MED26 Antibody

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Product Datasheet MED26 Antibody Catalog No: #33633 Package Size: #33633-1 50ul #33633-2 100ul Orders: [email protected] Support: [email protected] Description Product Name MED26 Antibody Host Species Rabbit Clonality Polyclonal Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. Applications WB Species Reactivity Hu Ms Specificity The antibody detects endogenous levels of total MED26 protein. Immunogen Type Peptide Immunogen Description Synthesized peptide derived from N-terminal of human MED26. Target Name MED26 Other Names ARC70; CRSP complex 7; CRSP70; MED26; activator-recruited cofactor 70 kDa component Accession No. Swiss-Prot: O95402NCBI Gene ID: 9441 SDS-PAGE MW 65kd Concentration 1.0mg/ml Formulation Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Storage Store at -20°C Application Details Western blotting: 1:500~1:3000 Images Western blot analysis of extracts from LOVO cells, using MED26 antibody #33633. Background Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 1 functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Ryu S., Nature 397:446-450(1999). Naeaer A.M., Nature 398:828-832(1999). Sato S., Mol. Cell 14:685-691(2004). Note: This product is for in vitro research use only and is not intended for use in humans or animals. Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 2.

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The Cyclin-Dependent Kinase 8 Module Sterically Blocks Mediator Interactions with RNA Polymerase II
The cyclin-dependent kinase 8 module sterically blocks Mediator interactions with RNA polymerase II Hans Elmlund*†, Vera Baraznenok‡, Martin Lindahl†, Camilla O. Samuelsen§, Philip J. B. Koeck*¶, Steen Holmberg§, Hans Hebert*ʈ, and Claes M. Gustafsson‡ʈ *Department of Biosciences and Nutrition, Karolinska Institutet and School of Technology and Health, Royal Institute of Technology, Novum, SE-141 87 Huddinge, Sweden; †Department of Molecular Biophysics, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden; ‡Division of Metabolic Diseases, Karolinska Institutet, Novum, SE-141 86 Huddinge, Sweden; §Department of Genetics, Institute of Molecular Biology, Oester Farimagsgade 2A, DK-1353 Copenhagen K, Denmark; and ¶University College of Southern Stockholm, SE-141 57 Huddinge, Sweden Communicated by Roger D. Kornberg, Stanford University School of Medicine, Stanford, CA, August 28, 2006 (received for review February 21, 2006) CDK8 (cyclin-dependent kinase 8), along with CycC, Med12, and Here, we use the S. pombe system to investigate the molecular Med13, form a repressive module (the Cdk8 module) that prevents basis for the distinct functional properties of S and L Mediator. RNA polymerase II (pol II) interactions with Mediator. Here, we We find that the Cdk8 module binds to the pol II-binding cleft report that the ability of the Cdk8 module to prevent pol II of Mediator, where it sterically blocks interactions with the interactions is independent of the Cdk8-dependent kinase activity. polymerase. In contrast to earlier assumptions, the Cdk8 kinase We use electron microscopy and single-particle reconstruction to activity is dispensable for negative regulation of pol II interac- demonstrate that the Cdk8 module forms a distinct structural tions with Mediator.
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Functional Diversification of the Nleg Effector Family in Enterohemorrhagic Escherichia Coli
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FBXL19 Recruits CDK-Mediator to Cpg Islands of Developmental Genes Priming Them for Activation During Lineage Commitment
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The Mammalian Mediator Complex
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector FEBS Letters 579 (2005) 904–908 FEBS 29061 Minireview The mammalian Mediator complex Joan Weliky Conawaya,b,c,*, Laurence Florensa, Shigeo Satoa, Chieri Tomomori-Satoa, Tari J. Parmelya, Tingting Yaoa, Selene K. Swansona, Charles A.S. Banksa, Michael P. Washburna, Ronald C. Conawaya,b a Stowers Institute for Medical Research, Kansas City, MO 64110, USA b Department of Biochemistry and Molecular Biology, Kansas University Medical Center, Kansas City, KS 66160, USA c Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73190, USA Received 25 October 2004; accepted 2 November 2004 Available online 24 November 2004 Edited by Gunnar von Heijne and Anders Liljas expressed in eukaryotes from yeast to man, is composed of Abstract The multiprotein Mediator (Med) complex is an evo- lutionarily conserved transcriptional regulator that plays impor- more than twenty subunits and has been named Mediator tant roles in activation and repression of RNA polymerase II (Med) for its role in mediating transcriptional signals from transcription. Prior studies identiﬁed a set of more than twenty DNA binding transcription factors bound at upstream pro- distinct polypeptides that compose the Saccharomyces cerevisiae moter elements and enhancers to RNA polymerase II and Mediator. Here we discuss eﬀorts to characterize the subunit the general initiation factors bound at the core promoter sur- composition and associated activities of the mammalian Med rounding the transcriptional start site. complex. Ó 2004 Federation of European Biochemical Societies. Published by Elsevier B.V.
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Master Thesis-Updated
POLR2A/RPB1 SUBUNIT OF RNA POLYMERASE II INTERACTS WITH NTD-MED14 CONTAINING CORE MEDIATOR COMPLEX TO FACILITATE BASAL AND ACTIVATOR DRIVEN TRANSCRIPTION A THESIS SUBMITTED TO THE GRADUATE SCHOOL OF ENGINEERING AND SCIENCE OF BILKENT UNIVERSITY IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF MASTER OF SCIENCE IN MOLECULAR BIOLOGY AND GENETICS By Javaid Jabbar June 2020 POLR2A/RPB1 SUBUNIT OF RNA POLYMERASE II INTERACTS WITH NTD- MED14 CONTAINING CORE MEDIATOR COMPLEX TO FACILITATE BASAL AND ACTIVATOR DRIVEN TRANSCRIPTION By Javaid Jabbar June 2020 We certify that we have read this thesis and in our opinion it is fully adequate, in scope and in quality, as a thesis for the degree of Master of Science. Murat Alper Cevher (Advisor) Serkan İsmail Göktuna Ayşe Elif Erson Bensan Approved for Graduate School of Engineering and Science: Ezhan Karaşan Director of Graduate School of Engineering and Science ii ABSTRACT POLR2A/RPB1 SUBUNIT OF RNA POLYMERASE II INTERACTS WITH NTD- MED14 CONTAINING CORE MEDIATOR COMPLEX TO FACILITATE BASAL AND ACTIVATOR DRIVEN TRANSCRIPTION Javaid Jabbar M.Sc in Molecular Biology and Genetics Advisor: Murat Alper Cevher June 2020 The Metazoan Mediator is a 2-MDa protein complex that consist of 30 subunits, most of which are evolutionarily conserved from yeast to humans8. The maintenance and regulation of the cell is dependent on spatiotemporal control of RNA polymerase II (Pol II) mediated transcription as a result of intrinsic and extrinsic signals. Perturbations caused by the environment and genetics can alter the fate of the cells and can lead to many diseases such as cancer.
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MED16 and MED23 of Mediator Are Coactivators of Lipopolysaccharide- and Heat-Shock-Induced Transcriptional Activators
MED16 and MED23 of Mediator are coactivators of lipopolysaccharide- and heat-shock-induced transcriptional activators Tae Whan Kim*, Yong-Jae Kwon*, Jung Mo Kim*†, Young-Hwa Song‡, Se Nyun Kim‡, and Young-Joon Kim*§ *Department of Biochemistry, Yonsei University, Seoul 120-749, South Korea; and ‡Digital Genomics, Seoul 120-749, South Korea Edited by Roger D. Kornberg, Stanford University School of Medicine, Stanford, CA, and approved June 21, 2004 (received for review March 22, 2004) Transcriptional activators interact with diverse proteins and recruit To understand the specificity of the Mediator complex in tran- transcriptional machinery to the activated promoter. Recruitment scriptional activation, we examined the effect of depleting individ- of the Mediator complex by transcriptional activators is usually the ual Mediator subunits one by one by RNA interference (RNAi) on key step in transcriptional activation. However, it is unclear how transcriptional activation in response to natural signals (LPS and Mediator recognizes different types of activator proteins. To sys- heat shock) or to the overexpression of synthetic activator proteins tematically identify the subunits responsible for the signal- and (DIF or HSF). We found that MED16 and MED23, of the 23 activator-speciﬁc functions of Mediator in Drosophila melano- Mediator proteins tested, were required for DIF- and HSF- gaster, each Mediator subunit was depleted by RNA interference, mediated transcriptional activation, respectively. GST pull-down and its effect on transcriptional activation of endogenous as well assays revealed that DIF and HSF fusion proteins bound to as synthetic promoters was examined. The depletion of some different Mediator proteins. In particular DIF was found to bind Mediator gene products caused general transcriptional defects, specifically to MED16.
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Structure of the Mammalian Mediator
bioRxiv preprint doi: https://doi.org/10.1101/2020.10.05.326918; this version posted October 6, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Structure of the Mammalian Mediator Haiyan Zhao1.#, Natalie Young1,#, Jens Kalchschmidt2,#, Jenna Lieberman2, Laila El Khattabi3, Rafael Casellas2,4 and Francisco J. Asturias1,* 1Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical School, Aurora CO 80045, USA 2Lymphocyte Nuclear Biology, NIAMS, NIH, Bethesda, MD 20892, USA 3Institut Cochin Laboratoire de Cytogénétique Constitutionnelle Pré et Post Natale, 75014 Paris France 4Center for Cancer Research, NCI, NIH, Bethesda, MD 20892, USA #,*These authors contributed equally to this work *Correspondence should be addressed to F.J.A. ([email protected]) 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.10.05.326918; this version posted October 6, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. The Mediator complex plays an essential and multi-faceted role in regulation of RNA polymerase II transcription in all eukaryotes. Structural analysis of yeast Mediator has provided an understanding of the conserved core of the complex and its interaction with RNA polymerase II but failed to reveal the structure of the Tail module that contains most subunits targeted by activators and repressors. Here we present a molecular model of mammalian (Mus musculus) Mediator, derived from a 4.0 Å resolution cryo-EM map of the complex.
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Structure of Mammalian Mediator Complex Reveals Tail Module Architecture and Interaction with a Conserved Core
ARTICLE https://doi.org/10.1038/s41467-021-21601-w OPEN Structure of mammalian Mediator complex reveals Tail module architecture and interaction with a conserved core Haiyan Zhao 1,5, Natalie Young1,5, Jens Kalchschmidt2,5, Jenna Lieberman2, Laila El Khattabi3, ✉ Rafael Casellas2,4 & Francisco J. Asturias1 1234567890():,; The Mediator complex plays an essential and multi-faceted role in regulation of RNA poly- merase II transcription in all eukaryotes. Structural analysis of yeast Mediator has provided an understanding of the conserved core of the complex and its interaction with RNA polymerase II but failed to reveal the structure of the Tail module that contains most subunits targeted by activators and repressors. Here we present a molecular model of mammalian (Mus musculus) Mediator, derived from a 4.0 Å resolution cryo-EM map of the complex. The mammalian Mediator structure reveals that the previously unresolved Tail module, which includes a number of metazoan speciﬁc subunits, interacts extensively with core Mediator and has the potential to inﬂuence its conformation and interactions. 1 Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical School, Aurora, CO, USA. 2 Lymphocyte Nuclear Biology, NIAMS, NIH, Bethesda, MD, USA. 3 Institut Cochin Laboratoire de Cytogénétique Constitutionnelle Pré et Post Natale, Paris, France. 4 Center for Cancer ✉ Research, NCI, NIH, Bethesda, MD, USA. 5These authors contributed equally: Haiyan Zhao, Natalie Young, Jens Kalchschmidt. email: Francisco. [email protected]
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Technic Al Data Sheet
PRODUCT NAME Med26 polyclonal antibody Other names: Transcriptional coactivator CRSP70, ARC70 Cat. No. C15410073 (pAb-073-050) Type: Polyclonal Size: 50 μg/ 25 μl Lot #: 001 Source: Rabbit Concentration: 2.0 μg/μl Description: Polyclonal antibody raised in rabbit against human Med26 (Mediator of RNA polymerase II transcription subunit 26), using a KLH-conjugated synthetic peptide containing a sequence from the N-terminal part of the protein. TECHNICAL DATA SHEET DATA TECHNICAL Specificity: Human: positive Other species: not tested Applications Suggested dilution References Western blotting 1:1,000 Fig 1 Purity: Protein G purified, polyclonal antibody in PBS containing 0.05% azide and 0.05% ProClin 300. Storage: Store at -20°C; for long storage, store at -80°C. Avoid multiple freeze-thaw cycles. Precautions: This product is for research use only. Not for use in diagnostic or therapeutic procedures. Last data sheet update: March 17, 2010 Target description Med26 (UniProt/Swiss-Prot entry O95402) is a component of the Mediator complex, a coactivator involved in the regulation of transcription of nearly all RNA polymerase II-dependent genes. The Mediator complex forms a bridge between gene-specific regulatory proteins and the RNA polymerase II transcription machinery. It is recruited to promoters by direct interactions with these regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and general transcription factors. Europe - Diagenode s.a. / [email protected] / [email protected] // North America - Diagenode Inc. / [email protected] / [email protected] www.diagenode.com TECHNICAL DATA SHEET DATA TECHNICAL Figure 1 Western blot analysis using the Diagenode antibody directed against Med26 Western blot was performed on nuclear extracts from HeLa cells (20 μg) with the Diagenode antibody against human Med26 (Cat.
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Mutual Exclusivity of MED12/MED12L, MED13/13L, and CDK8/19 Paralogs Revealed Within the CDK-Mediator Kinase Module Danette L
ics om & B te i ro o P in f f o o r l m a Journal of a n t r i Daniels et al., J Proteomics Bioinform 2013, S2 c u s o J DOI: 10.4172/jpb.S2-004 ISSN: 0974-276X Proteomics & Bioinformatics Research Article Article OpenOpen Access Access Mutual Exclusivity of MED12/MED12L, MED13/13L, and CDK8/19 Paralogs Revealed within the CDK-Mediator Kinase Module Danette L. Daniels1*, Michael Ford2*, Marie K. Schwinn1, Hélène Benink1, Matthew D. Galbraith3,4, Ravi Amunugama2, Richard Jones2, David Allen2, Noriko Okazaki5, Hisashi Yamakawa5, Futaba Miki5, Takahiro Nagase5, Joaquín M. Espinosa3,4, and Marjeta Urh1 1Promega Corporation, 2800 Woods Hollow Road, Madison, WI 53711, USA 2MSBioworks LLC, 3950 Varsity Drive, Ann Arbor, MI 48108, USA 3Howard Hughes Medical Institute, USA 4Department of Molecular, Cellular and Developmental Biology, University of Colorado at Boulder, Boulder, Colorado, 80309, USA 5Kazusa DNA Research Institute, Kisarazu 292-0818, Japan Abstract The macromolecular complex Mediator plays important roles in regulation of RNA Polymerase II (RNAPII) activity by DNA-binding proteins, non-coding RNAs, and chromatin. Structural and biochemical studies have shown that human Mediator exists in two forms; a core complex of 26 proteins, termed Mediator, and a larger complex containing the CDK8 kinase module, termed CDK-Mediator. Interestingly, 3 subunits of the kinase module have undergone independent gene duplications in vertebrates to generate the paralog pairs MED12/MED12L, MED13/ MED13L, and CDK8/CDK19. Each has been shown to interact with Mediator, yet clearly defining the composition of CDK kinase module has been challenging due to the large size (~600 kD), the similarities between paralogs, and potential combinatorial nature of complexes.
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