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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 mail@szabo-scandic.com • Mindermengenzuschlag www.szabo-scandic.com • Trockeneiszuschlag • Gefahrgutzuschlag linkedin.com/company/szaboscandic • Expressversand facebook.com/szaboscandic TNKS2 Antibody, HRP conjugated Product Code CSB-PA867136LB01HU Abbreviation Tankyrase-2 Storage Upon receipt, store at -20°C or -80°C. Avoid repeated freeze. Uniprot No. Q9H2K2 Immunogen Recombinant Human Tankyrase-2 protein (1-246AA) Raised In Rabbit Species Reactivity Human Tested Applications ELISA Relevance Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP- ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Stimulates 26S proteasome activity. Form Liquid Conjugate HRP Storage Buffer Preservative: 0.03% Proclin 300 Constituents: 50% Glycerol, 0.01M PBS, PH 7.4 Purification Method >95%, Protein G purified Isotype IgG Clonality Polyclonal Alias Tankyrase-2 (TANK2) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin- like 6) (ARTD6) (Poly [ADP-ribose] polymerase 5B) (TNKS-2) (TRF1-interacting ankyrin-related ADP-ribose polymerase 2) (Tankyrase II) (Tankyrase-like protein) (Tankyrase-related protein), TNKS2, PARP5B TANK2 TNKL Species Homo sapiens (Human) Research Area Epigenetics and Nuclear Signaling Target Names TNKS2 1.

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Genetics of Familial Non-Medullary Thyroid Carcinoma (FNMTC)
cancers Review Genetics of Familial Non-Medullary Thyroid Carcinoma (FNMTC) Chiara Diquigiovanni * and Elena Bonora Unit of Medical Genetics, Department of Medical and Surgical Sciences, University of Bologna, 40138 Bologna, Italy; elena.bonora6@unibo.it * Correspondence: chiara.diquigiovanni@unibo.it; Tel.: +39-051-208-8418 Simple Summary: Non-medullary thyroid carcinoma (NMTC) originates from thyroid follicular epithelial cells and is considered familial when occurs in two or more first-degree relatives of the patient, in the absence of predisposing environmental factors. Familial NMTC (FNMTC) cases show a high genetic heterogeneity, thus impairing the identification of pivotal molecular changes. In the past years, linkage-based approaches identified several susceptibility loci and variants associated with NMTC risk, however only few genes have been identified. The advent of next-generation sequencing technologies has improved the discovery of new predisposing genes. In this review we report the most significant genes where variants predispose to FNMTC, with the perspective that the integration of these new molecular findings in the clinical data of patients might allow an early detection and tailored therapy of the disease, optimizing patient management. Abstract: Non-medullary thyroid carcinoma (NMTC) is the most frequent endocrine tumor and originates from the follicular epithelial cells of the thyroid. Familial NMTC (FNMTC) has been defined in pedigrees where two or more first-degree relatives of the patient present the disease in absence of other predisposing environmental factors. Compared to sporadic cases, FNMTCs are often multifocal, recurring more frequently and showing an early age at onset with a worse outcome. FNMTC cases Citation: Diquigiovanni, C.; Bonora, E.
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Rat Anti-TERF1 Monoclonal Antibody, Clone 683D (CABT-RM172) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Rat Anti-TERF1 monoclonal antibody, clone 683D (CABT-RM172) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Specificity Specifically detects murine Telomeric repeat-binding factor 1 (TRF1). Target TERF1 Immunogen His-tagged full-length recombinant mouse Telomeric repeat-binding factor 1 (TRF1). Isotype IgG1, κ Source/Host Rat Species Reactivity Mouse Clone 683D Purification Protein G purified Conjugate unconjugated Applications FC, ICC, IF, WB Molecular Weight ~51 kDa observed; 48.22 kDa calculated. Uncharacterized bands may be observed in some lysate(s). Format Liquid Size 100 μg, 25 μg Buffer 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl Preservative 0.05% sodium azide Storage Stable for 1 year at 2-8°C from date of receipt. Warnings Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals. 45-1 Ramsey Road, Shirley, NY 11967, USA Email: info@creative-diagnostics.com Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved BACKGROUND Introduction Telomeric repeat-binding factor 1 is encoded by the Terf1 gene in murine species. TRF1 is a component of the shelterin complex that is involved in the regulation of telomere length and protection. It binds to telomeric DNA as a homodimer and protects telomeres.
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The Genetics and Clinical Manifestations of Telomere Biology Disorders Sharon A
REVIEW The genetics and clinical manifestations of telomere biology disorders Sharon A. Savage, MD1, and Alison A. Bertuch, MD, PhD2 3 Abstract: Telomere biology disorders are a complex set of illnesses meric sequence is lost with each round of DNA replication. defined by the presence of very short telomeres. Individuals with classic Consequently, telomeres shorten with aging. In peripheral dyskeratosis congenita have the most severe phenotype, characterized blood leukocytes, the cells most extensively studied, the rate 4 by the triad of nail dystrophy, abnormal skin pigmentation, and oral of attrition is greatest during the first year of life. Thereafter, leukoplakia. More significantly, these individuals are at very high risk telomeres shorten more gradually. When the extent of telo- of bone marrow failure, cancer, and pulmonary fibrosis. A mutation in meric DNA loss exceeds a critical threshold, a robust anti- one of six different telomere biology genes can be identified in 50–60% proliferative signal is triggered, leading to cellular senes- of these individuals. DKC1, TERC, TERT, NOP10, and NHP2 encode cence or apoptosis. Thus, telomere attrition is thought to 1 components of telomerase or a telomerase-associated factor and TINF2, contribute to aging phenotypes. 5 a telomeric protein. Progressively shorter telomeres are inherited from With the 1985 discovery of telomerase, the enzyme that ex- generation to generation in autosomal dominant dyskeratosis congenita, tends telomeric nucleotide repeats, there has been rapid progress resulting in disease anticipation. Up to 10% of individuals with apparently both in our understanding of basic telomere biology and the con- acquired aplastic anemia or idiopathic pulmonary fibrosis also have short nection of telomere biology to human disease.
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Telomere-Regulating Genes and the Telomere Interactome in Familial Cancers
Author Manuscript Published OnlineFirst on September 22, 2014; DOI: 10.1158/1541-7786.MCR-14-0305 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. Telomere-regulating Genes and the Telomere Interactome in Familial Cancers Authors: Carla Daniela Robles-Espinoza1, Martin del Castillo Velasco-Herrera1, Nicholas K. Hayward2 and David J. Adams1 Affiliations: 1Experimental Cancer Genetics, Wellcome Trust Sanger Institute, Hinxton, UK 2Oncogenomics Laboratory, QIMR Berghofer Medical Research Institute, Herston, Brisbane, Queensland, Australia Corresponding author: Carla Daniela Robles-Espinoza, Experimental Cancer Genetics, Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambs., UK. CB10 1SA. Telephone: +44 1223 834244, Fax +44 1223 494919, E-mail: cdre@sanger.ac.uk Financial support: C.D.R.-E., M.d.C.V.H. and D.J.A. were supported by Cancer Research UK and the Wellcome Trust (WT098051). C.D.R.-E. was also supported by the Consejo Nacional de Ciencia y Tecnología of Mexico. N.K.H. was supported by a fellowship from the National Health and Medical Research Council of Australia (NHMRC). Running title: Telomere-regulating genes in familial cancers Keywords: Telomeres, telomerase, shelterin, germline variation, cancer predisposition Conflicts of interest: The authors declare no conflicts of interest. Word count: 6,362 (including figure legends) Number of figures and tables: 2 figures in main text, 3 tables in supplementary material 1 Downloaded from mcr.aacrjournals.org on September 29, 2021. © 2014 American Association for Cancer Research. Author Manuscript Published OnlineFirst on September 22, 2014; DOI: 10.1158/1541-7786.MCR-14-0305 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited.
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Structural and Functional Consequences of a Disease Mutation in the Telomere Protein TPP1
Structural and functional consequences of a disease mutation in the telomere protein TPP1 Kamlesh Bishta,1, Eric M. Smitha,b,1, Valerie M. Tesmera, and Jayakrishnan Nandakumara,b,2 aDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109; and bProgram in Chemical Biology, University of Michigan, Ann Arbor, MI 48109 Edited by Joachim Lingner, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland, and accepted by Editorial Board Member Dinshaw J. Patel September 29, 2016 (received for review April 8, 2016) Telomerase replicates chromosome ends to facilitate continued cell The discovery of the TEL patch of TPP1 prompted the pre- division. Mutations that compromise telomerase function result in diction that this region could be a hotspot for mutations that stem cell failure diseases, such as dyskeratosis congenita (DC). One cause telomerase-deficiency diseases, such as DC. We recently such mutation (K170Δ), residing in the telomerase-recruitment factor reported a case of a severe variant of DC, Hoyeraal–Hreidarsson TPP1, provides an excellent opportunity to structurally, biochemi- syndrome (23), in which the proband was heterozygous for a cally, and genetically dissect the mechanism of such diseases. We deletion of a single amino acid of the TPP1 protein, namely lysine ACD show through site-directed mutagenesis and X-ray crystallography 170 (K170) (24). Our study placed the gene coding for TPP1 DKC1 TERC TERT that this TPP1 disease mutation deforms the conformation of two protein on a list with 10 other genes ( , , , RTEL1 TINF2 CTC1 NOP10 NHP2 WRAP53 PARN critical amino acids of the TEL [TPP1’s glutamate (E) and leucine-rich , , , , , ,and ) that are found mutated in DC and other telomere-related dis- (L)] patch, the surface of TPP1 that binds telomerase.
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(AS) Alternative Splicing Variants and TERF2 in Osteosarcoma
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Supplemental Table 1 Telomere Pathway Genes Evaluated in the Current Study
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Telomere Length Regulation in Mice Is Linked to a Novel Chromosome Locus
Proc. Natl. Acad. Sci. USA Vol. 95, pp. 8648–8653, July 1998 Cell Biology Telomere length regulation in mice is linked to a novel chromosome locus LINGXIANG ZHU*†,KAREN S. HATHCOCK*‡§,PRAKASH HANDE¶,PETER M. LANSDORP¶,MICHAEL F. SELDIN†, i AND RICHARD J. HODES‡ †Rowe Program in Genetics, Departments of Biological Chemistry and Medicine University of California, Davis, Davis, CA 95616; ‡Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892; ¶Terry Fox Laboratory for HematologyyOncology, British Columbia Cancer Research Center, 601 West 10th Avenue, Vancouver, BC V5Z 1L3, Canada; and iNational Institute on Aging, National Institutes of Health, Bethesda, MD 20892 Edited by Irving L. Weissman, Stanford University School of Medicine, Stanford, CA, and approved, May 20, 1998 (received for review September 15, 1997) ABSTRACT Little is known about the mechanisms that housed in the animal facility at PerImmune, Rockville, MD or regulate species-specific telomere length, particularly in mam- Bioqual, Rockville, MD. malian species. The genetic regulation of telomere length was Telomere Length Analysis. Single cell suspensions of spleen therefore investigated by using two inter-fertile species of were generated by conventional methods. Single cell suspen- mice, which differ in their telomere length. Mus musculus sions of liver were generated by incubating minced livers with (telomere length >25 kb) and Mus spretus (telomere length collagenase, type IV, (2 mgyml; Sigma) for 30 min at 37°C. 5–15 kb) were used to generate F1 crosses and reciprocal After depleting red blood cells, cell suspensions were mixed backcrosses, which were then analyzed for regulation of with an equal volume of 1.2% Incert Agarose (FMC) to make telomere length.
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