001174084) Human Tagged ORF Clone Product Data

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
DNA Polymerase Lambda (POLL) (NM 001174084) Human Tagged ORF Clone Product Data OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for RC230298 DNA Polymerase lambda (POLL) (NM_001174084) Human Tagged ORF Clone Product data: Product Type: Expression Plasmids Product Name: DNA Polymerase lambda (POLL) (NM_001174084) Human Tagged ORF Clone Tag: Myc-DDK Symbol: POLL Synonyms: BETAN; POLKAPPA Vector: pCMV6-Entry (PS100001) E. coli Selection: Kanamycin (25 ug/mL) Cell Selection: Neomycin This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 4 DNA Polymerase lambda (POLL) (NM_001174084) Human Tagged ORF Clone – RC230298 ORF Nucleotide >RC230298 ORF sequence Sequence: Red=Cloning site Blue=ORF Green=Tags(s) TTTTGTAATACGACTCACTATAGGGCGGCCGGGAATTCGTCGACTGGATCCGGTACCGAGGAGATCTGCC GCCGCGATCGCC ATGGATCCCAGGGGTATCTTGAAGGCATTTCCCAAGCGGCAGAAAATTCATGCTGATGCATCATCAAAAG TACTTGCAAAGATTCCTAGGAGGGAAGAGGGAGAAGAAGCAGAAGAGTGGCTGAGCTCCCTTCGGGCCCA TGTTGTGCGCACTGGCATTGGACGAGCCCGGGCAGAACTCTTTGAGAAGCAGATTGTTCAGCATGGCGGC CAGCTATGCCCTGCCCAGGGCCCAGGTGTCACTCACATTGTGGTGGATGAAGGCATGGACTATGAGCGAG CCCTCCGCCTTCTCAGACTACCCCAGCTGCCCCCGGGTGCTCAGCTGGTGAAGTCAGCCTGGCTGAGCTT GTGCCTTCAGGAGAGGAGGCTGGTGGATGTAGCTGGATTCAGCATCTTCATCCCCAGTAGGTACTTGGAC CATCCACAGCCCAGCAAGGCAGAGCAGGATGCTTCTATTCCTCCTGGCACCCATGAGGCCCTGCTTCAGA CAGCCCTTTCTCCTCCTCCTCCTCCCACCAGGCCTGTGTCTCCTCCCCAAAAGGCAAAAGAGGCACCAAA CACCCAAGCCCAGCCCATCTCTGATGATGAAGCCAGTGATGGGGAAGAAACCCAGGTTAGTGCAGCTGAT CTGGAAGCCCTCATCAGTGGCCACTACCCCACCTCCCTTGAGGGAGATTGTGAGCCTAGCCCAGCCCCTG CTGTCCTGGATAAGTGGGTCTGTGCACAGCCCTCAAGCCAGAAGGCGACCAATCACAACCTCCATATCAC AGAGAAGCTGGAAGTTCTGGCCAAAGCCTACAGTGTTCAGGGAGACAAGTGGAGGGCCCTGGGCTATGCC AAGGCCATCAATGCCCTCAAGAGCTTCCATAAGCCTGTCACCTCGTACCAGGGGGCCTGCAGTATCCCTG GGATTGGGAAGCGGATGGCTGAGAAAATCATAGAGATCCTGGAGAGCGGGCATTTGCGGAAGCTGGACCA TATCAGTGAGAGCGTGCCTGTCTTGGAGCTCTTCTCCAACATCTGGGGAGCTGGGACCAAGACTGCCCAG ATGTGGTACCAACAGGGCTTCCGAAGTCTGGAAGACATCCGCAGCCAGGCCTCCCTGACAACCCAGCAGG CCATCGGCCTGAAGCATTACAGTGACTTCCTGGAACGTATGCCCAGGGAGGAGGCTACAGAGATTGAGCA GACAGTCCAGAAAGCAGCCCAGGCCTTTAACTCTGGGCTGCTGTGTGTGGCATGTGGTTCATACCGACGG GGAAAGGCGACCTGTGGTGATGTCGACGTGCTCATCACTCACCCAGATGGCCGGTCCCACCGGGGTATCT TCAGCCGCCTCCTTGACAGTCTTCGGCAGGAAGGGTTCCTCACAGATGACTTGGTGAGCCAAGAGGAGAA TGGTCAGCAACAGAAGTACTTGGGGGTGTGCCGGCTCCCAGGGCCAGGGCGGCGGCACCGGCGCCTGGAC ATCATCGTGGTGCCCTATAGCGAGTTTGCCTGTGCCCTGCTCTACTTCACCGGCTCTGCACACTTCAACC GCTCCATGCGAGCCCTGGCCAAAACCAAGGGCATGAGTCTGTCAGAACATGCCCTCAGCACTGCTGTGGT CCGGAACACCCATGGCTGCAAGGTGGGGCCTGGCCGAGTGCTGCCCACTCCCACTGAGAAGGATGTCTTC AGGCTCTTAGGCCTCCCCTACCGAGAACCTGCTGAGCGGGACTGG ACGCGTACGCGGCCGCTCGAGCAGAAACTCATCTCAGAAGAGGATCTGGCAGCAAATGATATCCTGGATT ACAAGGATGACGACGATAAGGTTTAA Protein Sequence: >RC230298 protein sequence Red=Cloning site Green=Tags(s) MDPRGILKAFPKRQKIHADASSKVLAKIPRREEGEEAEEWLSSLRAHVVRTGIGRARAELFEKQIVQHGG QLCPAQGPGVTHIVVDEGMDYERALRLLRLPQLPPGAQLVKSAWLSLCLQERRLVDVAGFSIFIPSRYLD HPQPSKAEQDASIPPGTHEALLQTALSPPPPPTRPVSPPQKAKEAPNTQAQPISDDEASDGEETQVSAAD LEALISGHYPTSLEGDCEPSPAPAVLDKWVCAQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYA KAINALKSFHKPVTSYQGACSIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQ MWYQQGFRSLEDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRR GKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLPGPGRRHRRLD IIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNTHGCKVGPGRVLPTPTEKDVF RLLGLPYREPAERDW TRTRPLEQKLISEEDLAANDILDYKDDDDKV Chromatograms: https://cdn.origene.com/chromatograms/mk6530_d06.zip Restriction Sites: SgfI-MluI This product is to be used for laboratory only. Not for diagnostic or therapeutic use. ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 2 / 4 DNA Polymerase lambda (POLL) (NM_001174084) Human Tagged ORF Clone – RC230298 Cloning Scheme: Plasmid Map: ACCN: NM_001174084 ORF Size: 1725 bp This product is to be used for laboratory only. Not for diagnostic or therapeutic use. ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 3 / 4 DNA Polymerase lambda (POLL) (NM_001174084) Human Tagged ORF Clone – RC230298 OTI Disclaimer: Due to the inherent nature of this plasmid, standard methods to replicate additional amounts of DNA in E. coli are highly likely to result in mutations and/or rearrangements. Therefore, OriGene does not guarantee the capability to replicate this plasmid DNA. Additional amounts of DNA can be purchased from OriGene with batch-specific, full-sequence verification at a reduced cost. Please contact our customer care team at [email protected] or by calling 301.340.3188 option 3 for pricing and delivery. The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info OTI Annotation: This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. RefSeq: NM_001174084.1, NP_001167555.1 RefSeq Size: 2804 bp RefSeq ORF: 1728 bp Locus ID: 27343 UniProt ID: Q9UGP5 Protein Families: Druggable Genome Protein Pathways: Base excision repair, Non-homologous end-joining MW: 63.4 kDa Gene Summary: This gene encodes a DNA polymerase. DNA polymerases catalyze DNA-template-directed extension of the 3'-end of a DNA strand. This particular polymerase, which is a member of the X family of DNA polymerases, likely plays a role in non-homologous end joining and other DNA repair processes. Alternatively spliced transcript variants have been described. [provided by RefSeq, Mar 2010] This product is to be used for laboratory only. Not for diagnostic or therapeutic use. ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 4 / 4.
Load more

Recommended publications
  • Biochemical Studies of Dna Polymerase Theta A
    BIOCHEMICAL STUDIES OF DNA POLYMERASE THETA A Dissertation Submitted to the Temple University Graduate Board In Partial Fulfillment of the Requirements for the Degree DOCTOR OF PHILOSOPHY by Ahmet Y Ozdemir May 2019 Examining Committee Members: Richard T Pomerantz,PhD, Advisory Chair, Fels Institute for Cancer Research and Molecular Biology & Medical Genetics and Molecular Biochemistry Xavier Graña-Amat,PhD, Fels Institute for Cancer Research and Molecular Biology & Medical Genetics and Molecular Biochemistry Tomasz Skorski, MD, PhD, DSc, Fels Institute for Cancer Research and Molecular Biology & Microbiology and Immunology Italo Tempera, PhD, Fels Institute for Cancer Research and Molecular Biology & Microbiology and Immunology Alexander Mazin, PhD, External Member, Biochemistry & Molecular Biology, Drexel University © Copyright 2019 by Ahmet Y Ozdemir All Rights Reserved ii ABSTRACT POLQ is a unique multifunctional replication and repair gene that encodes a multidomain protein with a N-terminal superfamily 2 helicase and a C-terminal A-family polymerase. Although the function of the polymerase domain has been investigated, little is understood regarding the helicase domain. Multiple studies have reported that polymerase θ-helicase (Polθ-helicase) is unable to unwind DNA. However, it exhibits ATPase activity that is stimulated by single-stranded DNA, which presents a biochemical conundrum. In contrast to previous reports, we demonstrate that Polθ-helicase (residues 1– 894) efficiently unwinds DNA with 3'–5' polarity, including DNA with 3' or 5' overhangs, blunt- ended DNA, and replication forks. Polθ-helicase also efficiently unwinds RNA- DNA hybrids and exhibits a preference for unwinding the lagging strand at replication forks, similar to related HELQ helicase. Finally, we find that Polθ-helicase can facilitate strand displacement synthesis by Polθ-polymerase, suggesting a plausible function for the helicase domain.
    [Show full text]
  • Interactions of Dna Polymerase Theta and Ku70/80 With
    INTERACTIONS OF DNA POLYMERASE THETA AND KU70/80 WITH OXIDATIVE DNA DAMAGE by Daniel Laverty A dissertation submitted to Johns Hopkins University in conformity with the requirements for the degree of Doctor of Philosophy Baltimore, MD Submitted June 2018 Abstract Oxidized abasic sites (L, C4-AP, and DOB) are formed by ionizing radiation, reactive oxygen species, and some chemotherapeutics. Like abasic sites (AP), these lesions are cytotoxic and mutagenic and must be repaired, primarily by base excision repair (BER). If left unrepaired, abasic lesions stall replication and induce mutations. Repair of oxidized abasic lesions exhibits unique challenges, however. C4-AP and DOB inactivate the lyase activity of the repair enzymes DNA polymerase β and λ. Recently, several other enzymes were shown to possess lyase activity, allowing them to excise abasic lesions. Among these are DNA polymerase θ (Pol θ) and Ku70/80 (Ku). As Pol θ promotes resistance to cancer therapies which form oxidized abasic sites, the repair and replication of these lesions by Pol θ is potentially important. Ku is a core factor for non-homologous end-joining and removes AP from double strand breaks (DSBs). The interaction of Ku with oxidized abasic sites near DSB termini is potentially important for the response to ionizing radiation, which is used as a cancer treatment. Synthetic oligonucleotides containing abasic and oxidized abasic sites were prepared, and their repair or replication by Pol θ was analyzed. Pol θ bypasses C4-AP and L with reduced efficiency relative to AP and has a strong propensity to induce frameshift mutations during bypass of AP, C4-AP, L, and the oxidized nucleobase, thymidine glycol.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2014/0079836A1 Mcdaniel (43) Pub
    US 20140079836A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2014/0079836A1 McDaniel (43) Pub. Date: Mar. 20, 2014 (54) METHODS AND COMPOSITIONS FOR (52) U.S. Cl. ALTERING HEALTH, WELLBEING AND CPC ............... A61K 36/74 (2013.01); A61 K3I/122 LIFESPAN (2013.01) USPC ............. 424/777; 514/690: 435/375; 506/16; (71) Applicant: LifeSpan Extension, LLC, Virginia 435/6.12 Beach, VA (US) (72) Inventor: David H. McDaniel, Virginia Beach, VA (57) ABSTRACT (US) Described herein are the results of comprehensive genetic (73) Assignee: LifeSpan Extension, LLC expression and other molecular analysis p the effect s anti oxidants on biological systems, including specifically differ (21) Appl. No.: 14/084,553 ent human cells. Based on these analyses, methods and com (22) Filed: Nov. 19, 2013 positions are described for modifying or influencing the lifespan of cells, tissues, organs, and organisms. In various Related U.S. Application Data embodiments, there are provided methods for modulating the activity of the gene maintenance process in order to influence (60) Continuation of application No. 13/898.307, filed on the length and/or structural integrity of the telomere in living May 20, 2013, which is a division of application No. cells, as well as methods for modulating the rate/efficiency of 12/629,040, filed on Dec. 1, 2009, now abandoned. the cellular respiration provided by the mitochondria, mito (60) Provisional application No. 61/118,945, filed on Dec. chondrial biogenesis, and maintenance of the mitochondrial 1, 2008. membrane potential. Exemplary lifespan altering compounds include natural and synthetic antioxidants, such as plant anti Publication Classification oxidant and polyphenol compounds derived from coffee cherry, tea, berry, and so forth, including but not limited to (51) Int.
    [Show full text]
  • The Central Role of Acetyl-Coa in Plant Metabolism, As Examined Through Studies of ATP Citrate Lyase and the Bio1 Mutant of Arabidopsis Elizabeth K
    Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 2004 The central role of acetyl-CoA in plant metabolism, as examined through studies of ATP citrate lyase and the bio1 mutant of Arabidopsis Elizabeth K. Winters Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Genetics Commons, Molecular Biology Commons, and the Plant Sciences Commons Recommended Citation Winters, Elizabeth K., "The ec ntral role of acetyl-CoA in plant metabolism, as examined through studies of ATP citrate lyase and the bio1 mutant of Arabidopsis " (2004). Retrospective Theses and Dissertations. 1203. https://lib.dr.iastate.edu/rtd/1203 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]. The central role of acetyl-CoA in plant metabolism, as examined through studies of ATP citrate lyase and the biol mutant of Arabidopsis by Elizabeth K. Winters A dissertation submitted to the graduate faculty in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Major: Plant Physiology Program of Study Committee: Eve Syrkin Wurtele, Co-major Professor Basil J. Nikolau, Co-major Professor Thomas Baum James T. Colbert David J. Oliver Mark Westgate Iowa State University Ames, Iowa 2004 UMI Number: 3158378 INFORMATION TO USERS The quality of this reproduction is dependent upon the quality of the copy submitted.
    [Show full text]
  • The Dark Side of UV-Induced DNA Lesion Repair
    G C A T T A C G G C A T genes Review The Dark Side of UV-Induced DNA Lesion Repair Wojciech Strzałka 1, Piotr Zgłobicki 1, Ewa Kowalska 1, Aneta Ba˙zant 1, Dariusz Dziga 2 and Agnieszka Katarzyna Bana´s 1,* 1 Department of Plant Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland; [email protected] (W.S.); [email protected] (P.Z.); [email protected] (E.K.); [email protected] (A.B.) 2 Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland; [email protected] * Correspondence: [email protected]; Tel.: +48-12-664-6410 Received: 27 October 2020; Accepted: 29 November 2020; Published: 2 December 2020 Abstract: In their life cycle, plants are exposed to various unfavorable environmental factors including ultraviolet (UV) radiation emitted by the Sun. UV-A and UV-B, which are partially absorbed by the ozone layer, reach the surface of the Earth causing harmful effects among the others on plant genetic material. The energy of UV light is sufficient to induce mutations in DNA. Some examples of DNA damage induced by UV are pyrimidine dimers, oxidized nucleotides as well as single and double-strand breaks. When exposed to light, plants can repair major UV-induced DNA lesions, i.e., pyrimidine dimers using photoreactivation. However, this highly efficient light-dependent DNA repair system is ineffective in dim light or at night. Moreover, it is helpless when it comes to the repair of DNA lesions other than pyrimidine dimers.
    [Show full text]
  • Wo 2010/065567 A2
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date 10 June 2010 (10.06.2010) WO 2010/065567 A2 (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every A61K 36/889 (2006.01) A61K 31/16 (2006.01) kind of national protection available): AE, AG, AL, AM, A61K 36/736 (2006.01) A61K 31/05 (2006.01) AO, AT, AU, AZ, BA, BB, BG, BH, BR, BW, BY, BZ, A61K 31/166 (2006.01) A61P 5/00 (2006.01) CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (21) International Application Number: HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, PCT/US2009/066294 KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, (22) International Filing Date: ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, 1 December 2009 (01 .12.2009) NO, NZ, OM, PE, PG, PH, PL, PT, RO, RS, RU, SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TJ, TM, TN, TR, TT, (25) Filing Language: English TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (26) Publication Language: English (84) Designated States (unless otherwise indicated, for every (30) Priority Data: kind of regional protection available): ARIPO (BW, GH, 61/1 18,945 1 December 2008 (01 .12.2008) US GM, KE, LS, MW, MZ, NA, SD, SL, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, MD, RU, TJ, (71) Applicant (for all designated States except US): LIFES¬ TM), European (AT, BE, BG, CH, CY, CZ, DE, DK, EE, PAN EXTENSION LLC [US/US]; 933 First Colonial ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, Road, Suite 114, Virginia Beach, VA 23454 (US).
    [Show full text]
  • Investigation of Dna Damage Response at Interstitial Telomeric Sites in Chinese Hamster Cell Lines
    INVESTIGATION OF DNA DAMAGE RESPONSE AT INTERSTITIAL TELOMERIC SITES IN CHINESE HAMSTER CELL LINES A thesis submitted for a degree of Doctor of Philosophy by Sheila Matta Castillo College of Health and Life Sciences Department of Life Sciences Brunel University July 2018 Declaration I hereby declare that the research presented in this thesis is my own work, except where otherwise specified, and has not been submitted for any other degree. Sheila Matta July 2018 2 Abstract Telomeres are highly specialised structures that protect the ends of linear chromosomes from damage. Telomeric DNA consists of tandem repeats of a specific sequence (TTAGGG)n that varies in length depending on the species. Two telomere maintenance mechanisms are known to exist. Telomerase, an enzyme that synthesises new tandem repeats onto the end of linear chromosome and ALT (Alternative Lengthening of Chromosomes), which uses recombination to lengthen telomeric sequences. In some mammalian species, both mechanisms are known to co-exist. Telomeric DNA that is found at non-telomere sites are referred to as interstitial telomeric sequences (ITS). Several studies have shown that ITS sites in the Chinese hamster are preferred sites for radiation and spontaneous chromosomal damage. Once damage occurs, repair mechanisms such as HR (homologous recombination) and NHEJ (non-homologous end joined) are activated. However, the contribution to this repair by telomerase and ALT is unknown. The aim of this work therefore is to investigate the contribution that above mention mechanisms (HR, NHEJ, telomerase and ALT) make to ITS repair in Chinese hamster cells. Classical cytogenetic techniques such as Giemsa staining, chromosomal aberration analysis, FISH (Fluorescence in situ hybridazation, IHC (Immunohistochemistry), TIF (Telomere dysfunction induced foci), were used to quantify chromosomal damage after IR (ionising radiation) treatment of normal and repair deficient (HR and NHEJ) Chinese 3 hamster cell lines.
    [Show full text]
  • Small‐Molecule Inhibitors of Dna Polymerase Function
    SMALL‐MOLECULE INHIBITORS OF DNA POLYMERASE FUNCTION DISSERTATION zur Erlangung des Akademischen Grades des Doktors der Naturwissenschaften (Dr. rer. nat.) vorgelegt von Tobias Strittmatter aus Küssaberg‐Kadelburg an der Universität Konstanz Mathematisch‐Naturwissenschaftliche Sektion Fachbereich Chemie 2014 Tag der mündlichen Prüfung: 05. Dezember 2014 Prüfungsvorsitz: Prof. Dr. Gerhard Müller 1. Referent: Prof. Dr. Andreas Marx 2. Referent: Prof. Dr. Thomas U. Mayer Konstanzer Online-Publikations-System (KOPS) URL: http://nbn-resolving.de/urn:nbn:de:bsz:352-0-274434 „Meinen Eltern” Danksagung Die vorliegende Arbeit entstand in der Zeit von November 2009 bis August 2014 in der Arbeitsgruppe von Prof. Dr. Andreas Marx am Lehrstuhl für Organische und Zelluläre Chemie am Fachbereich Chemie der Universität Konstanz. Nach diesem Zeitraum geprägt von intensiver Forschungsarbeit liegt nun meine Dissertation vor und ein weiteres Kapitel meiner beruflichen Karriere kann nun erfolgreich abgeschlossen werden. Aus diesem Grund ist es jetzt auch an der Zeit, mich bei all denen zu bedanken, die mich während dieser spannenden Zeit begleitet, unterstützt und gefördert haben. Meinem Doktorvater Prof. Dr. Andreas Marx danke ich ganz herzlich für die Überlassung der sehr interessanten und interdisziplinären Themenstellung, sowie für das in mich gesetzte Vertrauen, welches mir viel Raum für die selbstständige Bearbeitung und kreative Gestaltung des Themas erlaubte. Ihm, wie auch den weiteren Mitgliedern meines „Thesis Committee“, Prof. Dr. Thomas Mayer und Herrn Prof. Dr. Michael Berthold, danke ich zudem für die anregenden wissenschaftlichen Diskussionen und die geleisteten Hilfestellungen. Prof. Dr. Thomas Mayer danke ich außerdem für die Übernahme des Zweitgutachtens und Herrn Prof. Dr. Gerhard Müller für die Übernahme des Prüfungsvorsitzes.
    [Show full text]
  • Phosphorylation Regulates Human Pol Stability and Damage Bypass Throughout the Cell Cycle
    Published online 24 July 2017 Nucleic Acids Research, 2017, Vol. 45, No. 16 9441–9454 doi: 10.1093/nar/gkx619 Phosphorylation regulates human pol␩ stability and damage bypass throughout the cell cycle Federica Bertoletti1,†, Valentina Cea1,†, Chih-Chao Liang2, Taiba Lanati1, Antonio Maffia1,3, Mario D.M. Avarello1, Lina Cipolla1, Alan R. Lehmann4, Martin A. Cohn2 and Simone Sabbioneda1,* 1Istituto di Genetica Molecolare-CNR, 27100, Pavia, Italy, 2Department of Biochemistry, University of Oxford, OX1 3QU, Oxford, UK, 3Dipartimento di Biologia e Biotecnologie ‘Lazzaro Spallanzani’, Universita` degli Studi di Pavia, 27100, Pavia, Italy and 4Genome Damage and Stability Centre, University of Sussex, BN1 9RQ, Brighton, UK Received April 26, 2017; Revised July 05, 2017; Editorial Decision July 06, 2017; Accepted July 06, 2017 ABSTRACT a distorted template (1). The majority of TLS polymerases belong to the Y family and include pol␩, pol␫, pol␬ and DNA translesion synthesis (TLS) is a crucial dam- Rev1 along with the B-family member pol␨ (1). The Y fam- age tolerance pathway that oversees the completion ily polymerases can bypass the damage by virtue of a more of DNA replication in the presence of DNA damage. open catalytic site that can accommodate DNA lesions, TLS polymerases are capable of bypassing a dis- such as cyclobutane pyrimidine dimers (CPDs), created by torted template but they are generally considered in- exposure to UV light (2). As a trade-off, this wider catalytic accurate and they need to be tightly regulated. We site is prone to errors during nucleotide incorporation, so have previously shown that pol␩ is phosphorylated TLS polymerases need to be tightly controlled.
    [Show full text]
  • CATALOG of ANTIBODIES for 293T Cells Using NB100-214
    Western blot analysis of CATALOG OF ANTIBODIES FOR 293T cells using NB100-214. Species: Hu Applications: IP, WB DNA REPAIR Immuno- fluorescent staining of SiHa cells using NB100-182. Species: Hu, Mu Applications: IF, IHC-P, IP, WB Western blot analysis of FANCG transfected COS1 cell lysate using NB100-2566. Species: Hu Applications: WB Western blot analysis of: (1) MCF-7 lysate (2) HeLa lysate (3) 293 lysate and (4) SKOV3 lysate using NB100-416. Species: Hu Applications: WB, IP Western blot analysis of 293T whole cell lysate using NB100-472. Species: Hu Applications: IP, WB Table of Contents DNA Repair Non-Homologous End Joining ...2 DNA repair refers to a collection of processes by which a cell identifies and Homologous Recombination .. 3-4 corrects damage to the DNA molecules that encode its genome. In human Checkpoint Signaling & Double Strand Break Repair .. 5-7 cells, both normal metabolic activities and environmental factors (such as UV Base Excision Repair ..................8 light) can cause DNA damage, resulting in up to half a million individual Nucleotide Excision ...................9 molecular lesions per cell per day. Many of these lesions cause structural Mismatch Repair .................... 10 damage to the DNA molecule and can alter or eliminate the cell’s ability DNA Polymerase .................... 11 to transcribe the gene that the affected DNA encodes. Other lesions induce Direct Reversal of Damage ..... 11 potentially harmful mutations in the cell’s genome, which affect the survival Longevity ............................... 12 of its daughter cells after it undergoes mitosis. Consequently, the DNA repair Syndromes Linked to process must be constantly active so that it can respond quickly to any damage DNA Repair Defects ..............
    [Show full text]
  • Open Mohammad Almishwat MS 2013
    The Pennsylvania State University The Graduate School Eberly College of Science TIME-RESOLVED X-RAY CRYSTALLOGRAPHY OF DNA POLYMERASES: A PLATFORM FOR STUDIES IN STRUCTURAL AND MECHANISTIC ENZYMOLOGY A Thesis in Biochemistry, Microbiology, and Molecular Biology by Mohammad A. Almishwat © 2013 Mohammad A. Almishwat Submitted in Partial Fulfillment of the Requirements for the Degree of Master of Science August 2013 The thesis of Mohammad A. Almishwat was reviewed and approved* by the following: Katsuhiko Murakami Associate Professor of Biochemistry and Molecular Biology Thesis Co-Adviser J. Gregory Ferry Stanley Person Professor of Biochemistry and Molecular Biology Thesis Co-Adviser Susan Hafenstein Assistant Professor of Medicine, Microbiology and Immunology Paul Babitzke Professor of Biochemistry and Molecular Biology Co-Director of Graduate Studies *Signatures are on file in the Graduate School. ii Abstract DNA-dependent DNA polymerase is the enzyme responsible for carrying out DNA replication. DNA polymerase regulates the faithful transmission of an organism’s genetic material, and performs various tasks involved in correcting errors that occur during the process of DNA replication. Extensive genetic and biochemical research has been done to characterize the general mechanism of DNA replication and the factors that govern its fidelity, and yet the mechanistic details of this fidelity, how a correct deoxynucleotide is selected for by the enzyme for incorporation, and an incorrect one is excluded, is yet to be determined. Structural studies of various DNA polymerases and their complexes with DNA have provided a great deal of insight into how catalysis in nucleotide incorporation occurs, and has also provided empirical models of how fidelity is brought about in these enzymes during DNA replication.
    [Show full text]
  • Ep 2336315 A2
    (19) TZZ ¥¥¥_ T (11) EP 2 336 315 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 22.06.2011 Bulletin 2011/25 C12N 15/10 (2006.01) C12Q 1/68 (2006.01) C40B 40/06 (2006.01) C40B 50/06 (2006.01) (21) Application number: 10192717.6 (22) Date of filing: 01.12.2006 (84) Designated Contracting States: • Husemoen, Birgitte Nystrup AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 2500 Valby (DK) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Dolberg, Johannes SK TR 1674 Copenhagen V (DK) Designated Extension States: • Jensen, Kim Birkebæk AL BA HR MK RS 2610 Rødovre (DK) • Petersen, Lene (30) Priority: 01.12.2005 DK 200501704 2100 Copenhagen Ø (DK) 02.12.2005 US 741490 P • Nørregaard-Madsen, Mads 3460 Birkerød (DK) (62) Document number(s) of the earlier application(s) in • Godskesen, Michael Anders accordance with Art. 76 EPC: 2950 Vedbæk (DK) 06818144.5 / 1 957 644 • Glad, Sanne Schrøder 2750 Ballerup (DK) (71) Applicant: Nuevolution A/S • Neve, Søren 2100 Copenhagen (DK) 2800 Lyngby (DK) • Thisted, Thomas (72) Inventors: 3600 Frederikssund (DK) • Franch, Thomas • Kronberg, Tine Titilola Akinleminu 3070 Snekkersten (DK) 3500 Værløse (DK) • Lundorf, Mikkel Dybro • Sams, Christian 4000 Roskilde (DK) 3500 Værløse (DK) • Jakobsen, Soren Nyboe • Felding, Jakob 2000 Frederiksberg (DK) 2920 Charlottenlund (DK) • Olsen, Eva Kampmann • Freskgård, Per-Ola 2730 Herlev (DK) 603 79 Norrkörping (SE) • Andersen, Anne Lee • Gouliaev, Alex Haahr 4100 Ringsted (DK) 3670 Veksø Sjælland (DK) • Holtmann, Anette • Pedersen, Henrik 2750 Ballerup (DK) 3540 Lynge (DK) • Hansen, Anders Holm 2400 Copenhagen NV (DK) (74) Representative: Aamand, Jesper L.
    [Show full text]