Mo25α/CAB39 (C49D8) Rabbit Mab A
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
FK506-Binding Protein 12.6/1B, a Negative Regulator of [Ca2+], Rescues Memory and Restores Genomic Regulation in the Hippocampus of Aging Rats
This Accepted Manuscript has not been copyedited and formatted. The final version may differ from this version. A link to any extended data will be provided when the final version is posted online. Research Articles: Neurobiology of Disease FK506-Binding Protein 12.6/1b, a negative regulator of [Ca2+], rescues memory and restores genomic regulation in the hippocampus of aging rats John C. Gant1, Eric M. Blalock1, Kuey-Chu Chen1, Inga Kadish2, Olivier Thibault1, Nada M. Porter1 and Philip W. Landfield1 1Department of Pharmacology & Nutritional Sciences, University of Kentucky, Lexington, KY 40536 2Department of Cell, Developmental and Integrative Biology, University of Alabama at Birmingham, Birmingham, AL 35294 DOI: 10.1523/JNEUROSCI.2234-17.2017 Received: 7 August 2017 Revised: 10 October 2017 Accepted: 24 November 2017 Published: 18 December 2017 Author contributions: J.C.G. and P.W.L. designed research; J.C.G., E.M.B., K.-c.C., and I.K. performed research; J.C.G., E.M.B., K.-c.C., I.K., and P.W.L. analyzed data; J.C.G., E.M.B., O.T., N.M.P., and P.W.L. wrote the paper. Conflict of Interest: The authors declare no competing financial interests. NIH grants AG004542, AG033649, AG052050, AG037868 and McAlpine Foundation for Neuroscience Research Corresponding author: Philip W. Landfield, [email protected], Department of Pharmacology & Nutritional Sciences, University of Kentucky, 800 Rose Street, UKMC MS 307, Lexington, KY 40536 Cite as: J. Neurosci ; 10.1523/JNEUROSCI.2234-17.2017 Alerts: Sign up at www.jneurosci.org/cgi/alerts to receive customized email alerts when the fully formatted version of this article is published. -
Effects of Rapamycin on Social Interaction Deficits and Gene
Kotajima-Murakami et al. Molecular Brain (2019) 12:3 https://doi.org/10.1186/s13041-018-0423-2 RESEARCH Open Access Effects of rapamycin on social interaction deficits and gene expression in mice exposed to valproic acid in utero Hiroko Kotajima-Murakami1,2, Toshiyuki Kobayashi3, Hirofumi Kashii1,4, Atsushi Sato1,5, Yoko Hagino1, Miho Tanaka1,6, Yasumasa Nishito7, Yukio Takamatsu7, Shigeo Uchino1,2 and Kazutaka Ikeda1* Abstract The mammalian target of rapamycin (mTOR) signaling pathway plays a crucial role in cell metabolism, growth, and proliferation. The overactivation of mTOR has been implicated in the pathogenesis of syndromic autism spectrum disorder (ASD), such as tuberous sclerosis complex (TSC). Treatment with the mTOR inhibitor rapamycin improved social interaction deficits in mouse models of TSC. Prenatal exposure to valproic acid (VPA) increases the incidence of ASD. Rodent pups that are exposed to VPA in utero have been used as an animal model of ASD. Activation of the mTOR signaling pathway was recently observed in rodents that were exposed to VPA in utero, and rapamycin ameliorated social interaction deficits. The present study investigated the effect of rapamycin on social interaction deficits in both adolescence and adulthood, and gene expressions in mice that were exposed to VPA in utero. We subcutaneously injected 600 mg/kg VPA in pregnant mice on gestational day 12.5 and used the pups as a model of ASD. The pups were intraperitoneally injected with rapamycin or an equal volume of vehicle once daily for 2 consecutive days. The social interaction test was conducted in the offspring after the last rapamycin administration at 5–6 weeks of ages (adolescence) or 10–11 weeks of age (adulthood). -
WO 2014/135655 Al 12 September 2014 (12.09.2014) P O P C T
(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 WO 2014/135655 Al 12 September 2014 (12.09.2014) P O P C T (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every C12Q 1/68 (2006.01) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, (21) International Application Number: BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, PCT/EP2014/054384 DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (22) International Filing Date: HN, HR, HU, ID, IL, IN, IR, IS, JP, KE, KG, KN, KP, KR, 6 March 2014 (06.03.2014) KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, (25) Filing Language: English OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, (26) Publication Language: English SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, (30) Priority Data: ZW. 13305253.0 6 March 2013 (06.03.2013) EP (84) Designated States (unless otherwise indicated, for every (71) Applicants: INSTITUT CURIE [FR/FR]; 26 rue d'Ulm, kind of regional protection available): ARIPO (BW, GH, F-75248 Paris cedex 05 (FR). CENTRE NATIONAL DE GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, SZ, TZ, LA RECHERCHE SCIENTIFIQUE [FR/FR]; 3 rue UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, Michel Ange, F-75016 Paris (FR). -
View.50 the Small figure Shows the R2 Between the Two Snps Highlighted in Red
META-ANALYSIS www.jasn.org Common Variants in UMOD Associate with Urinary Uromodulin Levels: A Meta-Analysis † ‡ | †† Matthias Olden,* Tanguy Corre, § Caroline Hayward, Daniela Toniolo,¶** Sheila Ulivi, ††‡‡ ‡ Paolo Gasparini, Giorgio Pistis,¶ Shih-Jen Hwang,* Sven Bergmann, § Harry Campbell,§§ ††‡‡ ††‡‡ || Massimiliano Cocca,¶ Ilaria Gandin, Giorgia Girotto, Bob Glaudemans, | ††† Nicholas D. Hastie, Johannes Loffing,¶¶ Ozren Polasek,*** Luca Rampoldi,§§ Igor Rudan, ‡‡‡ ††‡‡ Cinzia Sala,¶ Michela Traglia,¶ Peter Vollenweider, Dragana Vuckovic, || || | ‡ ||| ||| Sonia Youhanna, §§§ Julien Weber, §§§ Alan F. Wright, Zoltán Kutalik, § Murielle Bochud, || Caroline S. Fox,*¶¶¶ and Olivier Devuyst §§§ *National Heart, Lung, and Blood Institute’s Framingham Heart Study, Framingham, Massachusetts; †Department of Genetic Epidemiology, Institute of Epidemiology and Preventive Medicine, University of Regensburg, Regensburg, Germany; ‡Department of Medical Genetics, University of Lausanne, Lausanne, Switzerland; §Swiss Institute of Bioinformatics, Lausanne, Switzerland; |Institute of Genetics and Molecular Medicine, Western General Hospital, and ‡‡‡Centre for Population Health Sciences, University of Edinburgh, Edinburgh, Scotland, United Kingdom; ¶Division of Genetics and Cell Biology, San Raffaele Scientific Institute, Milano, Italy; **Institute of Molecular Genetics, National Research Council, Pavia, Italy; ††Institute for Maternal and Child Health, Burlo Garofolo Pediatric Institute Trieste, Italy; ‡‡Department of Medical Sciences, University of -
AMPK Causes Cell Cycle Arrest in LKB1-Deficient Cells Via Activation of CAMKK2
Published OnlineFirst May 2, 2016; DOI: 10.1158/1541-7786.MCR-15-0479 Cell Cycle and Senescence Molecular Cancer Research AMPK Causes Cell Cycle Arrest in LKB1-Deficient Cells via Activation of CAMKK2 Sarah Fogarty, Fiona A. Ross, Diana Vara Ciruelos, Alexander Gray, Graeme J. Gowans, and D. Grahame Hardie Abstract The AMP-activated protein kinase (AMPK) is activated by also caused G1 arrest similar to that caused by expression of LKB1, phosphorylation at Thr172, either by the tumor suppressor kinase while expression of a dominant-negative AMPK mutant, or a þ LKB1 or by an alternate pathway involving the Ca2 /calmodulin- double knockout of both AMPK-a subunits, also prevented the dependent kinase, CAMKK2. Increases in AMP:ATP and ADP:ATP cell-cycle arrest caused by A23187. These mechanistic findings ratios, signifying energy deficit, promote allosteric activation and confirm that AMPK activation triggers cell-cycle arrest, and also net Thr172 phosphorylation mediated by LKB1, so that the LKB1– suggest that the rapid proliferation of LKB1-null tumor cells is due AMPK pathway acts as an energy sensor. Many tumor cells carry to lack of the restraining influence of AMPK. However, cell-cycle loss-of-function mutations in the STK11 gene encoding LKB1, but arrest can be restored by reexpressing LKB1 or a constitutively LKB1 reexpression in these cells causes cell-cycle arrest. Therefore, active CAMKK2, or by pharmacologic agents that increase intra- þ it was investigated as to whether arrest by LKB1 is caused by cellular Ca2 and thus activate endogenous CAMKK2. activation of AMPK or of one of the AMPK-related kinases, which are also dependent on LKB1 but are not activated by CAMKK2. -
Three Novel Mutations of STK11 Gene in Chinese Patients with Peutz
Tan et al. BMC Medical Genetics (2016) 17:77 DOI 10.1186/s12881-016-0339-6 CASE REPORT Open Access Three novel mutations of STK11 gene in Chinese patients with Peutz–Jeghers syndrome Hu Tan1, Libin Mei1, Yanru Huang1, Pu Yang1, Haoxian Li1, Ying Peng1, Chen Chen1,2, Xianda Wei1, Qian Pan1, Desheng Liang1* and Lingqian Wu1* Abstract Background: Peutz–Jeghers syndrome (PJS) is a rare autosomal dominant inherited disorder characterized by gastrointestinal (GI) hamartomatous polyps, mucocutaneous hyperpigmentation, and an increased risk of cancer. Mutations in the serine–threonine kinase 11 gene (SKT11) are the major cause of PJS. Case presentation: Blood samples were collected from six PJS families including eight patients. Mutation screening of STK11 gene was performed in these six families by Sanger sequencing and multiplex ligation- dependent probe amplification (MLPA) assay. Three novel mutations (c.721G > C, c.645_726del82, and del(exon2–5)) and three recurrent mutations (c.752G > A, c.545 T > C and del(exon1)) in STK11 were detected in six Chinese PJS families. Genotype-phenotype correlations suggested that truncating mutations trend to result in severe complications. Conclusion: These findings broaden the mutation spectrum of the STK11 gene and would help clinicians and genetic counselors provide better clinical surveillance for PJS patients, especially for ones carrying truncating mutation. Keywords: Peutz–Jeghers syndrome (PJS), Serine-threonine kinase 11 (STK11), Truncating mutation, Severe complication Background as a cause of PJS in 1998 [3, 4]. The gene, 23 kb in size, Peutz–Jeghers syndrome (PJS) is a rare autosomal dom- consists of nine coding exon and one non-coding exon inant inherited disorder characterized by gastrointestinal and encodes a 433-amino acid protein, which consists of (GI) hamartomatous polyps, mucocutaneous hyperpig- three domains: the N-terminal non-catalytic domain, the mentation of the lips, buccal mucosa, and digits. -
1 Novel Expression Signatures Identified by Transcriptional Analysis
ARD Online First, published on October 7, 2009 as 10.1136/ard.2009.108043 Ann Rheum Dis: first published as 10.1136/ard.2009.108043 on 7 October 2009. Downloaded from Novel expression signatures identified by transcriptional analysis of separated leukocyte subsets in SLE and vasculitis 1Paul A Lyons, 1Eoin F McKinney, 1Tim F Rayner, 1Alexander Hatton, 1Hayley B Woffendin, 1Maria Koukoulaki, 2Thomas C Freeman, 1David RW Jayne, 1Afzal N Chaudhry, and 1Kenneth GC Smith. 1Cambridge Institute for Medical Research and Department of Medicine, Addenbrooke’s Hospital, Hills Road, Cambridge, CB2 0XY, UK 2Roslin Institute, University of Edinburgh, Roslin, Midlothian, EH25 9PS, UK Correspondence should be addressed to Dr Paul Lyons or Prof Kenneth Smith, Department of Medicine, Cambridge Institute for Medical Research, Addenbrooke’s Hospital, Hills Road, Cambridge, CB2 0XY, UK. Telephone: +44 1223 762642, Fax: +44 1223 762640, E-mail: [email protected] or [email protected] Key words: Gene expression, autoimmune disease, SLE, vasculitis Word count: 2,906 The Corresponding Author has the right to grant on behalf of all authors and does grant on behalf of all authors, an exclusive licence (or non-exclusive for government employees) on a worldwide basis to the BMJ Publishing Group Ltd and its Licensees to permit this article (if accepted) to be published in Annals of the Rheumatic Diseases and any other BMJPGL products to exploit all subsidiary rights, as set out in their licence (http://ard.bmj.com/ifora/licence.pdf). http://ard.bmj.com/ on September 29, 2021 by guest. Protected copyright. 1 Copyright Article author (or their employer) 2009. -
Anti-STK11 / LKB1 Antibody (ARG59116)
Product datasheet [email protected] ARG59116 Package: 50 μg anti-STK11 / LKB1 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes STK11 / LKB1 Tested Reactivity Hu Tested Application WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name STK11 / LKB1 Antigen Species Human Immunogen Recombinant protein corresponding to K62-C430 of Human STK11 / LKB1. Conjugation Un-conjugated Alternate Names hLKB1; Serine/threonine-protein kinase STK11; Liver kinase B1; Renal carcinoma antigen NY-REN-19; LKB1; EC 2.7.11.1; PJS Application Instructions Application table Application Dilution WB 0.1 - 0.5 µg/ml Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Calculated Mw 49 kDa Properties Form Liquid Purification Affinity purification with immunogen. Buffer 0.9% NaCl, 0.2% Na2HPO4, 0.05% Sodium azide and 5% BSA. Preservative 0.05% Sodium azide Stabilizer 5% BSA Concentration 0.5 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 or below. 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. www.arigobio.com 1/3 Bioinformation Gene Symbol STK11 Gene Full Name serine/threonine kinase 11 Background This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. -
Genome-Wide CRISPR-Cas9 Screens Reveal Loss of Redundancy Between PKMYT1 and WEE1 in Glioblastoma Stem-Like Cells
Article Genome-wide CRISPR-Cas9 Screens Reveal Loss of Redundancy between PKMYT1 and WEE1 in Glioblastoma Stem-like Cells Graphical Abstract Authors Chad M. Toledo, Yu Ding, Pia Hoellerbauer, ..., Bruce E. Clurman, James M. Olson, Patrick J. Paddison Correspondence [email protected] (J.M.O.), [email protected] (P.J.P.) In Brief Patient-derived glioblastoma stem-like cells (GSCs) can be grown in conditions that preserve patient tumor signatures and their tumor initiating capacity. Toledo et al. use these conditions to perform genome-wide CRISPR-Cas9 lethality screens in both GSCs and non- transformed NSCs, revealing PKMYT1 as a candidate GSC-lethal gene. Highlights d CRISPR-Cas9 lethality screens performed in patient brain- tumor stem-like cells d PKMYT1 is identified in GSCs, but not NSCs, as essential for facilitating mitosis d PKMYT1 and WEE1 act redundantly in NSCs, where their inhibition is synthetic lethal d PKMYT1 and WEE1 redundancy can be broken by over- activation of EGFR and AKT Toledo et al., 2015, Cell Reports 13, 2425–2439 December 22, 2015 ª2015 The Authors http://dx.doi.org/10.1016/j.celrep.2015.11.021 Cell Reports Article Genome-wide CRISPR-Cas9 Screens Reveal Loss of Redundancy between PKMYT1 and WEE1 in Glioblastoma Stem-like Cells Chad M. Toledo,1,2,14 Yu Ding,1,14 Pia Hoellerbauer,1,2 Ryan J. Davis,1,2,3 Ryan Basom,4 Emily J. Girard,3 Eunjee Lee,5 Philip Corrin,1 Traver Hart,6,7 Hamid Bolouri,1 Jerry Davison,4 Qing Zhang,4 Justin Hardcastle,1 Bruce J. Aronow,8 Christopher L. -
Primary Tumor Site 137 Larynix
US 20190187143A1 ( 19) United States (12 ) Patent Application Publication ( 10) Pub . No. : US 2019 /0187143 A1 Wallweber ( 43 ) Pub . Date : Jun . 20 , 2019 ( 54 ) COMPOSITIONS AND METHODS TO Publication Classification DETECT HEAD AND NECK CANCER (51 ) Int. Cl. (71 ) Applicant : Laboratory Corporation of America GOIN 33 / 574 ( 2006 .01 ) GOIN 33 /52 (2006 . 01) Holdings , Burlington , NC (US ) (52 ) U . S . CI. (72 ) Inventor : Gerald J . Wallweber , Foster City , CA CPC .. GOIN 33 /57407 ( 2013 .01 ) ; GOIN 33 /5748 (US ) ( 2013 .01 ) ; GOIN 33 /52 ( 2013 .01 ) (57 ) ABSTRACT ( 21 ) Appl. No. : 16 /224 , 974 Disclosed are compositions and methods to detect proteins associated with Head and Neck Cancer, generally , or more ( 22 ) Filed : Dec . 19 , 2018 particularly , biomarkers of Head and Neck Squamous Cell Carcinoma (HNSCC ) . Such markers may be useful to allow Related U . S . Application Data individuals susceptible to HNSCC to manage their lifestyle (60 ) Provisional application No. 62/ 608 ,296 , filed on Dec . and /or medical treatment to avoid further progression of 20 , 2017 . disease . Primary Tumor Site primarytumor Site 137 Larynix Har Oralen cavityel . Gene Accuracy Kappa Sensitivity Specificity 1 CAB39L 0 . 9600 0 . 7745 0 .9831 0 .7818 2 ADAM12 0 . 9688 0 . 7506 0 . 9938 0 .6727 . 3 SH3BGRL2 0 .9596 0 .6972 0 . 9846 0 . 6636 4 NRG2 0 .9553 0 . 6710 0 .9808 0 .6545 5 COL13A11 0 . 9546 0 . 6376 0 . 9854 0 .5909 6 GRIN2D 1 0 . 9539 0 .6326 0 . 9862 0 .5727 7 LOXL2 0 . 9525 0 .5906 0 . 9915 0 .4909 8 HSD1786 0 . 9411 0 . -
Whole-Genome Sequencing Identifies Genomic Heterogeneity at a Nucleotide and Chromosomal Level in Bladder Cancer
Whole-genome sequencing identifies genomic heterogeneity at a nucleotide and chromosomal level in bladder cancer Carl D. Morrisona,1,2, Pengyuan Liub,1, Anna Woloszynska-Readc, Jianmin Zhangd, Wei Luoc, Maochun Qine, Wiam Bsharaf, Jeffrey M. Conroya, Linda Sabatinif, Peter Vedellb, Donghai Xiongb, Song Liue, Jianmin Wange, He Shend, Yinwei Lid, Angela R. Omilianf, Annette Hillf, Karen Headf, Khurshid Gurug, Dimiter Kunnevh, Robert Leache, Kevin H. Enge, Christopher Darlaka, Christopher Hoeflicha, Srividya Veerankia, Sean Glennd, Ming Youb, Steven C. Pruitth, Candace S. Johnsonc, and Donald L. Trumpi aCenter for Personalized Medicine and Departments of cPharmacology and Therapeutics, dCancer Genetics, eBiostatistics and Bioinformatics, fPathology, gUrology, hMolecular and Cellular Biology, and iMedicine, Roswell Park Cancer Institute, Buffalo, NY 14263; and bDepartment of Physiology and the Cancer Center, Medical College of Wisconsin, Milwaukee, WI 53226 Edited* by Carlo M. Croce, The Ohio State University, Columbus, OH, and approved January 2, 2014 (received for review July 22, 2013) Using complete genome analysis, we sequenced five bladder tumors earlier studies in melanoma (13) and medulloblastoma (14), ev- accrued from patients with muscle-invasive transitional cell carcinoma idence of the association of TP53 mutations with specific copy of the urinary bladder (TCC-UB) and identified a spectrum of genomic number alterations, referred to as chromothripsis, was noted. The aberrations. In three tumors, complex genotype changes were noted. study in medulloblastoma (14) was particularly intriguing in that All three had tumor protein p53 mutations and a relatively large identification of a molecular subclass with TP53 mutations was number of single-nucleotide variants (SNVs; average of 11.2 per associated with chromothripsis and a more aggressive clinical megabase), structural variants (SVs; average of 46), or both. -
Identi Cation of Novel Hub Genes Through Expression Pro Les
Identication of Novel Hub Genes Through Expression Proles Analysis in Adrenocortical Carcinoma Chenhe Yao Beijing Zhicheng Biomedical Technology Co,Ltd Xiaoling Zhao Beijing Zhicheng Biomedical Technology Co,Ltd Xuemeng Shang Beijing Zhicheng Biomedical Technology Co,Ltd Binghan Jia Beijing Zhicheng Biomedical Technology Co,Ltd Shuaijie Dou Beijing Zhicheng Biomedical Technology Co,Ltd Weiliang Ye Beijing Zhicheng Biomedical Technology Co,Ltd Yuemei Yang ( [email protected] ) Beijing Zhicheng Biomedical Technology,Co.,Ltd. Research Keywords: Adrenocortical carcinoma, biomarkers, gene expression proling, Co-expression, prognosis Posted Date: July 1st, 2020 DOI: https://doi.org/10.21203/rs.3.rs-38768/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/21 Abstract Background: Adrenocortical carcinoma (ACC) is a heterogeneous and rare malignant tumor associated with a poor prognosis. The molecular mechanisms of ACC remain elusive and more accurate biomarkers for the prediction of prognosis are needed. Methods: In this study, integrative proling analyses were performed to identify novel hub genes in ACC to provide promising targets for future investigation. Three gene expression proling datasets in the GEO database were used for the identication of overlapped differentially expressed genes (DEGs) following the criteria of adj.P.Value<0.05 and |log2 FC|>0.5 in ACC. Novel hub genes were screened out following a series of processes: the retrieval of DEGs with no known associations with ACC on Pubmed, then the cross-validation of expression values and signicant associations with overall survival in the GEPIA2 and starBase databases, and nally the prediction of gene-tumor association in the GeneCards database.