Brpf1a (His) (Bromodomain and PHD Finger-Containing Protein 1, Peregrin, BR140, (Isoform 1))

Total Page:16

File Type:pdf, Size:1020Kb

Brpf1a (His) (Bromodomain and PHD Finger-Containing Protein 1, Peregrin, BR140, (Isoform 1)) BRPF1a (His) (Bromodomain and PHD finger-containing protein 1, Peregrin, BR140, (Isoform 1)) CATALOG NO.: RD-11-221 LOT NO.: DESCRIPTION: Human recombinant BRPF1a bromodomain (residues 627-746; Genbank Accession # NM_001003694; MW = 16.9 kDa) expressed in E. coli with an N-terminal His-tag. Relative to BRPF1b (BRPF1 Isoform 2), the BRPF1a bromodomain contains a six amino acid insert, EVTELD, after residue 660. A scaffolding component of the MOZ/MORF histone acetyltransferase (HAT) complex 1 and also an HBO1- BRPF1 HAT complex 2, native BRPF1a contains, in addition to its acetyllysine-binding bromodomain, two other presumed histone/chromatin binding domains, a PWWP domain 3,4 and a PHD zinc-finger. The BRPF1 bromodomain binds multiple acetyllysines in histone N-terminal tails, with preference for H2AK5Ac, H4K12Ac and H3K14Ac 5. BRPF1 forms a complex with MOZ-TIF2 fusion proteins formed due to chromosomal translocations associated with acute myeloid leukemia (AML) 6. Depletion of BRPF1 interferes with the MOZ- TIF2-driven transformation and upregulation of HOX gene expression, suggesting that BRPF1 could be a therapeutic target for AML 6. PURITY: >95% by SDS-PAGE SUPPLIED AS: _ µg/µL in 50 mM Tris HCl, pH 7.5, 500 mM NaCl, 1 mM TCEP, 10% glycerol as determined by OD 280. STORAGE: -70°C. Thaw quickly and store on ice before use. The remaining, unused, undiluted protein should be snap frozen, for example in a dry/ice ethanol bath or liquid nitrogen. Minimize freeze/thaws if possible, but very low volume aliquots (<5 µl) or storage of diluted protein is not recommended. REFERENCES: 1) M. Ullah et al. Mol. Cell. Biol. 2008 28 6828: 2) M. Lalonde et al. Genes Dev. 2013 27 2009; 3) A. Vezzoli et al. Nat. Struct. Mol. Biol. 2010 17 617; 4) H. Wu et al. PLoS One 2011 6 e18919; 5) A. Poplawski et al. J. Mol. Biol. 2014 426 1661; 6) H. Shima et al. Int. J. Hematol. 2014 99 21 Coomassie blue - stained SDS-PAGE (4-12% acrylamide) of 4 µg of RBC BRPF1a (His). MW markers (left) are, from top, 220, 160, 120, 100, 90, 80, 70, 60, 50 , 40, 30, 25, 20 , 15 &10 kDa. This product is NOT intended for therapeutic or diagnostic use in animals or in humans. Reaction Biology Corp., One Great Valley Parkway, Malvern PA 19355 Tel. 877-347-2368 Fax 610-722-0246 [email protected] www.reactionbiology.com .
Recommended publications
  • Bromodomain Factors of BET Family Are New Essential Actors Of
    Bromodomain factors of BET family are new essential actors of pericentric heterochromatin transcriptional activation in response to heat shock Edwige Col, Neda Hoghoughi, Solenne Dufour, Jessica Penin, Sivan Koskas, Virginie Faure, Maria Ouzounova, Hector Hernandez-Vargash, Nicolas Reynoird, Sylvain Daujat, et al. To cite this version: Edwige Col, Neda Hoghoughi, Solenne Dufour, Jessica Penin, Sivan Koskas, et al.. Bromodomain factors of BET family are new essential actors of pericentric heterochromatin transcriptional acti- vation in response to heat shock. Scientific Reports, Nature Publishing Group, 2017, 7, pp.5418. 10.1038/s41598-017-05343-8. hal-02989794 HAL Id: hal-02989794 https://hal.archives-ouvertes.fr/hal-02989794 Submitted on 5 Nov 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. www.nature.com/scientificreports OPEN Bromodomain factors of BET family are new essential actors of pericentric heterochromatin Received: 5 August 2016 Accepted: 30 May 2017 transcriptional activation in Published: xx xx xxxx response to heat shock Edwige Col1, Neda Hoghoughi1, Solenne Dufour1, Jessica Penin1, Sivan Koskas1, Virginie Faure1, Maria Ouzounova2, Hector Hernandez-Vargash2, Nicolas Reynoird1, Sylvain Daujat4, Eric Folco1, Marc Vigneron3, Robert Schneider4,5, André Verdel1, Saadi Khochbin1, Zdenko Herceg2, Cécile Caron1 & Claire Vourc’h1 The heat shock response is characterized by the transcriptional activation of both hsp genes and noncoding and repeated satellite III DNA sequences located at pericentric heterochromatin.
    [Show full text]
  • Table 2. Functional Classification of Genes Differentially Regulated After HOXB4 Inactivation in HSC/Hpcs
    Table 2. Functional classification of genes differentially regulated after HOXB4 inactivation in HSC/HPCs Symbol Gene description Fold-change (mean ± SD) Signal transduction Adam8 A disintegrin and metalloprotease domain 8 1.91 ± 0.51 Arl4 ADP-ribosylation factor-like 4 - 1.80 ± 0.40 Dusp6 Dual specificity phosphatase 6 (Mkp3) - 2.30 ± 0.46 Ksr1 Kinase suppressor of ras 1 1.92 ± 0.42 Lyst Lysosomal trafficking regulator 1.89 ± 0.34 Mapk1ip1 Mitogen activated protein kinase 1 interacting protein 1 1.84 ± 0.22 Narf* Nuclear prelamin A recognition factor 2.12 ± 0.04 Plekha2 Pleckstrin homology domain-containing. family A. (phosphoinosite 2.15 ± 0.22 binding specific) member 2 Ptp4a2 Protein tyrosine phosphatase 4a2 - 2.04 ± 0.94 Rasa2* RAS p21 activator protein 2 - 2.80 ± 0.13 Rassf4 RAS association (RalGDS/AF-6) domain family 4 3.44 ± 2.56 Rgs18 Regulator of G-protein signaling - 1.93 ± 0.57 Rrad Ras-related associated with diabetes 1.81 ± 0.73 Sh3kbp1 SH3 domain kinase bindings protein 1 - 2.19 ± 0.53 Senp2 SUMO/sentrin specific protease 2 - 1.97 ± 0.49 Socs2 Suppressor of cytokine signaling 2 - 2.82 ± 0.85 Socs5 Suppressor of cytokine signaling 5 2.13 ± 0.08 Socs6 Suppressor of cytokine signaling 6 - 2.18 ± 0.38 Spry1 Sprouty 1 - 2.69 ± 0.19 Sos1 Son of sevenless homolog 1 (Drosophila) 2.16 ± 0.71 Ywhag 3-monooxygenase/tryptophan 5- monooxygenase activation protein. - 2.37 ± 1.42 gamma polypeptide Zfyve21 Zinc finger. FYVE domain containing 21 1.93 ± 0.57 Ligands and receptors Bambi BMP and activin membrane-bound inhibitor - 2.94 ± 0.62
    [Show full text]
  • Functional Roles of Bromodomain Proteins in Cancer
    cancers Review Functional Roles of Bromodomain Proteins in Cancer Samuel P. Boyson 1,2, Cong Gao 3, Kathleen Quinn 2,3, Joseph Boyd 3, Hana Paculova 3 , Seth Frietze 3,4,* and Karen C. Glass 1,2,4,* 1 Department of Pharmaceutical Sciences, Albany College of Pharmacy and Health Sciences, Colchester, VT 05446, USA; [email protected] 2 Department of Pharmacology, Larner College of Medicine, University of Vermont, Burlington, VT 05405, USA; [email protected] 3 Department of Biomedical and Health Sciences, University of Vermont, Burlington, VT 05405, USA; [email protected] (C.G.); [email protected] (J.B.); [email protected] (H.P.) 4 University of Vermont Cancer Center, Burlington, VT 05405, USA * Correspondence: [email protected] (S.F.); [email protected] (K.C.G.) Simple Summary: This review provides an in depth analysis of the role of bromodomain-containing proteins in cancer development. As readers of acetylated lysine on nucleosomal histones, bromod- omain proteins are poised to activate gene expression, and often promote cancer progression. We examined changes in gene expression patterns that are observed in bromodomain-containing proteins and associated with specific cancer types. We also mapped the protein–protein interaction network for the human bromodomain-containing proteins, discuss the cellular roles of these epigenetic regu- lators as part of nine different functional groups, and identify bromodomain-specific mechanisms in cancer development. Lastly, we summarize emerging strategies to target bromodomain proteins in cancer therapy, including those that may be essential for overcoming resistance. Overall, this review provides a timely discussion of the different mechanisms of bromodomain-containing pro- Citation: Boyson, S.P.; Gao, C.; teins in cancer, and an updated assessment of their utility as a therapeutic target for a variety of Quinn, K.; Boyd, J.; Paculova, H.; cancer subtypes.
    [Show full text]
  • Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin
    cells Review Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin Agnieszka Bochy ´nska,Juliane Lüscher-Firzlaff and Bernhard Lüscher * ID Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University, Pauwelsstrasse 30, 52057 Aachen, Germany; [email protected] (A.B.); jluescher-fi[email protected] (J.L.-F.) * Correspondence: [email protected]; Tel.: +49-241-8088850; Fax: +49-241-8082427 Received: 18 January 2018; Accepted: 27 February 2018; Published: 2 March 2018 Abstract: Regulation of gene expression is achieved by sequence-specific transcriptional regulators, which convey the information that is contained in the sequence of DNA into RNA polymerase activity. This is achieved by the recruitment of transcriptional co-factors. One of the consequences of co-factor recruitment is the control of specific properties of nucleosomes, the basic units of chromatin, and their protein components, the core histones. The main principles are to regulate the position and the characteristics of nucleosomes. The latter includes modulating the composition of core histones and their variants that are integrated into nucleosomes, and the post-translational modification of these histones referred to as histone marks. One of these marks is the methylation of lysine 4 of the core histone H3 (H3K4). While mono-methylation of H3K4 (H3K4me1) is located preferentially at active enhancers, tri-methylation (H3K4me3) is a mark found at open and potentially active promoters. Thus, H3K4 methylation is typically associated with gene transcription. The class 2 lysine methyltransferases (KMTs) are the main enzymes that methylate H3K4. KMT2 enzymes function in complexes that contain a necessary core complex composed of WDR5, RBBP5, ASH2L, and DPY30, the so-called WRAD complex.
    [Show full text]
  • Histone-Binding of DPF2 Mediates Its Repressive Role in Myeloid Differentiation
    Histone-binding of DPF2 mediates its repressive role in myeloid differentiation Ferdinand M. Hubera,1, Sarah M. Greenblattb,1, Andrew M. Davenporta,1, Concepcion Martinezb,YeXub,LyP.Vuc, Stephen D. Nimerb,2, and André Hoelza,2 aDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125; bSylvester Comprehensive Cancer Center, University of Miami Miller School of Medicine, Miami, FL 33136; and cMolecular Pharmacology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065 Edited by Douglas C. Rees, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA, and approved April 26, 2017 (received for review January 6, 2017) Double plant homeodomain finger 2 (DPF2) is a highly evolution- RUNX1 form a methylation-dependent repressive complex in arily conserved member of the d4 protein family that is ubiqui- AML, although it remains unclear whether the two proteins bind tously expressed in human tissues and was recently shown to each other directly or act concertedly as part of a larger complex. inhibit the myeloid differentiation of hematopoietic stem/progen- Here, we present the crystal structure of the human DPF2 itor and acute myelogenous leukemia cells. Here, we present the tandem PHD finger domain at a 1.6-Å resolution. We demon- crystal structure of the tandem plant homeodomain finger domain strate that the DPF2 tandem PHD finger domain binds acetylated of human DPF2 at 1.6-Å resolution. We show that DPF2 interacts H3 and H4 histone tails, identify the primary determinants of with the acetylated tails of both histones 3 and 4 via bipartite histone recognition, and confirm these interactions in vivo.
    [Show full text]
  • Function of Bromodomain and Extra-Terminal Motif Proteins (Bets) in Gata1-Mediated Transcription
    University of Pennsylvania ScholarlyCommons Publicly Accessible Penn Dissertations 2015 Function of Bromodomain and Extra-Terminal Motif Proteins (bets) in Gata1-Mediated Transcription Aaron James Stonestrom University of Pennsylvania, [email protected] Follow this and additional works at: https://repository.upenn.edu/edissertations Part of the Molecular Biology Commons, and the Pharmacology Commons Recommended Citation Stonestrom, Aaron James, "Function of Bromodomain and Extra-Terminal Motif Proteins (bets) in Gata1-Mediated Transcription" (2015). Publicly Accessible Penn Dissertations. 1148. https://repository.upenn.edu/edissertations/1148 This paper is posted at ScholarlyCommons. https://repository.upenn.edu/edissertations/1148 For more information, please contact [email protected]. Function of Bromodomain and Extra-Terminal Motif Proteins (bets) in Gata1-Mediated Transcription Abstract Bromodomain and Extra-Terminal motif proteins (BETs) associate with acetylated histones and transcription factors. While pharmacologic inhibition of this ubiquitous protein family is an emerging therapeutic approach for neoplastic and inflammatory disease, the mechanisms through which BETs act remain largely uncharacterized. Here we explore the role of BETs in the physiologically relevant context of erythropoiesis driven by the transcription factor GATA1. First, we characterize functions of the BET family as a whole using a pharmacologic approach. We find that BETs are broadly required for GATA1-mediated transcriptional activation, but that repression is largely BET-independent. BETs support activation by facilitating both GATA1 occupancy and transcription downstream of its binding. Second, we test the specific olesr of BETs BRD2, BRD3, and BRD4 in GATA1-activated transcription. BRD2 and BRD4 are required for efficient anscriptionaltr activation by GATA1. Despite co-localizing with the great majority of GATA1 binding sites, we find that BRD3 is not equirr ed for GATA1-mediated transcriptional activation.
    [Show full text]
  • Epigenetics Page 1
    Epigenetics esiRNA ID Gene Name Gene Description Ensembl ID HU-13237-1 ACTL6A actin-like 6A ENSG00000136518 HU-13925-1 ACTL6B actin-like 6B ENSG00000077080 HU-14457-1 ACTR1A ARP1 actin-related protein 1 homolog A, centractin alpha (yeast) ENSG00000138107 HU-10579-1 ACTR2 ARP2 actin-related protein 2 homolog (yeast) ENSG00000138071 HU-10837-1 ACTR3 ARP3 actin-related protein 3 homolog (yeast) ENSG00000115091 HU-09776-1 ACTR5 ARP5 actin-related protein 5 homolog (yeast) ENSG00000101442 HU-00773-1 ACTR6 ARP6 actin-related protein 6 homolog (yeast) ENSG00000075089 HU-07176-1 ACTR8 ARP8 actin-related protein 8 homolog (yeast) ENSG00000113812 HU-09411-1 AHCTF1 AT hook containing transcription factor 1 ENSG00000153207 HU-15150-1 AIRE autoimmune regulator ENSG00000160224 HU-12332-1 AKAP1 A kinase (PRKA) anchor protein 1 ENSG00000121057 HU-04065-1 ALG13 asparagine-linked glycosylation 13 homolog (S. cerevisiae) ENSG00000101901 HU-13552-1 ALKBH1 alkB, alkylation repair homolog 1 (E. coli) ENSG00000100601 HU-06662-1 ARID1A AT rich interactive domain 1A (SWI-like) ENSG00000117713 HU-12790-1 ARID1B AT rich interactive domain 1B (SWI1-like) ENSG00000049618 HU-09415-1 ARID2 AT rich interactive domain 2 (ARID, RFX-like) ENSG00000189079 HU-03890-1 ARID3A AT rich interactive domain 3A (BRIGHT-like) ENSG00000116017 HU-14677-1 ARID3B AT rich interactive domain 3B (BRIGHT-like) ENSG00000179361 HU-14203-1 ARID3C AT rich interactive domain 3C (BRIGHT-like) ENSG00000205143 HU-09104-1 ARID4A AT rich interactive domain 4A (RBP1-like) ENSG00000032219 HU-12512-1 ARID4B AT rich interactive domain 4B (RBP1-like) ENSG00000054267 HU-12520-1 ARID5A AT rich interactive domain 5A (MRF1-like) ENSG00000196843 HU-06595-1 ARID5B AT rich interactive domain 5B (MRF1-like) ENSG00000150347 HU-00556-1 ASF1A ASF1 anti-silencing function 1 homolog A (S.
    [Show full text]
  • Recognition of Cancer Mutations in Histone H3K36 by Epigenetic Writers and Readers Brianna J
    EPIGENETICS https://doi.org/10.1080/15592294.2018.1503491 REVIEW Recognition of cancer mutations in histone H3K36 by epigenetic writers and readers Brianna J. Kleina, Krzysztof Krajewski b, Susana Restrepoa, Peter W. Lewis c, Brian D. Strahlb, and Tatiana G. Kutateladzea aDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO, USA; bDepartment of Biochemistry & Biophysics, The University of North Carolina School of Medicine, Chapel Hill, NC, USA; cWisconsin Institute for Discovery, University of Wisconsin, Madison, WI, USA ABSTRACT ARTICLE HISTORY Histone posttranslational modifications control the organization and function of chromatin. In Received 30 May 2018 particular, methylation of lysine 36 in histone H3 (H3K36me) has been shown to mediate gene Revised 1 July 2018 transcription, DNA repair, cell cycle regulation, and pre-mRNA splicing. Notably, mutations at or Accepted 12 July 2018 near this residue have been causally linked to the development of several human cancers. These KEYWORDS observations have helped to illuminate the role of histones themselves in disease and to clarify Histone; H3K36M; cancer; the mechanisms by which they acquire oncogenic properties. This perspective focuses on recent PTM; methylation advances in discovery and characterization of histone H3 mutations that impact H3K36 methyla- tion. We also highlight findings that the common cancer-related substitution of H3K36 to methionine (H3K36M) disturbs functions of not only H3K36me-writing enzymes but also H3K36me-specific readers. The latter case suggests that the oncogenic effects could also be linked to the inability of readers to engage H3K36M. Introduction from yeast to humans and has been shown to have a variety of functions that range from the control Histone proteins are main components of the of gene transcription and DNA repair, to cell cycle nucleosome, the fundamental building block of regulation and nutrient stress response [8].
    [Show full text]
  • Aberrant Activity of Histone–Lysine N-Methyltransferase 2 (KMT2) Complexes in Oncogenesis
    International Journal of Molecular Sciences Review Aberrant Activity of Histone–Lysine N-Methyltransferase 2 (KMT2) Complexes in Oncogenesis Elzbieta Poreba 1,* , Krzysztof Lesniewicz 2 and Julia Durzynska 1,* 1 Institute of Experimental Biology, Faculty of Biology, Adam Mickiewicz University, ul. Uniwersytetu Pozna´nskiego6, 61-614 Pozna´n,Poland 2 Department of Molecular and Cellular Biology, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University, ul. Uniwersytetu Pozna´nskiego6, 61-614 Pozna´n,Poland; [email protected] * Correspondence: [email protected] (E.P.); [email protected] (J.D.); Tel.: +48-61-829-5857 (E.P.) Received: 19 November 2020; Accepted: 6 December 2020; Published: 8 December 2020 Abstract: KMT2 (histone-lysine N-methyltransferase subclass 2) complexes methylate lysine 4 on the histone H3 tail at gene promoters and gene enhancers and, thus, control the process of gene transcription. These complexes not only play an essential role in normal development but have also been described as involved in the aberrant growth of tissues. KMT2 mutations resulting from the rearrangements of the KMT2A (MLL1) gene at 11q23 are associated with pediatric mixed-lineage leukemias, and recent studies demonstrate that KMT2 genes are frequently mutated in many types of human cancers. Moreover, other components of the KMT2 complexes have been reported to contribute to oncogenesis. This review summarizes the recent advances in our knowledge of the role of KMT2 complexes in cell transformation. In addition, it discusses the therapeutic targeting of different components of the KMT2 complexes. Keywords: histone–lysine N-methyltransferase 2; COMPASS; COMPASS-like; H3K4 methylation; oncogenesis; cancer; epigenetics; chromatin 1.
    [Show full text]
  • Pointing the Finger
    RESEARCH HIGHLIGHTS Nature Reviews Molecular Cell Biology | AOP, published online 14 June 2006; doi:10.1038/nrm1966 DOI: 10.1038/nrm1966 URLs BPTF http://ca.expasy.org/uniprot/ Q9UIG2 ING2 http://ca.expasy.org/uniprot/ Q9ESK4 GENE EXPRESSION Pointing the finger Mechanistic links between specific histone-tail tumour suppressors, bound specifically to modifications and their effects on gene H3K4me3. ING2 is a subunit of a SIN3a–HDAC1 expression have been difficult to establish. histone-deacetylase complex. The authors However, four papers in Nature now identify the showed that in response to DNA damage, binding plant homeodomain (PHD) finger as an important of the ING2 PHD finger to H3K4me3 that is effector domain that binds to the trimethylated present at the promoters of actively transcribed K4 residue of histone H3 (H3K4me3) and couples proliferation genes enhanced the association of it to gene activation in one case and to gene the ING2–HDAC1 complex at these genes. This repression in another. resulted in increased histone-deacetylase activity Wysocka et al. affinity purified the BPTF and hence acute repression of the cognate (bromodomain and PHD finger transcription transcript. These findings, together with those of factor) subunit of NURF — an ATP-dependent Wysocka et al., indicate that PHD fingers have a chromatin remodelling complex — using an general role as effector domains that link H3K4me3-containing peptide. Mutational analysis H3K4me3 to diverse biological outcomes. narrowed the H3K4me3-interaction region to the The molecular mechanism that underlies the second, conserved bromodomain-proximal PHD recognition of H3K4me3 by the PHD finger of finger of BPTF. Knockdown of the histone ING2 was reported in a fourth linked paper.
    [Show full text]
  • Further Delineation of the Clinical Spectrum of KAT6B Disorders and Allelic Series of Pathogenic Variants
    ARTICLE © American College of Medical Genetics and Genomics Further delineation of the clinical spectrum of KAT6B disorders and allelic series of pathogenic variants Li Xin Zhang1, Gabrielle Lemire, MD2, Claudia Gonzaga-Jauregui, PhD3, Sirinart Molidperee, Gr. Cert1, Carolina Galaz-Montoya, MD3, David S. Liu, MD3, Alain Verloes, MD PhD4, Amelle G. Shillington, DO5, Kosuke Izumi, MD PhD6, Alyssa L. Ritter, MS LCGC7, Beth Keena, MS LCGC6, Elaine Zackai, MD7,8, Dong Li, PhD9, Elizabeth Bhoj, MD PhD7, Jennifer M. Tarpinian, MS CGC10, Emma Bedoukian, MS LCGC10, Mary K. Kukolich, MD11, A. Micheil Innes, MD12, Grace U. Ediae, BSc13, Sarah L. Sawyer, MD PhD14, Karippoth Mohandas Nair, MD15, Para Chottil Soumya, MD15, Kinattinkara R. Subbaraman, MD15, Frank J. Probst, MD PhD3,16, Jennifer A. Bassetti, MD3,16, Reid V. Sutton, MD3,16, Richard A. Gibbs, PhD3, Chester Brown, MD PhD17, Philip M. Boone, MD PhD18, Ingrid A. Holm, MD MPH18, Marco Tartaglia, PhD19, Giovanni Battista Ferrero, MD PhD20, Marcello Niceta, MD PhD19, Maria Lisa Dentici, MD19, Francesca Clementina Radio, MD PhD19, Boris Keren, MD21, Constance F. Wells, MD22, Christine Coubes, MD22, Annie Laquerrière, MD PhD23, Jacqueline Aziza, MD24, Charlotte Dubucs, MD24, Sheela Nampoothiri, MD25, David Mowat, MD26, Millan S. Patel, MD27, Ana Bracho, MD28, Francisco Cammarata-Scalisi, MD29, Alper Gezdirici, MD30, Alberto Fernandez-Jaen, MD31, Natalie Hauser, MD32, Yuri A. Zarate, MD33, Katherine A. Bosanko, MS CGC33, Klaus Dieterich, MD PhD34, John C. Carey, MD MPH35, Jessica X. Chong, PhD36,37, Deborah A. Nickerson, PhD37,38, Michael J. Bamshad, MD36,37, Brendan H. Lee, MD PhD3, Xiang-Jiao Yang, PhD39, James R.
    [Show full text]
  • Download Product Insert (PDF)
    PRODUCT INFORMATION BRD3 bromodomains 1 and 2 (human, recombinant) Item No. 14864 Overview and Properties Synonyms: Bromodomain containing protein 3, ORFX, RING3L, RING3-like protein Source: Recombinant N-terminal GST-tagged protein expressed in E. coli Amino Acids: 2-434 Uniprot No.: Q15059 Molecular Weight: 75.0 kDa Storage: -80°C (as supplied) Stability: ≥2 years Purity: batch specific (≥85% estimated by SDS-PAGE) Supplied in: 50 mM Tris, pH 8.0, with 150 mM sodium chloride and 20% glycerol Protein Concentration: batch specific mg/ml Activity: batch specific U/ml Specific Activity: batch specific U/mg Information represents the product specifications. Batch specific analytical results are provided on each certificate of analysis. Image 1 2 3 4 · · · · · · ·250 kDa · · · · · · ·150 kDa · · · · · · ·100 kDa · · · · · · ·75 kDa · · · · · · ·50 kDa · · · · · · ·37 kDa · · · · · · ·25 kDa · · · · · · ·20 kDa · · · · · · ·15 kDa Lane 1: BRD3 (4 µg) Lane 2: BRD3 (6 µg) Lane 3: BRD3 (8 µg) Lane 4: MW Markers WARNING CAYMAN CHEMICAL THIS PRODUCT IS FOR RESEARCH ONLY - NOT FOR HUMAN OR VETERINARY DIAGNOSTIC OR THERAPEUTIC USE. 1180 EAST ELLSWORTH RD SAFETY DATA ANN ARBOR, MI 48108 · USA This material should be considered hazardous until further information becomes available. Do not ingest, inhale, get in eyes, on skin, or on clothing. Wash thoroughly after handling. Before use, the user must review the complete Safety Data Sheet, which has been sent via email to your institution. PHONE: [800] 364-9897 WARRANTY AND LIMITATION OF REMEDY [734] 971-3335 Buyer agrees to purchase the material subject to Cayman’s Terms and Conditions. Complete Terms and Conditions including Warranty and Limitation of Liability information can be found on our website.
    [Show full text]