MAF1 Polyclonal Antibody

Total Page:16

File Type:pdf, Size:1020Kb

MAF1 Polyclonal Antibody PRODUCT DATA SHEET Bioworld Technology,Inc. MAF1 polyclonal antibody Catalog: BS61103 Host: Rabbit Reactivity: Human,Mouse,Rat BackGround: munogen and the purity is > 95% (by SDS-PAGE). MAF1 is a 256 amino acid protein that localizes to the Applications: nucleus and is the human homolog of the yeast Maf1 WB: 1:500~1:1000 protein. Interacting with BRF2, MAF1 functions to medi- Storage&Stability: ate signals that specifically repress the activity of RNA Store at 4°C short term. Aliquot and store at -20°C long polymerase III (Pol III), specifically by inhibiting the as- term. Avoid freeze-thaw cycles. sembly of TFIIIB onto DNA. The gene encoding MAF1 Specificity: maps to human chromosome 8, which consists of nearly MAF1 polyclonal antibody detects endogenous levels of 146 million base pairs, houses more than 800 genes and is MAF1 protein. associated with a variety of diseases and malignancies. DATA: Schizophrenia, bipolar disorder, Trisomy 8, Pfeiffer syn- drome, congenital hypothyroidism, Waardenburg syn- drome and some leukemias and lymphomas are thought to occur as a result of defects in specific genes that map to chromosome 8. Product: Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2 Western blot (WB) analysis of MAF1 polyclonal antibody at 1:500 dilu- Molecular Weight: tion Lane1:HEK293T whole cell lysate ~ 29 kDa Lane2:RAW264.7 whole cell lysate Lane3:H9C2 whole cell lysate Swiss-Prot: Note: Q9H063 For research use only, not for use in diagnostic procedure. Purification&Purity: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific im- Bioworld Technology, Inc. Bioworld technology, co. Ltd. Add: 1660 South Highway 100, Suite 500 St. Louis Park, Add: No 9, weidi road Qixia District Nanjing, 210046, MN 55416,USA. P. R. China. Email: [email protected] Email: [email protected] Tel: 6123263284 Tel: 0086-025-68037686 Fax: 6122933841 Fax: 0086-025-68035151 .
Recommended publications
  • Analysis of Gene Expression Data for Gene Ontology
    ANALYSIS OF GENE EXPRESSION DATA FOR GENE ONTOLOGY BASED PROTEIN FUNCTION PREDICTION A Thesis Presented to The Graduate Faculty of The University of Akron In Partial Fulfillment of the Requirements for the Degree Master of Science Robert Daniel Macholan May 2011 ANALYSIS OF GENE EXPRESSION DATA FOR GENE ONTOLOGY BASED PROTEIN FUNCTION PREDICTION Robert Daniel Macholan Thesis Approved: Accepted: _______________________________ _______________________________ Advisor Department Chair Dr. Zhong-Hui Duan Dr. Chien-Chung Chan _______________________________ _______________________________ Committee Member Dean of the College Dr. Chien-Chung Chan Dr. Chand K. Midha _______________________________ _______________________________ Committee Member Dean of the Graduate School Dr. Yingcai Xiao Dr. George R. Newkome _______________________________ Date ii ABSTRACT A tremendous increase in genomic data has encouraged biologists to turn to bioinformatics in order to assist in its interpretation and processing. One of the present challenges that need to be overcome in order to understand this data more completely is the development of a reliable method to accurately predict the function of a protein from its genomic information. This study focuses on developing an effective algorithm for protein function prediction. The algorithm is based on proteins that have similar expression patterns. The similarity of the expression data is determined using a novel measure, the slope matrix. The slope matrix introduces a normalized method for the comparison of expression levels throughout a proteome. The algorithm is tested using real microarray gene expression data. Their functions are characterized using gene ontology annotations. The results of the case study indicate the protein function prediction algorithm developed is comparable to the prediction algorithms that are based on the annotations of homologous proteins.
    [Show full text]
  • Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino-Like Mouse Models: Tracking the Role of the Hairless Gene
    University of Tennessee, Knoxville TRACE: Tennessee Research and Creative Exchange Doctoral Dissertations Graduate School 5-2006 Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino-like Mouse Models: Tracking the Role of the Hairless Gene Yutao Liu University of Tennessee - Knoxville Follow this and additional works at: https://trace.tennessee.edu/utk_graddiss Part of the Life Sciences Commons Recommended Citation Liu, Yutao, "Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino- like Mouse Models: Tracking the Role of the Hairless Gene. " PhD diss., University of Tennessee, 2006. https://trace.tennessee.edu/utk_graddiss/1824 This Dissertation is brought to you for free and open access by the Graduate School at TRACE: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of TRACE: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. To the Graduate Council: I am submitting herewith a dissertation written by Yutao Liu entitled "Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino-like Mouse Models: Tracking the Role of the Hairless Gene." I have examined the final electronic copy of this dissertation for form and content and recommend that it be accepted in partial fulfillment of the requirements for the degree of Doctor of Philosophy, with a major in Life Sciences. Brynn H. Voy, Major Professor We have read this dissertation and recommend its acceptance: Naima Moustaid-Moussa, Yisong Wang, Rogert Hettich Accepted for the Council: Carolyn R.
    [Show full text]
  • Trna GENES AFFECT MULTIPLE ASPECTS of LOCAL CHROMOSOME BEHAVIOR
    tRNA GENES AFFECT MULTIPLE ASPECTS OF LOCAL CHROMOSOME BEHAVIOR by Matthew J Pratt-Hyatt A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy (Cellular and Molecular Biology) in The University of Michigan 2008 Doctoral Committee: Professor David R. Engelke, Chair Professor Robert S. Fuller Associate Professor Mats E. Ljungman Associate Professor Thomas E. Wilson Assistant Professor Daniel A. Bochar © Matthew J. Pratt-Hyatt All rights reserved 2008 . To my loving family Who’ve helped me so much ii Acknowledgements I would first like to thank my mentor, David Engelke. His help has been imperative to the development of my scientific reasoning, writing, and public speaking. He has been incredibly supportive at each phase of my graduate career here at the University of Michigan. Second, I would like to thank the past and present members of the Engelke lab. I would especially like to thank Paul Good, May Tsoi, Glenn Wozniak, Kevin Kapadia, and Becky Haeusler for all of their help. For this dissertation I would like to thank the following people for their assistance. For Chapter II, I would like to thank Kevin Kapadia and Paul Good for technical assistance. I would also like to thank David Engelke and Tom Wilson for help with critical thinking and writing. For Chapter III, I would like to thank David Engelke and Rebecca Haeusler for their major writing contribution. I would also like to acknowledge that Rebecca Haeusler did the majority of the work that led to figures 1-3 in that chapter. For Chapter IV, I would like to thank Anita Hopper, David Engelke and Rebecca Haeusler for their writing contributions.
    [Show full text]
  • Supplementary Table 3: Genes Only Influenced By
    Supplementary Table 3: Genes only influenced by X10 Illumina ID Gene ID Entrez Gene Name Fold change compared to vehicle 1810058M03RIK -1.104 2210008F06RIK 1.090 2310005E10RIK -1.175 2610016F04RIK 1.081 2610029K11RIK 1.130 381484 Gm5150 predicted gene 5150 -1.230 4833425P12RIK -1.127 4933412E12RIK -1.333 6030458P06RIK -1.131 6430550H21RIK 1.073 6530401D06RIK 1.229 9030607L17RIK -1.122 A330043C08RIK 1.113 A330043L12 1.054 A530092L01RIK -1.069 A630054D14 1.072 A630097D09RIK -1.102 AA409316 FAM83H family with sequence similarity 83, member H 1.142 AAAS AAAS achalasia, adrenocortical insufficiency, alacrimia 1.144 ACADL ACADL acyl-CoA dehydrogenase, long chain -1.135 ACOT1 ACOT1 acyl-CoA thioesterase 1 -1.191 ADAMTSL5 ADAMTSL5 ADAMTS-like 5 1.210 AFG3L2 AFG3L2 AFG3 ATPase family gene 3-like 2 (S. cerevisiae) 1.212 AI256775 RFESD Rieske (Fe-S) domain containing 1.134 Lipo1 (includes AI747699 others) lipase, member O2 -1.083 AKAP8L AKAP8L A kinase (PRKA) anchor protein 8-like -1.263 AKR7A5 -1.225 AMBP AMBP alpha-1-microglobulin/bikunin precursor 1.074 ANAPC2 ANAPC2 anaphase promoting complex subunit 2 -1.134 ANKRD1 ANKRD1 ankyrin repeat domain 1 (cardiac muscle) 1.314 APOA1 APOA1 apolipoprotein A-I -1.086 ARHGAP26 ARHGAP26 Rho GTPase activating protein 26 -1.083 ARL5A ARL5A ADP-ribosylation factor-like 5A -1.212 ARMC3 ARMC3 armadillo repeat containing 3 -1.077 ARPC5 ARPC5 actin related protein 2/3 complex, subunit 5, 16kDa -1.190 activating transcription factor 4 (tax-responsive enhancer element ATF4 ATF4 B67) 1.481 AU014645 NCBP1 nuclear cap
    [Show full text]
  • Structure-Function Analysis of the RNA Polymerase III Subcomplex C17/25 and Genome-Wide Distribution of RNA Polymerase II
    Dissertation zur Erlangung des Doktorgrades der Fakultät für Chemie und Pharmazie der Ludwig-Maximilians-Universität München Structure-function analysis of the RNA polymerase III subcomplex C17/25 and genome-wide distribution of RNA polymerase II Anna Justyna Jasiak aus Kedzierzyn-Kozle, Polen 2008 Erklärung II Erklärung Diese Dissertation wurde im Sinne von §13 Abs. 3 der Promotionsordnung vom 29. Januar 1998 von Herrn Prof. Dr. Patrick Cramer betreut. Ehrenwörtliche Versicherung Diese Dissertation wurde selbständig und ohne unerlaubte Hilfe erarbeitet. München, am 21. November 2008 Anna J. Jasiak Dissertation eingereicht am 21. November 2008 1. Gutachter: Prof. Dr. Patrick Cramer 2. Gutachter: Prof. Dr. Klaus Förstemann Mündliche Prüfung am 14. Januar 2009 Acknowledgements III Acknowledgements I would like to thank my supervisor Prof. Patrick Cramer for creating a highly motivating scientific environment and his open-minded attitude in trying new methods. I have started my PhD with a purely crystallographic project and thanks to his never-ending enthusiasms and ideas I have got a unique opportunity to gain an insight into a broad range of in vivo and in vitro techniques. I have enjoyed it very much. I am deeply grateful for his support and understanding shown during the last phase of my PhD. Special thanks to Karim Armache and Laurent Larivière for their help in solving C17/25 structure, to Michaela Bertero for teaching me how to handle the protein crystals and to Dietmar Martin for the discussion and help on the ChIP-chip project. Moreover, I would like to thank to my collaborators Johannes Söding and Holger Hartmann for their input in microarray data analysis and Birgit Märtens for yeast complementation studies.
    [Show full text]
  • Molecular Basis of RNA Polymerase III Transcription Repression by Maf1
    Dissertation zur Erlangung des Doktorgrades der Fakultät für Chemie und Pharmazie der Ludwig-Maximilians-Universität München Molecular basis of RNA polymerase III transcription repression by Maf1 & Structure of human mitochondrial RNA polymerase Eva Rieke Ringel aus Essen 2011 Dissertation zur Erlangung des Doktorgrades der Fakultät für Chemie und Pharmazie der Ludwig-Maximilians-Universität München Molecular basis of RNA polymerase III transcription repression by Maf1 & Structure of human mitochondrial RNA polymerase Eva Rieke Ringel aus Essen 2011 Erklärung Diese Dissertation wurde im Sinne von § 13 Abs. 3 bzw. 4 der Promotionsordnung vom 29. Januar 1998 (in der Fassung der sechsten Änderungssatzung vom 16. August 2010) von Herrn Prof. Dr. Patrick Cramer betreut. Ehrenwörtliche Versicherung Diese Dissertation wurde selbständig, ohne unerlaubte Hilfe erarbeitet. München, ..................................... .................................................................... Eva Rieke Ringel Dissertation eingereicht am 26.05.2011 1. Gutachter Prof. Dr. Patrick Cramer 2. Gutachter Prof. Dr. Dietmar Martin Mündliche Prüfung am 26.07.2011 Acknowledgements Life-science is like teamsports. If you want to play in a high league, you need to have good players and, even more importantly, a strong and diehard team effort. Without good passes from your teammates you would never score a goal and without the right tactics, training input and motivation from your coach, there would be nothing to win. I am very grateful that I was part of such a successful and inspiring squad, the Cramer lab team. I want to thank Patrick, the coach, not only for letting me be part of this team but also for his leadership. You gave me at the right time a lot of freedom to decide over my daily labwork and provided helpful feedback and project plans, when it was required.
    [Show full text]
  • MAF1 Sirna (M): Sc-75732
    SAN TA C RUZ BI OTEC HNOL OG Y, INC . MAF1 siRNA (m): sc-75732 BACKGROUND STORAGE AND RESUSPENSION MAF1 is a 256 amino acid protein that localizes to the nucleus and is the hu- Store lyophilized siRNA duplex at -20° C with desiccant. Stable for at least man homolog of the yeast Maf1 protein. Interacting with BRF2, MAF1 func- one year from the date of shipment. Once resuspended, store at -20° C, tions to mediate signals that specifically repress the activity of RNA poly - avoid contact with RNAses and repeated freeze thaw cycles. merase III (Pol III), specifically by inhibiting the assembly of TFIIIB onto DNA. Resuspend lyophilized siRNA duplex in 330 µl of the RNAse-free water The gene encoding MAF1 maps to human chromosome 8, which consists of pro vided. Resuspension of the siRNA duplex in 330 µl of RNAse-free water nearly 146 million base pairs, houses more than 800 genes and is associated makes a 10 µM solution in a 10 µM Tris-HCl, pH 8.0, 20 mM NaCl, 1 mM with a variety of diseases and malignancies. Schizophrenia, bipolar disorder, EDTA buffered solution. Trisomy 8, Pfeiffer syndrome, congenital hypothyroidism, Waardenburg syn - drome and some leukemias and lymphomas are thought to occur as a result APPLICATIONS of defects in specific genes that map to chromosome 8. MAF1 siRNA (m) is recommended for the inhibition of MAF1 expression in REFERENCES mouse cells. 1. Pluta, K., et al. 2001. MAF1 p, a negative effector of RNA polymerase III in SUPPORT REAGENTS Saccharomyces cerevisiae . Mol. Cell. Biol.
    [Show full text]
  • Analyzing the Mirna-Gene Networks to Mine the Important Mirnas Under Skin of Human and Mouse
    Hindawi Publishing Corporation BioMed Research International Volume 2016, Article ID 5469371, 9 pages http://dx.doi.org/10.1155/2016/5469371 Research Article Analyzing the miRNA-Gene Networks to Mine the Important miRNAs under Skin of Human and Mouse Jianghong Wu,1,2,3,4,5 Husile Gong,1,2 Yongsheng Bai,5,6 and Wenguang Zhang1 1 College of Animal Science, Inner Mongolia Agricultural University, Hohhot 010018, China 2Inner Mongolia Academy of Agricultural & Animal Husbandry Sciences, Hohhot 010031, China 3Inner Mongolia Prataculture Research Center, Chinese Academy of Science, Hohhot 010031, China 4State Key Laboratory of Genetic Resources and Evolution, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China 5Department of Biology, Indiana State University, Terre Haute, IN 47809, USA 6The Center for Genomic Advocacy, Indiana State University, Terre Haute, IN 47809, USA Correspondence should be addressed to Yongsheng Bai; [email protected] and Wenguang Zhang; [email protected] Received 11 April 2016; Revised 15 July 2016; Accepted 27 July 2016 Academic Editor: Nicola Cirillo Copyright © 2016 Jianghong Wu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Genetic networks provide new mechanistic insights into the diversity of species morphology. In this study, we have integrated the MGI, GEO, and miRNA database to analyze the genetic regulatory networks under morphology difference of integument of humans and mice. We found that the gene expression network in the skin is highly divergent between human and mouse.
    [Show full text]
  • MAF1 Represses CDKN1A Through a Pol III-Dependent Mechanism
    1 2 MAF1 Represses CDKN1A through a 3 Pol III-Dependent Mechanism 4 5 6 Yu-Ling Lee 1, Yuan-Ching Li1, Chia-Hsin Su1, Chun-Hui Chiao1, I-Hsuan Lin1, and Ming-Ta 7 Hsu1,# 8 9 10 1Institute of Biochemistry and Molecular Biology, School of Life Science, National 11 Yang-Ming University, Taipei, Taiwan. 12 13 Running Head: MAF1-Regulated-Pol III-Mediated CDKN1A 14 15 16 17 # Corresponding author 18 Ming-Ta Hsu, Ph.D. 19 Distinguished Chair Professor, Institute of Biochemistry and Molecular Biology 20 National Yang Ming University 21 E mail: [email protected] 22 Telephone: 011-8862-2826-7230 1 23 Abstract 24 MAF1 represses Pol III-mediated transcription by interfering with TFIIIB and Pol III. 25 Herein, we found that MAF1 knockdown induced CDKN1A transcription and chromatin 26 looping concurrently with Pol III recruitment. Simultaneous knockdown of MAF1 with Pol III 27 or BRF1 (subunit of TFIIIB) diminished the activation and looping effect, which indicates that 28 recruiting Pol III was required for activation of Pol II-mediated transcription and chromatin 29 looping. ChIP analysis after MAF1 knockdown indicated enhanced binding of Pol III and 30 BRF1, as well as of CFP1, p300, and PCAF, which are factors that mediate active histone 31 marks, along with the binding of TBP and POLR2E to the CDKN1A promoter. Simultaneous 32 knockdown with Pol III abolished these regulatory events. Similar results were obtained for 33 GDF15. Our results reveal a novel mechanism by which MAF1 and Pol III regulate the 34 activity of a protein-coding gene transcribed by Pol II.
    [Show full text]
  • Oddpols 2021 International Conference on Transcription Mechanism and Regulation Table of Contents: Oddpols 2021 Organizers and Sponsors
    OddPols 2021 International Conference on Transcription Mechanism and Regulation Table of Contents: OddPols 2021 Organizers and Sponsors.............................................................................1 Call for Summations and Papers............................................................................................2 Information for Zoom Breakout Rooms and Socialization.....................................................3 OddPols 2021 Virtual Schedule .............................................................................................4 Day 1.............................................................................................................................4 Day 2.............................................................................................................................6 Day 3.............................................................................................................................8 Day 4...........................................................................................................................10 Day 5...........................................................................................................................12 Abstracts..............................................................................................................................14 Participant Directory..........................................................................................................137 Organizing Committee: Craig Cameron, U. of North Carolina Astrid
    [Show full text]
  • Ocular Coloboma: a Reassessment in the Age of Molecular Neuroscience
    881 REVIEW Ocular coloboma: a reassessment in the age of molecular neuroscience C Y Gregory-Evans, M J Williams, S Halford, K Gregory-Evans ............................................................................................................................... J Med Genet 2004;41:881–891. doi: 10.1136/jmg.2004.025494 Congenital colobomata of the eye are important causes of NORMAL EYE DEVELOPMENT The processes that occur during formation of the childhood visual impairment and blindness. Ocular vertebrate eye are well documented and include coloboma can be seen in isolation and in an impressive (i) multiple inductive and morphogenetic events, number of multisystem syndromes, where the eye (ii) proliferation and differentiation of cells into mature tissue, and (iii) establishment of neural phenotype is often seen in association with severe networks connecting the retina to the higher neurological or craniofacial anomalies or other systemic neural centres such as the superior colliculus, the developmental defects. Several studies have shown that, in geniculate nucleus, and the occipital lobes.8–10 At around day 30 of gestation, the ventral surface addition to inheritance, environmental influences may be of the optic vesicle and stalk invaginates leading causative factors. Through work to identify genes to the formation of a double-layered optic cup. underlying inherited coloboma, significant inroads are This invagination gives rise to the optic fissure, allowing blood vessels from the vascular meso- being made into understanding the molecular events derm to enter the developing eye. Fusion of the controlling closure of the optic fissure. In general, severity edges of this fissure starts centrally at about of disease can be linked to the temporal expression of the 5 weeks and proceeds anteriorly towards the rim of the optic cup and posteriorly along the optic gene, but this is modified by factors such as tissue stalk, with completion by 7 weeks.11 Failure of specificity of gene expression and genetic redundancy.
    [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]