PA2G4 Antibody (F54781)

Total Page:16

File Type:pdf, Size:1020Kb

PA2G4 Antibody (F54781) PA2G4 Antibody / EBP1 / ErbB3-binding protein 1 (F54781) Catalog No. Formulation Size F54781-0.4ML In 1X PBS, pH 7.4, with 0.09% sodium azide 0.4 ml F54781-0.08ML In 1X PBS, pH 7.4, with 0.09% sodium azide 0.08 ml Bulk quote request Availability 1-3 business days Species Reactivity Human Format Purified Clonality Polyclonal (rabbit origin) Isotype Rabbit Ig Purity Purified UniProt Q9UQ80 Localization Cytoplasmic, nuclear Applications Immunofluorescence : 1:25 Flow cytometry : 1:25 (1x10e6 cells) Immunohistochemistry (FFPE) : 1:25 Western blot : 1:500-1:1000 Limitations This PA2G4 antibody is available for research use only. IHC testing of FFPE human lung carcinoma tissue with PA2G4 antibody. HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to staining. Immunofluorescent staining of fixed and permeabilized human U-251 cells with PA2G4 antibody (green), DAPI nuclear stain (blue) and anti-Actin (red). Western blot testing of human 1) A431 and 2) Jurkat cell lysate with PA2G4 antibody. Predicted molecular weight ~44 kDa. Flow cytometry testing of human A2058 cells with PA2G4 antibody; Blue=isotype control, Green= PA2G4 antibody. Description PA2G4 is an RNA-binding protein that is involved in growth regulation. This protein is present in pre-ribosomal ribonucleoprotein complexes and may be involved in ribosome assembly and the regulation of intermediate and late steps of rRNA processing. The protein can interact with the cytoplasmic domain of the ErbB3 receptor and may contribute to transducing growth regulatory signals. It is also a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. It has been implicated in growth inhibition and the induction of differentiation of human cancer cells. Application Notes The stated application concentrations are suggested starting points. Titration of the PA2G4 antibody may be required due to differences in protocols and secondary/substrate sensitivity. Immunogen A portion of amino acids 228-255 from the human protein was used as the immunogen for the PA2G4 antibody. Storage Aliquot the PA2G4 antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles. Ordering: Phone:858.663.9055 | Fax:1.267.821.0800 | Email:[email protected] Copyright © NSJ Bioreagents. All rights reserved.
Recommended publications
  • EBP1/PA2G4 Rabbit Pab
    Leader in Biomolecular Solutions for Life Science EBP1/PA2G4 Rabbit pAb Catalog No.: A5376 Basic Information Background Catalog No. This gene encodes an RNA-binding protein that is involved in growth regulation. This A5376 protein is present in pre-ribosomal ribonucleoprotein complexes and may be involved in ribosome assembly and the regulation of intermediate and late steps of rRNA Observed MW processing. This protein can interact with the cytoplasmic domain of the ErbB3 receptor 44kDa and may contribute to transducing growth regulatory signals. This protein is also a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle Calculated MW regulatory genes through its interactions with histone deacetylases. This protein has 38kDa/43kDa been implicated in growth inhibition and the induction of differentiation of human cancer cells. Six pseudogenes, located on chromosomes 3, 6, 9, 18, 20 and X, have been Category identified. Primary antibody Applications WB, IHC Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 5036 Q9UQ80 IHC 1:50 - 1:200 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 1-394 of human EBP1/PA2G4 (NP_006182.2). Synonyms PA2G4;EBP1;HG4-1;p38-2G4 Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using EBP1/PA2G4 antibody (A5376) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution.
    [Show full text]
  • Genome-Wide Analysis of Androgen Receptor Binding and Gene Regulation in Two CWR22-Derived Prostate Cancer Cell Lines
    Endocrine-Related Cancer (2010) 17 857–873 Genome-wide analysis of androgen receptor binding and gene regulation in two CWR22-derived prostate cancer cell lines Honglin Chen1, Stephen J Libertini1,4, Michael George1, Satya Dandekar1, Clifford G Tepper 2, Bushra Al-Bataina1, Hsing-Jien Kung2,3, Paramita M Ghosh2,3 and Maria Mudryj1,4 1Department of Medical Microbiology and Immunology, University of California Davis, 3147 Tupper Hall, Davis, California 95616, USA 2Division of Basic Sciences, Department of Biochemistry and Molecular Medicine, Cancer Center and 3Department of Urology, University of California Davis, Sacramento, California 95817, USA 4Veterans Affairs Northern California Health Care System, Mather, California 95655, USA (Correspondence should be addressed to M Mudryj at Department of Medical Microbiology and Immunology, University of California, Davis; Email: [email protected]) Abstract Prostate carcinoma (CaP) is a heterogeneous multifocal disease where gene expression and regulation are altered not only with disease progression but also between metastatic lesions. The androgen receptor (AR) regulates the growth of metastatic CaPs; however, sensitivity to androgen ablation is short lived, yielding to emergence of castrate-resistant CaP (CRCaP). CRCaP prostate cancers continue to express the AR, a pivotal prostate regulator, but it is not known whether the AR targets similar or different genes in different castrate-resistant cells. In this study, we investigated AR binding and AR-dependent transcription in two related castrate-resistant cell lines derived from androgen-dependent CWR22-relapsed tumors: CWR22Rv1 (Rv1) and CWR-R1 (R1). Expression microarray analysis revealed that R1 and Rv1 cells had significantly different gene expression profiles individually and in response to androgen.
    [Show full text]
  • A Dissertation Entitled the Androgen Receptor
    A Dissertation entitled The Androgen Receptor as a Transcriptional Co-activator: Implications in the Growth and Progression of Prostate Cancer By Mesfin Gonit Submitted to the Graduate Faculty as partial fulfillment of the requirements for the PhD Degree in Biomedical science Dr. Manohar Ratnam, Committee Chair Dr. Lirim Shemshedini, Committee Member Dr. Robert Trumbly, Committee Member Dr. Edwin Sanchez, Committee Member Dr. Beata Lecka -Czernik, Committee Member Dr. Patricia R. Komuniecki, Dean College of Graduate Studies The University of Toledo August 2011 Copyright 2011, Mesfin Gonit This document is copyrighted material. Under copyright law, no parts of this document may be reproduced without the expressed permission of the author. An Abstract of The Androgen Receptor as a Transcriptional Co-activator: Implications in the Growth and Progression of Prostate Cancer By Mesfin Gonit As partial fulfillment of the requirements for the PhD Degree in Biomedical science The University of Toledo August 2011 Prostate cancer depends on the androgen receptor (AR) for growth and survival even in the absence of androgen. In the classical models of gene activation by AR, ligand activated AR signals through binding to the androgen response elements (AREs) in the target gene promoter/enhancer. In the present study the role of AREs in the androgen- independent transcriptional signaling was investigated using LP50 cells, derived from parental LNCaP cells through extended passage in vitro. LP50 cells reflected the signature gene overexpression profile of advanced clinical prostate tumors. The growth of LP50 cells was profoundly dependent on nuclear localized AR but was independent of androgen. Nevertheless, in these cells AR was unable to bind to AREs in the absence of androgen.
    [Show full text]
  • Open Data for Differential Network Analysis in Glioma
    International Journal of Molecular Sciences Article Open Data for Differential Network Analysis in Glioma , Claire Jean-Quartier * y , Fleur Jeanquartier y and Andreas Holzinger Holzinger Group HCI-KDD, Institute for Medical Informatics, Statistics and Documentation, Medical University Graz, Auenbruggerplatz 2/V, 8036 Graz, Austria; [email protected] (F.J.); [email protected] (A.H.) * Correspondence: [email protected] These authors contributed equally to this work. y Received: 27 October 2019; Accepted: 3 January 2020; Published: 15 January 2020 Abstract: The complexity of cancer diseases demands bioinformatic techniques and translational research based on big data and personalized medicine. Open data enables researchers to accelerate cancer studies, save resources and foster collaboration. Several tools and programming approaches are available for analyzing data, including annotation, clustering, comparison and extrapolation, merging, enrichment, functional association and statistics. We exploit openly available data via cancer gene expression analysis, we apply refinement as well as enrichment analysis via gene ontology and conclude with graph-based visualization of involved protein interaction networks as a basis for signaling. The different databases allowed for the construction of huge networks or specified ones consisting of high-confidence interactions only. Several genes associated to glioma were isolated via a network analysis from top hub nodes as well as from an outlier analysis. The latter approach highlights a mitogen-activated protein kinase next to a member of histondeacetylases and a protein phosphatase as genes uncommonly associated with glioma. Cluster analysis from top hub nodes lists several identified glioma-associated gene products to function within protein complexes, including epidermal growth factors as well as cell cycle proteins or RAS proto-oncogenes.
    [Show full text]
  • PA2G4 Antibody (Center R243) Blocking Peptide Synthetic Peptide Catalog # Bp2848d
    10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 PA2G4 Antibody (Center R243) Blocking Peptide Synthetic peptide Catalog # BP2848d Specification PA2G4 Antibody (Center R243) Blocking PA2G4 Antibody (Center R243) Blocking Peptide - Peptide - Background Product Information PA2G4 is an RNA-binding protein that is Primary Accession Q9UQ80 involved in growth regulation. This protein is present in pre-ribosomal ribonucleoprotein complexes and may be involved in ribosome PA2G4 Antibody (Center R243) Blocking Peptide - Additional Information assembly and the regulation of intermediate and late steps of rRNA processing. The protein can interact with the cytoplasmic domain of Gene ID 5036 the ErbB3 receptor and may contribute to transducing growth regulatory signals. It is also Other Names a transcriptional co-repressor of androgen Proliferation-associated protein 2G4, Cell receptor-regulated genes and other cell cycle cycle protein p38-2G4 homolog, hG4-1, regulatory genes through its interactions with ErbB3-binding protein 1, PA2G4, EBP1 histone deacetylases. It has been implicated in Target/Specificity growth inhibition and the induction of The synthetic peptide sequence used to differentiation of human cancer cells. generate the antibody <a href=/products/AP2848d>AP2848d</a> PA2G4 Antibody (Center R243) Blocking was selected from the Center region of Peptide - References human PA2G4. A 10 to 100 fold molar excess to antibody is recommended. Zhang,Y., Mol. Cancer Ther. 7 (10), 3176-3186 Precise conditions should be optimized for a (2008)Zhang,Y., Cancer Lett. 265 (2), 298-306 particular assay. (2008)Okada,M., J. Biol. Chem. 282 (50), 36744-36754 (2007) Format Peptides are lyophilized in a solid powder format.
    [Show full text]
  • A High-Throughput Approach to Uncover Novel Roles of APOBEC2, a Functional Orphan of the AID/APOBEC Family
    Rockefeller University Digital Commons @ RU Student Theses and Dissertations 2018 A High-Throughput Approach to Uncover Novel Roles of APOBEC2, a Functional Orphan of the AID/APOBEC Family Linda Molla Follow this and additional works at: https://digitalcommons.rockefeller.edu/ student_theses_and_dissertations Part of the Life Sciences Commons A HIGH-THROUGHPUT APPROACH TO UNCOVER NOVEL ROLES OF APOBEC2, A FUNCTIONAL ORPHAN OF THE AID/APOBEC FAMILY A Thesis Presented to the Faculty of The Rockefeller University in Partial Fulfillment of the Requirements for the degree of Doctor of Philosophy by Linda Molla June 2018 © Copyright by Linda Molla 2018 A HIGH-THROUGHPUT APPROACH TO UNCOVER NOVEL ROLES OF APOBEC2, A FUNCTIONAL ORPHAN OF THE AID/APOBEC FAMILY Linda Molla, Ph.D. The Rockefeller University 2018 APOBEC2 is a member of the AID/APOBEC cytidine deaminase family of proteins. Unlike most of AID/APOBEC, however, APOBEC2’s function remains elusive. Previous research has implicated APOBEC2 in diverse organisms and cellular processes such as muscle biology (in Mus musculus), regeneration (in Danio rerio), and development (in Xenopus laevis). APOBEC2 has also been implicated in cancer. However the enzymatic activity, substrate or physiological target(s) of APOBEC2 are unknown. For this thesis, I have combined Next Generation Sequencing (NGS) techniques with state-of-the-art molecular biology to determine the physiological targets of APOBEC2. Using a cell culture muscle differentiation system, and RNA sequencing (RNA-Seq) by polyA capture, I demonstrated that unlike the AID/APOBEC family member APOBEC1, APOBEC2 is not an RNA editor. Using the same system combined with enhanced Reduced Representation Bisulfite Sequencing (eRRBS) analyses I showed that, unlike the AID/APOBEC family member AID, APOBEC2 does not act as a 5-methyl-C deaminase.
    [Show full text]
  • Drugging MYCN Oncogenic Signalling Through the MYCN-PA2G4 Binding Interface
    Author Manuscript Published OnlineFirst on September 9, 2019; DOI: 10.1158/0008-5472.CAN-19-1112 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. Drugging MYCN oncogenic signalling through the MYCN-PA2G4 binding interface Jessica Koach1, 2, #, Jessica K. Holien3#, Hassina Massudi1#, Daniel R. Carter1,4,5, Olivia C. Ciampa1, Mika Herath1, Taylor Lim1, Janith A. Seneviratne1, Giorgio Milazzo6, Jayne E. Murray1, Joshua A. McCarroll1,7, Bing Liu1, Chelsea Mayoh1, Bryce Keenan1, Brendan W. Stevenson3, Michael A. Gorman3,8, Jessica L. Bell9, Larissa Doughty3,8, Stefan Hüttelmaier9, Andre Oberthuer10,11, Matthias Fischer10,12, Andrew J. Gifford1,13, Tao Liu1, Xiaoling Zhang14, Shizhen Zhu14, W. Clay Gustafson2, Michelle Haber1, Murray D. Norris1, Jamie I. Fletcher1, Giovanni Perini6, Michael W. Parker3,8, Belamy B. Cheung1,4,15,*, Glenn M. Marshall1,4,16,* 1Children’s Cancer Institute Australia for Medical Research, Lowy Cancer Research Centre, UNSW Sydney, Kensington, NSW, Australia; 2Department of Pediatrics, Helen Diller Family Comprehensive Cancer Center, University of California, San Francisco, California, USA; 3ACRF Rational Drug Discovery Centre, St. Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia; 4School of Women's & Children's Health, UNSW Sydney, Randwick NSW 2031, Australia; 5School of Biomedical Engineering, University of Technology Sydney, Australia; 6Department of Pharmacy and Biotechnology, University of Bologna, Bologna, Italy; 7Australian Centre
    [Show full text]
  • Renoprotective Effect of Combined Inhibition of Angiotensin-Converting Enzyme and Histone Deacetylase
    BASIC RESEARCH www.jasn.org Renoprotective Effect of Combined Inhibition of Angiotensin-Converting Enzyme and Histone Deacetylase † ‡ Yifei Zhong,* Edward Y. Chen, § Ruijie Liu,*¶ Peter Y. Chuang,* Sandeep K. Mallipattu,* ‡ ‡ † | ‡ Christopher M. Tan, § Neil R. Clark, § Yueyi Deng, Paul E. Klotman, Avi Ma’ayan, § and ‡ John Cijiang He* ¶ *Department of Medicine, Mount Sinai School of Medicine, New York, New York; †Department of Nephrology, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China; ‡Department of Pharmacology and Systems Therapeutics and §Systems Biology Center New York, Mount Sinai School of Medicine, New York, New York; |Baylor College of Medicine, Houston, Texas; and ¶Renal Section, James J. Peters Veterans Affairs Medical Center, New York, New York ABSTRACT The Connectivity Map database contains microarray signatures of gene expression derived from approximately 6000 experiments that examined the effects of approximately 1300 single drugs on several human cancer cell lines. We used these data to prioritize pairs of drugs expected to reverse the changes in gene expression observed in the kidneys of a mouse model of HIV-associated nephropathy (Tg26 mice). We predicted that the combination of an angiotensin-converting enzyme (ACE) inhibitor and a histone deacetylase inhibitor would maximally reverse the disease-associated expression of genes in the kidneys of these mice. Testing the combination of these inhibitors in Tg26 mice revealed an additive renoprotective effect, as suggested by reduction of proteinuria, improvement of renal function, and attenuation of kidney injury. Furthermore, we observed the predicted treatment-associated changes in the expression of selected genes and pathway components. In summary, these data suggest that the combination of an ACE inhibitor and a histone deacetylase inhibitor could have therapeutic potential for various kidney diseases.
    [Show full text]
  • Genome-Wide Association Study Reveals First Locus for Anorexia Nervosa and Metabolic Correlations
    bioRxiv preprint doi: https://doi.org/10.1101/088815; this version posted December 6, 2016. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Genome-Wide Association Study Reveals First Locus for Anorexia Nervosa and Metabolic Correlations Authors Duncan, E.L.* ... 210 additional authors Thornton, L.M. Hinney, A. Daly, M.J. Sullivan, P.F. Zeggini, E. Breen, G. Bulik, C.M.* * Corresponding authors Abstract Anorexia nervosa (AN) is a serious eating disorder characterized by restriction of energy intake relative to requirements, resulting in abnormally low body weight. It has a lifetime prevalence of approximately 1%, disproportionately affects females1,2, and has no well replicated evidence of effective pharmacological or psychological treatments despite high morbidity and mortality2. Twin studies support a genetic basis for the observed aggregation of AN in families3, with heritability estimates of 48%-74%4. Although initial genome-wide association studies (GWASs) were underpowered5,6, evidence suggested that signals for AN would be detected with increased power5. We present a GWAS of 3,495 AN cases and 10,982 controls with one genome-wide significant locus (index variant rs4622308, p=4.3x10-9) in a region (chr12:56,372,585- % 56,482,185) which includes six genes. The SNP-chip heritability (h"#$) of AN from these data is 0.20 (SE=0.02), suggesting that a substantial fraction of the twin-based heritability stems from common genetic variation.
    [Show full text]
  • Human Transcription Factors Responsive to Initial Reprogramming Predominantly Undergo Legitimate Reprogramming During Fbroblast Conversion to Ipscs Ricardo R
    www.nature.com/scientificreports OPEN Human transcription factors responsive to initial reprogramming predominantly undergo legitimate reprogramming during fbroblast conversion to iPSCs Ricardo R. Cevallos1, Yvonne J. K. Edwards1,2, John M. Parant3, Bradley K. Yoder2 & Kejin Hu1* The four transcription factors OCT4, SOX2, KLF4, and MYC (OSKM) together can convert human fbroblasts to induced pluripotent stem cells (iPSCs). It is, however, perplexing that they can do so only for a rare population of the starting cells with a long latency. Transcription factors (TFs) defne identities of both the starting fbroblasts and the end product, iPSCs, and are also of paramount importance for the reprogramming process. It is critical to upregulate or activate the iPSC-enriched TFs while downregulate or silence the fbroblast-enriched TFs. This report explores the initial TF responses to OSKM as the molecular underpinnings for both the potency aspects and the limitation sides of the OSKM reprogramming. The authors frst defned the TF reprogramome, i.e., the full complement of TFs to be reprogrammed. Most TFs were resistant to OSKM reprogramming at the initial stages, an observation consistent with the inefciency and long latency of iPSC reprogramming. Surprisingly, the current analyses also revealed that most of the TFs (at least 83 genes) that did respond to OSKM induction underwent legitimate reprogramming. The initial legitimate transcriptional responses of TFs to OSKM reprogramming were also observed in the reprogramming fbroblasts from a diferent individual. Such early biased legitimate reprogramming of the responsive TFs aligns well with the robustness aspect of the otherwise inefcient and stochastic OSKM reprogramming. OCT4, SOX2, KLF4, and MYC (collectively OSKM) can convert human fbroblasts into induced pluripotent stem cells (iPSCs), which are the man-made version of embryonic stem cells (ESCs)1–3.
    [Show full text]
  • EBP1 (PA2G4) Mouse Monoclonal Antibody [Clone ID: OTI1D3] 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 TA503203 EBP1 (PA2G4) Mouse Monoclonal Antibody [Clone ID: OTI1D3] Product data: Product Type: Primary Antibodies Clone Name: OTI1D3 Applications: WB Recommend Dilution: WB 1:2000 Reactivity: Human Host: Mouse Isotype: IgG1 Clonality: Monoclonal Immunogen: Full length human recombinant protein of human PA2G4 (NP_006182) produced in HEK293T cell. Formulation: PBS (PH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide. Concentration: 1 mg/ml Purification: Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G) Predicted Protein Size: 43.6 kDa Gene Name: proliferation-associated 2G4 Database Link: NP_006182 Entrez Gene 5036 Human Background: This gene encodes an RNA-binding protein that is involved in growth regulation. This protein is present in pre-ribosomal ribonucleoprotein complexes and may be involved in ribosome assembly and the regulation of intermediate and late steps of rRNA processing. This protein can interact with the cytoplasmic domain of the ErbB3 receptor and may contribute to transducing growth regulatory signals. This protein is also a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. This protein has been implicated in growth inhibition and the induction of differentiation of human cancer cells. Six pseudogenes, located on chromosomes 3, 6, 9, 18, 20 and X, have been identified. [provided by RefSeq] Synonyms: EBP1; HG4-1; p38-2G4 Protein Families: Druggable Genome, Protease, Stem cell - Pluripotency This product is to be used for laboratory only.
    [Show full text]
  • Human EBP1 / PA2G4 Protein (His Tag)
    Human EBP1 / PA2G4 Protein (His Tag) Catalog Number: 12994-H07E General Information SDS-PAGE: Gene Name Synonym: EBP1; HG4-1; p38-2G4; 38kDa; AA672939; Ebp1; Plfap Protein Construction: A DNA sequence encoding the human PA2G4 (Q9UQ80) (Ser 2-Asp 394) was expressed, with a polyhistide tag at the N-terminus. Source: Human Expression Host: E. coli QC Testing Purity: > 92 % as determined by SDS-PAGE Endotoxin: Protein Description Please contact us for more information. EBP1, also known as PA2G4, is an RNA-binding protein which belongs to Stability: the peptidase M24 family. It can be detected n several cell lines tested, including primary and transformed cell lines. EBP1 also present in pre- Samples are stable for up to twelve months from date of receipt at -70 ℃ ribosomal ribonucleoprotein complexes and may be involved in ribosome assembly and the regulation of intermediate and late steps of rRNA Predicted N terminal: Met 1 processing. This protein is a transcriptional co-repressor of androgen Molecular Mass: receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. PA2G4 can interact with the The recombinant human PA2G4 consisting of 404 amino acids and has a cytoplasmic domain of the ErbB3 receptor and may contribute to calculated molecular mass of 45.2 kDa. It migrates as an approximately 32 transducing growth regulatory signals. EBP1 has been implicated in growth KDa band in SDS-PAGE under reducing conditions. inhibition and the induction of differentiation of human cancer cells. It seems to be involved in growth regulation. EBP1 also mediates cap- Formulation: independent translation of specific viral IRESs (internal ribosomal entry site).
    [Show full text]