MED18 Antibody (R32989)

Total Page:16

File Type:pdf, Size:1020Kb

MED18 Antibody (R32989) MED18 Antibody (R32989) Catalog No. Formulation Size R32989 0.5mg/ml if reconstituted with 0.2ml sterile DI water 100 ug Bulk quote request Availability 1-3 business days Species Reactivity Human, Mouse, Rat Format Antigen affinity purified Clonality Polyclonal (rabbit origin) Isotype Rabbit IgG Purity Antigen affinity Buffer Lyophilized from 1X PBS with 2.5% BSA, 0.025% sodium azide UniProt Q9BUE0 Localization Nuclear, cytoplasmic Applications Western Blot : 0.5-1ug/ml IHC (FFPE) : 1-2ug/ml Flow cytometry : 1-3ug/million cells Direct ELISA (recombinant human protein) : 0.1-0.5ug/ml (BSA-free format available) Limitations This MED18 antibody is available for research use only. Western blot testing of human 1) A431, 2) K562, 3) U-2 OS, 4) HL60, 5) rat liver and 6) mouse kidney lysate with MED18 antibody at 0.5ug/ml. Predicted molecular weight ~24 kDa. IHC testing of FFPE human lung cancer tissue with MED18 antibody at 1ug/ml. Required HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to testing. IHC testing of FFPE human intestinal cancer tissue with MED18 antibody at 1ug/ml. Required HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to testing. IHC testing of FFPE human breast cancer tissue with MED18 antibody at 1ug/ml. Required HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to testing. IHC testing of FFPE mouse brain tissue with MED18 antibody at 1ug/ml. Required HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to testing. IHC testing of FFPE mouse small intestine tissue with MED18 antibody at 1ug/ml. Required HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to testing. IHC testing of FFPE rat brain tissue with MED18 antibody at 1ug/ml. Required HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to testing. IHC testing of FFPE rat small intestine tissue with MED18 antibody at 1ug/ml. Required HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to testing. Flow cytometry testing of human A431 cells with MED18 antibody at 1ug/million cells (blocked with goat sera); Red=cells alone, Green=isotype control, Blue= MED18 antibody. Immunofluorescent staining of FFPE human A431 cells with MED18 antibody (red) and DAPI (blue). Required HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to testing. Description MED18 is a component of the Mediator complex, which is a coactivator for DNA-binding factors that activate transcription via RNA polymerase II. Using in vitro-translated epitope-tagged proteins for protein-binding assays, it is found that MED18 directly interacted with the Mediator subunit TRFP (MED20). The MED18-TRFP heterodimer could also be coimmunoprecipitated from cotransfected insect cells. The MED18 gene was mapped to chromosome 1p35.3 based on an alignment of the MED18 sequence with the genomic sequence. Application Notes Optimal dilution of the MED18 antibody should be determined by the researcher. Immunogen A recombinant human protein corresponding to amino acids M1-M208 was used as the immunogen for the MED18 antibody. Storage After reconstitution, the MED18 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing. Ordering: Phone:858.663.9055 | Fax:1.267.821.0800 | Email:[email protected] Copyright © NSJ Bioreagents. All rights reserved.
Recommended publications
  • Proteomic Analysis of the Mediator Complex Interactome in Saccharomyces Cerevisiae Received: 26 October 2016 Henriette Uthe, Jens T
    www.nature.com/scientificreports OPEN Proteomic Analysis of the Mediator Complex Interactome in Saccharomyces cerevisiae Received: 26 October 2016 Henriette Uthe, Jens T. Vanselow & Andreas Schlosser Accepted: 25 January 2017 Here we present the most comprehensive analysis of the yeast Mediator complex interactome to date. Published: 27 February 2017 Particularly gentle cell lysis and co-immunopurification conditions allowed us to preserve even transient protein-protein interactions and to comprehensively probe the molecular environment of the Mediator complex in the cell. Metabolic 15N-labeling thereby enabled stringent discrimination between bona fide interaction partners and nonspecifically captured proteins. Our data indicates a functional role for Mediator beyond transcription initiation. We identified a large number of Mediator-interacting proteins and protein complexes, such as RNA polymerase II, general transcription factors, a large number of transcriptional activators, the SAGA complex, chromatin remodeling complexes, histone chaperones, highly acetylated histones, as well as proteins playing a role in co-transcriptional processes, such as splicing, mRNA decapping and mRNA decay. Moreover, our data provides clear evidence, that the Mediator complex interacts not only with RNA polymerase II, but also with RNA polymerases I and III, and indicates a functional role of the Mediator complex in rRNA processing and ribosome biogenesis. The Mediator complex is an essential coactivator of eukaryotic transcription. Its major function is to communi- cate regulatory signals from gene-specific transcription factors upstream of the transcription start site to RNA Polymerase II (Pol II) and to promote activator-dependent assembly and stabilization of the preinitiation complex (PIC)1–3. The yeast Mediator complex is composed of 25 subunits and forms four distinct modules: the head, the middle, and the tail module, in addition to the four-subunit CDK8 kinase module (CKM), which can reversibly associate with the 21-subunit Mediator complex.
    [Show full text]
  • Molecular and Cellular Mechanisms of the Angiogenic Effect of Poly(Methacrylic Acid-Co-Methyl Methacrylate) Beads
    Molecular and Cellular Mechanisms of the Angiogenic Effect of Poly(methacrylic acid-co-methyl methacrylate) Beads by Lindsay Elizabeth Fitzpatrick A thesis submitted in conformity with the requirements for the degree of Doctor of Philosophy Institute of Biomaterials and Biomedical Engineering University of Toronto © Copyright by Lindsay Elizabeth Fitzpatrick 2012 Molecular and Cellular Mechanisms of the Angiogenic Effect of Poly(methacrylic acid-co-methyl methacrylate) Beads Lindsay Elizabeth Fitzpatrick Doctorate of Philosophy Institute of Biomaterials and Biomedical Engineering University of Toronto 2012 Abstract Poly(methacrylic acid -co- methyl methacrylate) beads were previously shown to have a therapeutic effect on wound closure through the promotion of angiogenesis. However, it was unclear how this polymer elicited its beneficial properties. The goal of this thesis was to characterize the host response to MAA beads by identifying molecules of interest involved in MAA-mediated angiogenesis (in comparison to poly(methyl methacrylate) beads, PMMA). Using a model of diabetic wound healing and a macrophage-like cell line (dTHP-1), eight molecules of interest were identified in the host response to MAA beads. Gene and/or protein expression analysis showed that MAA beads increased the expression of Shh, IL-1β, IL-6, TNF- α and Spry2, but decreased the expression of CXCL10 and CXCL12, compared to PMMA and no beads. MAA beads also appeared to modulate the expression of OPN. In vivo, the global gene expression of OPN was increased in wounds treated with MAA beads, compared to PMMA and no beads. In contrast, dTHP-1 decreased OPN gene expression compared to PMMA and no beads, but expressed the same amount of secreted OPN, suggesting that the cells decreased the expression of the intracellular isoform of OPN.
    [Show full text]
  • 1 Mutational Heterogeneity in Cancer Akash Kumar a Dissertation
    Mutational Heterogeneity in Cancer Akash Kumar A dissertation Submitted in partial fulfillment of requirements for the degree of Doctor of Philosophy University of Washington 2014 June 5 Reading Committee: Jay Shendure Pete Nelson Mary Claire King Program Authorized to Offer Degree: Genome Sciences 1 University of Washington ABSTRACT Mutational Heterogeneity in Cancer Akash Kumar Chair of the Supervisory Committee: Associate Professor Jay Shendure Department of Genome Sciences Somatic mutation plays a key role in the formation and progression of cancer. Differences in mutation patterns likely explain much of the heterogeneity seen in prognosis and treatment response among patients. Recent advances in massively parallel sequencing have greatly expanded our capability to investigate somatic mutation. Genomic profiling of tumor biopsies could guide the administration of targeted therapeutics on the basis of the tumor’s collection of mutations. Central to the success of this approach is the general applicability of targeted therapies to a patient’s entire tumor burden. This requires a better understanding of the genomic heterogeneity present both within individual tumors (intratumoral) and amongst tumors from the same patient (intrapatient). My dissertation is broadly organized around investigating mutational heterogeneity in cancer. Three projects are discussed in detail: analysis of (1) interpatient and (2) intrapatient heterogeneity in men with disseminated prostate cancer, and (3) investigation of regional intratumoral heterogeneity in
    [Show full text]
  • Anti-MED18 Antibody (ARG59208)
    Product datasheet [email protected] ARG59208 Package: 50 μg anti-MED18 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes MED18 Tested Reactivity Hu, Ms, Rat Tested Application FACS, ICC/IF, IHC-P, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name MED18 Species Human Immunogen Recombinant protein corresponding to M1-M208 of Human MED18. Conjugation Un-conjugated Alternate Names Mediator of RNA polymerase II transcription subunit 18; p28b; Mediator complex subunit 18 Application Instructions Application table Application Dilution FACS 1:150 - 1:500 ICC/IF 1:200 - 1:1000 IHC-P 0.5 - 1 µg/ml WB 0.1 - 0.5 µg/ml Application Note IHC-P: Antigen Retrieval: Heat mediation was performed in Citrate buffer (pH 6.0) for 20 min. * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. 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. www.arigobio.com 1/4 Note For laboratory research only, not for drug, diagnostic or other use. Bioinformation Gene Symbol MED18 Gene Full Name mediator complex subunit 18 Background MED18 is a component of the Mediator complex, which is a coactivator for DNA-binding factors that activate transcription via RNA polymerase II (Sato et al., 2003 [PubMed 12584197]).[supplied by OMIM, Oct 2008] Function Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes.
    [Show full text]
  • Role of the Mediator Complex in Ethanol Tolerance in Yeast
    ROLE OF THE MEDIATOR COMPLEX IN ETHANOL TOLERANCE IN YEAST An Undergraduate Research Scholars Thesis by JACKSON VALENCIA Submitted to the Undergraduate Research Scholars program at Texas A&M University in partial fulfillment of the requirements for the designation as an UNDERGRADUATE RESEARCH SCHOLAR Approved by Research Advisor: Dr. William Park May 2018 Major: Biochemistry TABLE OF CONTENTS Page ABSTRACT ............................................................................................................................ 1 ACKNOWLEDGMENTS ........................................................................................................ 2 NOMENCLATURE................................................................................................................. 3 CHAPTER I. INTRODUCTION .................................................................................................. 5 II. MATERIALS & METHODS.................................................................................. 7 Materials ........................................................................................................... 7 Methods ............................................................................................................ 8 III. RESULTS .............................................................................................................14 Ethanol tolerance in Med8138 ± TAP ................................................................14 Growth of constructs in which Med8138-176 was replaced by SBP......................15
    [Show full text]
  • Structure and Mechanism of the RNA Polymerase II Transcription Machinery
    Downloaded from genesdev.cshlp.org on October 9, 2021 - Published by Cold Spring Harbor Laboratory Press REVIEW Structure and mechanism of the RNA polymerase II transcription machinery Allison C. Schier and Dylan J. Taatjes Department of Biochemistry, University of Colorado, Boulder, Colorado 80303, USA RNA polymerase II (Pol II) transcribes all protein-coding ingly high resolution, which has rapidly advanced under- genes and many noncoding RNAs in eukaryotic genomes. standing of the molecular basis of Pol II transcription. Although Pol II is a complex, 12-subunit enzyme, it lacks Structural biology continues to transform our under- the ability to initiate transcription and cannot consistent- standing of complex biological processes because it allows ly transcribe through long DNA sequences. To execute visualization of proteins and protein complexes at or near these essential functions, an array of proteins and protein atomic-level resolution. Combined with mutagenesis and complexes interact with Pol II to regulate its activity. In functional assays, structural data can at once establish this review, we detail the structure and mechanism of how enzymes function, justify genetic links to human dis- over a dozen factors that govern Pol II initiation (e.g., ease, and drive drug discovery. In the past few decades, TFIID, TFIIH, and Mediator), pausing, and elongation workhorse techniques such as NMR and X-ray crystallog- (e.g., DSIF, NELF, PAF, and P-TEFb). The structural basis raphy have been complemented by cryoEM, cross-linking for Pol II transcription regulation has advanced rapidly mass spectrometry (CXMS), and other methods. Recent in the past decade, largely due to technological innova- improvements in data collection and imaging technolo- tions in cryoelectron microscopy.
    [Show full text]
  • MASTERMIND-LIKE 1-Dependent Notch Target Gene Activation Requires a Sequence-Paired Site and a TATA Box
    San Jose State University SJSU ScholarWorks Master's Theses Master's Theses and Graduate Research Summer 2013 MASTERMIND-LIKE 1-Dependent Notch Target Gene Activation Requires a Sequence-Paired Site and a TATA Box Cassandra Agbayani Ramos San Jose State University Follow this and additional works at: https://scholarworks.sjsu.edu/etd_theses Recommended Citation Ramos, Cassandra Agbayani, "MASTERMIND-LIKE 1-Dependent Notch Target Gene Activation Requires a Sequence-Paired Site and a TATA Box" (2013). Master's Theses. 4360. DOI: https://doi.org/10.31979/etd.rh9z-z2ej https://scholarworks.sjsu.edu/etd_theses/4360 This Thesis is brought to you for free and open access by the Master's Theses and Graduate Research at SJSU ScholarWorks. It has been accepted for inclusion in Master's Theses by an authorized administrator of SJSU ScholarWorks. For more information, please contact [email protected]. MASTERMIND-LIKE 1-DEPENDENT NOTCH TARGET GENE ACTIVATION REQUIRES A SEQUENCE-PAIRED SITE AND A TATA BOX A Thesis Presented to The Faculty of the Department of Biological Sciences San José State University In Partial Fulfillment of the Requirements for the Degree Master of Science by Cassandra Agbayani Ramos August 2013 © 2013 Cassandra Agbayani Ramos ALL RIGHTS RESERVED The Designated Thesis Committee Approves the Thesis Titled MASTERMIND-LIKE 1-DEPENDENT NOTCH TARGET GENE ACTIVATION REQUIRES A SEQUENCE-PAIRED SITE AND A TATA BOX by Cassandra Agbayani Ramos APPROVED FOR THE DEPARTMENT OF BIOLOGICAL SCIENCES SAN JOSÉ STATE UNIVERSITY August 2013 Dr. Brandon White Department of Biological Sciences Dr. Elizabeth Skovran Department of Biological Sciences Dr. Brooke Lustig Department of Chemistry ABSTRACT MASTERMIND-LIKE 1-DEPENDENT NOTCH TARGET GENE ACTIVATION REQUIRES A SEQUENCE-PAIRED SITE AND A TATA BOX by Cassandra Agbayani Ramos Notch signaling plays an important role in mammalian cellular proliferation, apoptosis, and differentiation.
    [Show full text]
  • Microarray Bioinformatics and Its Applications to Clinical Research
    Microarray Bioinformatics and Its Applications to Clinical Research A dissertation presented to the School of Electrical and Information Engineering of the University of Sydney in fulfillment of the requirements for the degree of Doctor of Philosophy i JLI ··_L - -> ...·. ...,. by Ilene Y. Chen Acknowledgment This thesis owes its existence to the mercy, support and inspiration of many people. In the first place, having suffering from adult-onset asthma, interstitial cystitis and cold agglutinin disease, I would like to express my deepest sense of appreciation and gratitude to Professors Hong Yan and David Levy for harbouring me these last three years and providing me a place at the University of Sydney to pursue a very meaningful course of research. I am also indebted to Dr. Craig Jin, who has been a source of enthusiasm and encouragement on my research over many years. In the second place, for contexts concerning biological and medical aspects covered in this thesis, I am very indebted to Dr. Ling-Hong Tseng, Dr. Shian-Sehn Shie, Dr. Wen-Hung Chung and Professor Chyi-Long Lee at Change Gung Memorial Hospital and University of Chang Gung School of Medicine (Taoyuan, Taiwan) as well as Professor Keith Lloyd at University of Alabama School of Medicine (AL, USA). All of them have contributed substantially to this work. In the third place, I would like to thank Mrs. Inge Rogers and Mr. William Ballinger for their helpful comments and suggestions for the writing of my papers and thesis. In the fourth place, I would like to thank my swim coach, Hirota Homma.
    [Show full text]
  • A Noncoding RNA Gene on Chromosome 10P15. 3 May Function
    BMC Molecular Biology BioMed Central Research article Open Access A noncoding RNA gene on chromosome 10p15.3 may function upstream of hTERT † † Norimasa Miura* 1,ReinaSato1, Tomoe Tsukamoto1,MikaShimizu1, Hiroko Kabashima1,MihoTakeda1, Shunsaku Takahashi1, Tomomi Harada1,JamesEWest2, Harry Drabkin3,JoseEMejia4, Goshi Shiota5, Yoshikazu Murawaki6, Arvind Virmani7, Adi F Gazdar7, Mitsuo Oshimura8 and Junichi Hasegawa1 Address: 1Division of Pharmacotherapeutics, Department of Pathophysiological and Therapeutic Science, Faculty of Medicine, Tottori University, Yonago, Tottori 683-8503, Japan, 2Department of S/M Cardiovascular Pulmonary Research, School of Medicine, Colorado University at Denver and Health Sciences Center, Denver, Colorado 80262, USA, 3Department of S/M Medical Oncology, School of Medicine, Colorado University at Denver and Health Sciences Center, Denver, Colorado 80262, USA, 4Development of human artificial chromosomes for gene therapy, Weatherall Institute of Molecular Medicine, Medical Science Division, Oxford University, Oxford, OX3 9DU, UK, 5Division of Molecular and Genetic Medicine, Department of Genetic Medicine and Regenerative Therapeutics, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Sciences, Tottori University, Yonago, Tottori 683-8503, Japan, 6Division of Medicine and Clinical Science, Department of Multidisciplinary Internal Medicine, School of Medicine, Tottori University Faculty of Medicine, Yonago, Tottori 683- 8504, Japan, 7Hamon Center for Therapeutic Oncology Research and
    [Show full text]
  • Coexpression Networks Based on Natural Variation in Human Gene Expression at Baseline and Under Stress
    University of Pennsylvania ScholarlyCommons Publicly Accessible Penn Dissertations Fall 2010 Coexpression Networks Based on Natural Variation in Human Gene Expression at Baseline and Under Stress Renuka Nayak University of Pennsylvania, [email protected] Follow this and additional works at: https://repository.upenn.edu/edissertations Part of the Computational Biology Commons, and the Genomics Commons Recommended Citation Nayak, Renuka, "Coexpression Networks Based on Natural Variation in Human Gene Expression at Baseline and Under Stress" (2010). Publicly Accessible Penn Dissertations. 1559. https://repository.upenn.edu/edissertations/1559 This paper is posted at ScholarlyCommons. https://repository.upenn.edu/edissertations/1559 For more information, please contact [email protected]. Coexpression Networks Based on Natural Variation in Human Gene Expression at Baseline and Under Stress Abstract Genes interact in networks to orchestrate cellular processes. Here, we used coexpression networks based on natural variation in gene expression to study the functions and interactions of human genes. We asked how these networks change in response to stress. First, we studied human coexpression networks at baseline. We constructed networks by identifying correlations in expression levels of 8.9 million gene pairs in immortalized B cells from 295 individuals comprising three independent samples. The resulting networks allowed us to infer interactions between biological processes. We used the network to predict the functions of poorly-characterized human genes, and provided some experimental support. Examining genes implicated in disease, we found that IFIH1, a diabetes susceptibility gene, interacts with YES1, which affects glucose transport. Genes predisposing to the same diseases are clustered non-randomly in the network, suggesting that the network may be used to identify candidate genes that influence disease susceptibility.
    [Show full text]
  • Table S1. 103 Ferroptosis-Related Genes Retrieved from the Genecards
    Table S1. 103 ferroptosis-related genes retrieved from the GeneCards. Gene Symbol Description Category GPX4 Glutathione Peroxidase 4 Protein Coding AIFM2 Apoptosis Inducing Factor Mitochondria Associated 2 Protein Coding TP53 Tumor Protein P53 Protein Coding ACSL4 Acyl-CoA Synthetase Long Chain Family Member 4 Protein Coding SLC7A11 Solute Carrier Family 7 Member 11 Protein Coding VDAC2 Voltage Dependent Anion Channel 2 Protein Coding VDAC3 Voltage Dependent Anion Channel 3 Protein Coding ATG5 Autophagy Related 5 Protein Coding ATG7 Autophagy Related 7 Protein Coding NCOA4 Nuclear Receptor Coactivator 4 Protein Coding HMOX1 Heme Oxygenase 1 Protein Coding SLC3A2 Solute Carrier Family 3 Member 2 Protein Coding ALOX15 Arachidonate 15-Lipoxygenase Protein Coding BECN1 Beclin 1 Protein Coding PRKAA1 Protein Kinase AMP-Activated Catalytic Subunit Alpha 1 Protein Coding SAT1 Spermidine/Spermine N1-Acetyltransferase 1 Protein Coding NF2 Neurofibromin 2 Protein Coding YAP1 Yes1 Associated Transcriptional Regulator Protein Coding FTH1 Ferritin Heavy Chain 1 Protein Coding TF Transferrin Protein Coding TFRC Transferrin Receptor Protein Coding FTL Ferritin Light Chain Protein Coding CYBB Cytochrome B-245 Beta Chain Protein Coding GSS Glutathione Synthetase Protein Coding CP Ceruloplasmin Protein Coding PRNP Prion Protein Protein Coding SLC11A2 Solute Carrier Family 11 Member 2 Protein Coding SLC40A1 Solute Carrier Family 40 Member 1 Protein Coding STEAP3 STEAP3 Metalloreductase Protein Coding ACSL1 Acyl-CoA Synthetase Long Chain Family Member 1 Protein
    [Show full text]
  • Datasheet A10600-2 Anti-MED18 Antibody
    Product datasheet Anti-MED18 Antibody Catalog Number: A10600-2 BOSTER BIOLOGICAL TECHNOLOGY Special NO.1, International Enterprise Center, 2nd Guanshan Road, Wuhan, China Web: www.boster.com.cn Phone: +86 27 67845390 Fax: +86 27 67845390 Email: [email protected] Basic Information Product Name Anti-MED18 Antibody Gene Name MED18 Source Rabbit IgG Species Reactivity human,mouse,rat Tested Application WB,IHC-P,FCM,Direct ELISA,ICC/IF Contents 500ug/ml antibody with PBS ,0.02% NaN3 , 1mg BSA and 50% glycerol. Immunogen E. coli-derived human MED18 recombinant protein (Position: M1-M208). Purification Immunogen affinity purified. Observed MW 24KD Dilution Ratios Western blot: 1:500-2000 Immunohistochemistry in paraffin section: 1:50-400 Flow Cytometry: 1-3μg/1x106 cells Direct ELISA: 1:100-1000 Immunocytochemistry/Immunofluorescence (ICC/IF): 1:50-400 (Boiling the paraffin sections in 10mM citrate buffer,pH6.0,or PH8.0 EDTA repair liquid for 20 mins is required for the staining of formalin/paraffin sections.) Optimal working dilutions must be determined by end user. Storage 12 months from date of receipt,-20℃ as supplied.6 months 2 to 8℃ after reconstitution. Avoid repeated freezing and thawing Background Information MED18 is a component of the Mediator complex, which is a coactivator for DNA-binding factors that activate transcription via RNA polymerase II. Using in vitro-translated epitope-tagged proteins for protein-binding assays, it is found that MED18 directly interacted with the Mediator subunit TRFP (MED20). The MED18-TRFP heterodimer could also be coimmunoprecipitated from cotransfected insect cells. The MED18 gene was mapped to chromosome 1p35.3 based on an alignment of the MED18 sequence with the genomic sequence.
    [Show full text]