Polyclonal Antibody to JIP-2 (C-Term)

Total Page:16

File Type:pdf, Size:1020Kb

Polyclonal Antibody to JIP-2 (C-Term) AP10392PU-N OriGene Technologies Inc. OriGene EU Acris Antibodies GmbH 9620 Medical Center Drive, Ste 200 Schillerstr. 5 Rockville, MD 20850 32052 Herford UNITED STATES GERMANY Phone: +1-888-267-4436 Phone: +49-5221-34606-0 Fax: +1-301-340-8606 Fax: +49-5221-34606-11 [email protected] [email protected] Polyclonal Antibody to JIP-2 (C-term) - Aff - Purified Alternate names: C-jun-amino-terminal kinase-interacting protein 2, IB2, Islet-brain-2, JIP2, JIP2, JNK MAP kinase scaffold protein 2, JNK-interacting protein 2, MAPK8IP2, Mitogen-activated protein kinase 8-interacting protein 2, PRKM8IPL Catalog No.: AP10392PU-N Quantity: 0.1 mg Background: c-Jun amino-terminal kinase (JNK) is a member of the stress-activated group of mitogen- activated protein (MAP) kinases that are implicated in the control of cell growth. The JNK- interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 plays a number of roles including IL1 beta-induced apoptosis inhibition in insulin-secreting cells; may function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins; interacts with components of the JNK signaling pathway namely JNK, MAPKK7 and MLK2, MLK3 and DLK; binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2), the cytoplasmic tails of LRP1 and LRP2 (Megalin), the TPR motif-containing C- terminal of kinesin light chain and interacts with the cytoplasmic domain of APP. This protein has been classified as a housekeeping protein based on its essential role in cell physiology. Several splice variants are known with molecular weights (kDa)/pIs of 88.0/4.36 (isoform 1), 84.7/4.40 (isoform 2), 64.9/4.48 (isoform 3), 49.1/4.49 (isoform 4). Uniprot ID: Q13387 NCBI: NP_036456 GeneID: 23542 Host / Isotype: Rabbit / IgG Immunogen: Rabbits were immunized with a synthetic peptide, based on a C-terminal sequence conserved in all isoforms of Human JIP2 and differing from Mouse, Rat and Canine JIP2 by a single amino acid substitution. AA Sequence: n-LEYYQEHLAYACPTEDIYLE-c Format: State: Liquid purified IgG fraction. Purification: Affinity Chromatography. Buffer System: 50% Glycerol, 0.01% Sodium Azide and 1.0 mg/ml BSA. Applications: Western Blot (0.2-1.0 µg/ml). Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user. For research and in vitro use only. Not for diagnostic or therapeutic work. OG/20121030 Material Safety Datasheets are available at www.acris-antibodies.com or on request. Acris Antibodies is now part of the OriGene family. Learn more at www.origene.com 1 / 2 AP10392PU-N: Polyclonal Antibody to JIP-2 (C-term) - Aff - Purified Specificity: This antibody recognizes JIP2. Species: Human and Primate. Other species not tested. Storage: Store the antibody (in aliquots) at -20°C. Avoid repeated freezing and thawing. Shelf life: one year from despatch. For research and in vitro use only. Not for diagnostic or therapeutic work. OG/20121030 Material Safety Datasheets are available at www.acris-antibodies.com or on request. Acris Antibodies is now part of the OriGene family. Learn more at www.origene.com 2 / 2 Powered by TCPDF (www.tcpdf.org).
Recommended publications
  • Functional Genomics Analysis of Phelan-Mcdermid Syndrome 22Q13 Region During Human Neurodevelopment
    Delft University of Technology Functional genomics analysis of Phelan-McDermid syndrome 22q13 region during human neurodevelopment Ziats, Catherine A.; Grosvenor, Luke P.; Sarasua, Sara M.; Thurm, Audrey E.; Swedo, Susan E.; Mahfouz, Ahmed; Rennert, Owen M.; Ziats, Mark N. DOI 10.1371/journal.pone.0213921 Publication date 2019 Document Version Final published version Published in PLoS ONE Citation (APA) Ziats, C. A., Grosvenor, L. P., Sarasua, S. M., Thurm, A. E., Swedo, S. E., Mahfouz, A., Rennert, O. M., & Ziats, M. N. (2019). Functional genomics analysis of Phelan-McDermid syndrome 22q13 region during human neurodevelopment. PLoS ONE, 14(3), 1-13. [e0213921]. https://doi.org/10.1371/journal.pone.0213921 Important note To cite this publication, please use the final published version (if applicable). Please check the document version above. Copyright Other than for strictly personal use, it is not permitted to download, forward or distribute the text or part of it, without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license such as Creative Commons. Takedown policy Please contact us and provide details if you believe this document breaches copyrights. We will remove access to the work immediately and investigate your claim. This work is downloaded from Delft University of Technology. For technical reasons the number of authors shown on this cover page is limited to a maximum of 10. RESEARCH ARTICLE Functional genomics analysis of Phelan- McDermid syndrome 22q13 region during human neurodevelopment 1☯ 2,3☯ 4 2 Catherine A. ZiatsID *, Luke P. Grosvenor , Sara M. Sarasua , Audrey E.
    [Show full text]
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
    [Show full text]
  • Functional Parsing of Driver Mutations in the Colorectal Cancer Genome Reveals Numerous Suppressors of Anchorage-Independent
    Supplementary information Functional parsing of driver mutations in the colorectal cancer genome reveals numerous suppressors of anchorage-independent growth Ugur Eskiocak1, Sang Bum Kim1, Peter Ly1, Andres I. Roig1, Sebastian Biglione1, Kakajan Komurov2, Crystal Cornelius1, Woodring E. Wright1, Michael A. White1, and Jerry W. Shay1. 1Department of Cell Biology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9039. 2Department of Systems Biology, University of Texas M.D. Anderson Cancer Center, Houston, TX 77054. Supplementary Figure S1. K-rasV12 expressing cells are resistant to p53 induced apoptosis. Whole-cell extracts from immortalized K-rasV12 or p53 down regulated HCECs were immunoblotted with p53 and its down-stream effectors after 10 Gy gamma-radiation. ! Supplementary Figure S2. Quantitative validation of selected shRNAs for their ability to enhance soft-agar growth of immortalized shTP53 expressing HCECs. Each bar represents 8 data points (quadruplicates from two separate experiments). Arrows denote shRNAs that failed to enhance anchorage-independent growth in a statistically significant manner. Enhancement for all other shRNAs were significant (two tailed Studentʼs t-test, compared to none, mean ± s.e.m., P<0.05)." ! Supplementary Figure S3. Ability of shRNAs to knockdown expression was demonstrated by A, immunoblotting for K-ras or B-E, Quantitative RT-PCR for ERICH1, PTPRU, SLC22A15 and SLC44A4 48 hours after transfection into 293FT cells. Two out of 23 tested shRNAs did not provide any knockdown. " ! Supplementary Figure S4. shRNAs against A, PTEN and B, NF1 do not enhance soft agar growth in HCECs without oncogenic manipulations (Student!s t-test, compared to none, mean ± s.e.m., ns= non-significant).
    [Show full text]
  • E6-Induced Selective Translation of WNT4 and JIP2 Promotes the Progression of Cervical Cancer Via a Noncanonical WNT Signaling Pathway
    Signal Transduction and Targeted Therapy www.nature.com/sigtrans ARTICLE OPEN E6-induced selective translation of WNT4 and JIP2 promotes the progression of cervical cancer via a noncanonical WNT signaling pathway Lin Zhao1,2, Longlong Wang1, Chenglan Zhang1, Ze Liu1, Yongjun Piao 1, Jie Yan1, Rong Xiang1, Yuanqing Yao1,2 and Yi Shi 1 mRNA translation reprogramming occurs frequently in many pathologies, including cancer and viral infection. It remains largely unknown whether viral-induced alterations in mRNA translation contribute to carcinogenesis. Most cervical cancer is caused by high-risk human papillomavirus infection, resulting in the malignant transformation of normal epithelial cells mainly via viral E6 and E7 oncoproteins. Here, we utilized polysome profiling and deep RNA sequencing to systematically evaluate E6-regulated mRNA translation in HPV18-infected cervical cancer cells. We found that silencing E6 can cause over a two-fold change in the translation efficiency of ~653 mRNAs, most likely in an eIF4E- and eIF2α-independent manner. In addition, we identified that E6 can selectively upregulate the translation of WNT4, JIP1, and JIP2, resulting in the activation of the noncanonical WNT/PCP/JNK pathway to promote cell proliferation in vitro and tumor growth in vivo. Ectopic expression of WNT4/JIP2 can effectively rescue the decreased cell proliferation caused by E6 silencing, strongly suggesting that the WNT4/JIP2 pathway mediates the role of E6 in promoting cell proliferation. Thus, our results revealed a novel oncogenic mechanism
    [Show full text]
  • Epigenetic Mechanisms Are Involved in the Oncogenic Properties of ZNF518B in Colorectal Cancer
    Epigenetic mechanisms are involved in the oncogenic properties of ZNF518B in colorectal cancer Francisco Gimeno-Valiente, Ángela L. Riffo-Campos, Luis Torres, Noelia Tarazona, Valentina Gambardella, Andrés Cervantes, Gerardo López-Rodas, Luis Franco and Josefa Castillo SUPPLEMENTARY METHODS 1. Selection of genomic sequences for ChIP analysis To select the sequences for ChIP analysis in the five putative target genes, namely, PADI3, ZDHHC2, RGS4, EFNA5 and KAT2B, the genomic region corresponding to the gene was downloaded from Ensembl. Then, zoom was applied to see in detail the promoter, enhancers and regulatory sequences. The details for HCT116 cells were then recovered and the target sequences for factor binding examined. Obviously, there are not data for ZNF518B, but special attention was paid to the target sequences of other zinc-finger containing factors. Finally, the regions that may putatively bind ZNF518B were selected and primers defining amplicons spanning such sequences were searched out. Supplementary Figure S3 gives the location of the amplicons used in each gene. 2. Obtaining the raw data and generating the BAM files for in silico analysis of the effects of EHMT2 and EZH2 silencing The data of siEZH2 (SRR6384524), siG9a (SRR6384526) and siNon-target (SRR6384521) in HCT116 cell line, were downloaded from SRA (Bioproject PRJNA422822, https://www.ncbi. nlm.nih.gov/bioproject/), using SRA-tolkit (https://ncbi.github.io/sra-tools/). All data correspond to RNAseq single end. doBasics = TRUE doAll = FALSE $ fastq-dump -I --split-files SRR6384524 Data quality was checked using the software fastqc (https://www.bioinformatics.babraham. ac.uk /projects/fastqc/). The first low quality removing nucleotides were removed using FASTX- Toolkit (http://hannonlab.cshl.edu/fastxtoolkit/).
    [Show full text]
  • Compound Phenotype in a Girl with R(22), Concomitant Microdeletion 22Q13.32- Q13.33 and Mosaic Monosomy 22 Anna A
    Kashevarova et al. Molecular Cytogenetics (2018) 11:26 https://doi.org/10.1186/s13039-018-0375-3 RESEARCH Open Access Compound phenotype in a girl with r(22), concomitant microdeletion 22q13.32- q13.33 and mosaic monosomy 22 Anna A. Kashevarova1* , Elena O. Belyaeva1, Aleksandr M. Nikonov2, Olga V. Plotnikova2, Nikolay A. Skryabin1, Tatyana V. Nikitina1, Stanislav A. Vasilyev1, Yulia S. Yakovleva1,3, Nadezda P. Babushkina1, Ekaterina N. Tolmacheva1, Mariya E. Lopatkina1, Renata R. Savchenko1, Lyudmila P. Nazarenko1,3 and Igor N. Lebedev1,3 Abstract Background: Ring chromosome instability may influence a patient’s phenotype and challenge its interpretation. Results: Here, we report a 4-year-old girl with a compound phenotype. Cytogenetic analysis revealed her karyotype to be 46,XX,r(22). aCGH identified a 180 kb 22q13.32 duplication, a de novo 2.024 Mb subtelomeric 22q13.32-q13.33 deletion, which is associated with Phelan-McDermid syndrome, and a maternal single gene 382-kb TUSC7 deletion of uncertain clinical significance located in the region of the 3q13.31 deletion syndrome. All chromosomal aberrations were confirmed by real-time PCR in lymphocytes and detected in skin fibroblasts. The deletions were also found in the buccal epithelium. According to FISH analysis, 8% and 24% of the patient’s lymphocytes and skin fibroblasts, respectively, had monosomy 22. Conclusions: We believe that a combination of 22q13.32-q13.33 deletion and monosomy 22 in a portion of cells can better define the clinical phenotype of the patient. Importantly, the in vivo presence of monosomic cells indicates ring chromosome instability, which may favor karyotype correction that is significant for the development of chromosomal therapy protocols.
    [Show full text]
  • Integrative Analysis of Disease Signatures Shows Inflammation Disrupts Juvenile Experience-Dependent Cortical Plasticity
    New Research Development Integrative Analysis of Disease Signatures Shows Inflammation Disrupts Juvenile Experience- Dependent Cortical Plasticity Milo R. Smith1,2,3,4,5,6,7,8, Poromendro Burman1,3,4,5,8, Masato Sadahiro1,3,4,5,6,8, Brian A. Kidd,2,7 Joel T. Dudley,2,7 and Hirofumi Morishita1,3,4,5,8 DOI:http://dx.doi.org/10.1523/ENEURO.0240-16.2016 1Department of Neuroscience, Icahn School of Medicine at Mount Sinai, New York, New York 10029, 2Department of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, New York 10029, 3Department of Psychiatry, Icahn School of Medicine at Mount Sinai, New York, New York 10029, 4Department of Ophthalmology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, 5Mindich Child Health and Development Institute, Icahn School of Medicine at Mount Sinai, New York, New York 10029, 6Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York 10029, 7Icahn Institute for Genomics and Multiscale Biology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, and 8Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, New York 10029 Visual Abstract Throughout childhood and adolescence, periods of heightened neuroplasticity are critical for the development of healthy brain function and behavior. Given the high prevalence of neurodevelopmental disorders, such as autism, identifying disruptors of developmental plasticity represents an essential step for developing strategies for prevention and intervention. Applying a novel computational approach that systematically assessed connections between 436 transcriptional signatures of disease and multiple signatures of neuroplasticity, we identified inflammation as a common pathological process central to a diverse set of diseases predicted to dysregulate Significance Statement During childhood and adolescence, heightened neuroplasticity allows the brain to reorganize and adapt to its environment.
    [Show full text]
  • Chromosome 22 Array-CGH Profiling of Breast Cancer Delimited Minimal Common Regions of Genomic Imbalances and Revealed Frequent Intra-Tumoral Genetic Heterogeneity
    935-945 9/9/06 12:32 Page 935 INTERNATIONAL JOURNAL OF ONCOLOGY 29: 935-945, 2006 935 Chromosome 22 array-CGH profiling of breast cancer delimited minimal common regions of genomic imbalances and revealed frequent intra-tumoral genetic heterogeneity MAGDALENA BENETKIEWICZ1,4, ARKADIUSZ PIOTROWSKI1, TERESITA DÍAZ DE STÅHL1, MICHAL JANKOWSKI2, DARIUSZ BALA2, JACEK HOFFMAN2, EWA SRUTEK2, RYSZARD LASKOWSKI2, WOJCIECH ZEGARSKI2 and JAN P. DUMANSKI1,3 1Department of Genetics and Pathology, Rudbeck Laboratory, Uppsala University, 751 85 Uppsala, Sweden; 2Department of Breast Cancer, Clinic of Oncological Surgery, Oncology Center, Collegium Medicum Nicolaus Copernicus University, 85 796 Bydgoszcz, Poland; 3Department of Genetics, University of Alabama at Birmingham, KAUL 420, 1530 3rd Ave. S, Birmingham, AL 35294, USA Received March 27, 2006; Accepted June 2, 2006 Abstract. Breast cancer is a common malignancy and the Introduction second most frequent cause of death among women. Our aim was to perform DNA copy number profiling of 22q in Breast cancer is the most common malignancy among women breast tumors using a methodology which is superior, as and the second most common cause of death after lung cancer compared to the ones applied previously. We studied 83 (1). It is a complex genetic disorder and some aberrations have biopsies from 63 tumors obtained from 60 female patients. A been correlated with heterogeneous histology and clinical general conclusion is that multiple distinct patterns of genetic behavior. Breast carcinoma arises from the epithelium of aberrations were observed, which included deletion(s) and/or glandular tissue, which includes ducts and lobules. Histo- gain(s), ranging in size from affecting the whole chromo- logically, this neoplasm can be classified into non-invasive some to only a few hundred kb.
    [Show full text]
  • Role of the JIP4 Scaffold Protein in the Regulation of Mitogen-Activated Protein Kinase Signaling Pathways† Nyaya Kelkar,‡ Claire L
    University of Massachusetts Medical School eScholarship@UMMS Open Access Articles Open Access Publications by UMMS Authors 2005-03-16 Role of the JIP4 scaffold protein in the regulation of mitogen- activated protein kinase signaling pathways Nyaya Kelkar University of Massachusetts Medical School Et al. Let us know how access to this document benefits ou.y Follow this and additional works at: https://escholarship.umassmed.edu/oapubs Part of the Life Sciences Commons, and the Medicine and Health Sciences Commons Repository Citation Kelkar N, Standen CL, Davis RJ. (2005). Role of the JIP4 scaffold protein in the regulation of mitogen- activated protein kinase signaling pathways. Open Access Articles. https://doi.org/10.1128/ MCB.25.7.2733-2743.2005. Retrieved from https://escholarship.umassmed.edu/oapubs/1414 This material is brought to you by eScholarship@UMMS. It has been accepted for inclusion in Open Access Articles by an authorized administrator of eScholarship@UMMS. For more information, please contact [email protected]. MOLECULAR AND CELLULAR BIOLOGY, Apr. 2005, p. 2733–2743 Vol. 25, No. 7 0270-7306/05/$08.00ϩ0 doi:10.1128/MCB.25.7.2733–2743.2005 Copyright © 2005, American Society for Microbiology. All Rights Reserved. Role of the JIP4 Scaffold Protein in the Regulation of Mitogen-Activated Protein Kinase Signaling Pathways† Nyaya Kelkar,‡ Claire L. Standen, and Roger J. Davis* Howard Hughes Medical Institute and Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts Received 13 November 2004/Returned for modification 16 December 2004/Accepted 22 December 2004 The c-Jun NH2-terminal kinase (JNK)-interacting protein (JIP) group of scaffold proteins (JIP1, JIP2, and JIP3) can interact with components of the JNK signaling pathway and potently activate JNK.
    [Show full text]
  • Role of JIP1-JNK Signaling in Beta-Cell Function and Autophagy
    University of Massachusetts Medical School eScholarship@UMMS GSBS Dissertations and Theses Graduate School of Biomedical Sciences 2018-01-19 Role of JIP1-JNK Signaling in Beta-Cell Function and Autophagy Seda Barutcu University of Massachusetts Medical School Let us know how access to this document benefits ou.y Follow this and additional works at: https://escholarship.umassmed.edu/gsbs_diss Part of the Biology Commons, Cell Biology Commons, and the Cellular and Molecular Physiology Commons Repository Citation Barutcu S. (2018). Role of JIP1-JNK Signaling in Beta-Cell Function and Autophagy. GSBS Dissertations and Theses. https://doi.org/10.13028/M2VT2X. Retrieved from https://escholarship.umassmed.edu/ gsbs_diss/954 Creative Commons License This work is licensed under a Creative Commons Attribution-Noncommercial 4.0 License This material is brought to you by eScholarship@UMMS. It has been accepted for inclusion in GSBS Dissertations and Theses by an authorized administrator of eScholarship@UMMS. For more information, please contact [email protected]. ROLE OF JIP1-JNK SIGNALING IN BETA-CELL FUNCTION AND AUTOPHAGY A Dissertation Presented By SEDA BARUTCU Submitted to the Faculty of the University of Massachusetts Graduate School of Biomedical Sciences, Worcester in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY January 19th, 2018 Program in Molecular Medicine ROLE OF JIP1-JNK SIGNALING IN BETA-CELL FUNCTION AND AUTOPHAGY A Dissertation Presented By Seda Barutcu This work was undertaken in the Graduate School of Biomedical Sciences Program in Molecular Medicine Under the mentorship of Roger J. Davis, Ph.D., Thesis Advisor Amy K. Walker, Ph.D., Member of Committee David A.
    [Show full text]
  • Autocrine IFN Signaling Inducing Profibrotic Fibroblast Responses By
    Downloaded from http://www.jimmunol.org/ by guest on September 23, 2021 Inducing is online at: average * The Journal of Immunology , 11 of which you can access for free at: 2013; 191:2956-2966; Prepublished online 16 from submission to initial decision 4 weeks from acceptance to publication August 2013; doi: 10.4049/jimmunol.1300376 http://www.jimmunol.org/content/191/6/2956 A Synthetic TLR3 Ligand Mitigates Profibrotic Fibroblast Responses by Autocrine IFN Signaling Feng Fang, Kohtaro Ooka, Xiaoyong Sun, Ruchi Shah, Swati Bhattacharyya, Jun Wei and John Varga J Immunol cites 49 articles Submit online. Every submission reviewed by practicing scientists ? is published twice each month by Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts http://jimmunol.org/subscription Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html http://www.jimmunol.org/content/suppl/2013/08/20/jimmunol.130037 6.DC1 This article http://www.jimmunol.org/content/191/6/2956.full#ref-list-1 Information about subscribing to The JI No Triage! Fast Publication! Rapid Reviews! 30 days* Why • • • Material References Permissions Email Alerts Subscription Supplementary The Journal of Immunology The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2013 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. This information is current as of September 23, 2021. The Journal of Immunology A Synthetic TLR3 Ligand Mitigates Profibrotic Fibroblast Responses by Inducing Autocrine IFN Signaling Feng Fang,* Kohtaro Ooka,* Xiaoyong Sun,† Ruchi Shah,* Swati Bhattacharyya,* Jun Wei,* and John Varga* Activation of TLR3 by exogenous microbial ligands or endogenous injury-associated ligands leads to production of type I IFN.
    [Show full text]
  • Barkbase: Epigenomic Annotation of Canine Genomes
    G C A T T A C G G C A T genes Article BarkBase: Epigenomic Annotation of Canine Genomes Kate Megquier 1, Diane P. Genereux 1 , Jessica Hekman 1 , Ross Swofford 1, Jason Turner-Maier 1, Jeremy Johnson 1, Jacob Alonso 1, Xue Li 1,2, Kathleen Morrill 1,2, Lynne J. Anguish 3, Michele Koltookian 1, Brittney Logan 2, Claire R. Sharp 4 , Lluis Ferrer 5, Kerstin Lindblad-Toh 1,6, Vicki N. Meyers-Wallen 7, Andrew Hoffman 8,9 and Elinor K. Karlsson 1,2,10,* 1 Vertebrate Genomics, Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA; [email protected] (K.M.); [email protected] (D.P.G.); [email protected] (J.H.); swoff[email protected] (R.S.); [email protected] (J.T.-M.); [email protected] (J.J.); [email protected] (J.A.); [email protected] (X.L.); [email protected] (K.M.); [email protected] (M.K.); [email protected] (K.L.-T.) 2 Bioinformatics and Integrative Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA; [email protected] 3 Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA; [email protected] 4 School of Veterinary and Life Sciences, College of Veterinary Medicine, Murdoch University, Perth, Murdoch, WA 6150, Australia; [email protected] 5 Departament de Medicina i Cirurgia Animals Veterinary School, Universitat Autonoma de Barcelona, 08193 Barcelona, Spain; [email protected] 6 Science for Life Laboratory, Department of Medical Biochemistry &
    [Show full text]