TAF13 Rabbit Pab

Total Page：16

File Type：pdf, Size：1020Kb

Leader in Biomolecular Solutions for Life Science TAF13 Rabbit pAb Catalog No.: A9637 Basic Information Background Catalog No. Initiation of transcription by RNA polymerase II requires the activities of more than 70 A9637 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as Observed MW the scaffold for assembly of the remainder of the transcription complex, and acts as a 14kDa channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. Calculated MW TAFs may participate in basal transcription, serve as coactivators, function in promoter 14kDa recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes a small subunit associated with a subset Category of TFIID complexes. This subunit interacts with TBP and with two other small subunits of TFIID, TAF10 and TAF11. There is a pseudogene located on chromosome 6. Primary antibody Applications WB Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 6884 Q15543 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 1-124 of human TAF13 (NP_005636.1). Synonyms TAF13;TAF(II)18;TAF2K;TAFII-18;TAFII18;MRT60 Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using TAF13 antibody (A9637) at 1:3000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Enhanced Kit (RM00021). Exposure time: 90s. Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..

Copy Link

Recommended publications

Characterization of Genomic Copy Number Variation in Mus Musculus Associated with the Germline of Inbred and Wild Mouse Populations, Normal Development, and Cancer
Western University Scholarship@Western Electronic Thesis and Dissertation Repository 4-18-2019 2:00 PM Characterization of genomic copy number variation in Mus musculus associated with the germline of inbred and wild mouse populations, normal development, and cancer Maja Milojevic The University of Western Ontario Supervisor Hill, Kathleen A. The University of Western Ontario Graduate Program in Biology A thesis submitted in partial fulfillment of the equirr ements for the degree in Doctor of Philosophy © Maja Milojevic 2019 Follow this and additional works at: https://ir.lib.uwo.ca/etd Part of the Genetics and Genomics Commons Recommended Citation Milojevic, Maja, "Characterization of genomic copy number variation in Mus musculus associated with the germline of inbred and wild mouse populations, normal development, and cancer" (2019). Electronic Thesis and Dissertation Repository. 6146. https://ir.lib.uwo.ca/etd/6146 This Dissertation/Thesis is brought to you for free and open access by Scholarship@Western. It has been accepted for inclusion in Electronic Thesis and Dissertation Repository by an authorized administrator of Scholarship@Western. For more information, please contact [email protected]. Abstract Mus musculus is a human commensal species and an important model of human development and disease with a need for approaches to determine the contribution of copy number variants (CNVs) to genetic variation in laboratory and wild mice, and arising with normal mouse development and disease. Here, the Mouse Diversity Genotyping array (MDGA)-approach to CNV detection is developed to characterize CNV differences between laboratory and wild mice, between multiple normal tissues of the same mouse, and between primary mammary gland tumours and metastatic lung tissue.
[Show full text]
The Function of TAF10 Proteins in Drosophila Melanogaster
The function of dTAF10 proteins in Drosophila melanogaster Zoltán Gábor Páhi Ph.D. thesis summary Supervisors: Imre Miklós Boros Ph.D, D.Sc. Head of the Department Tibor Pankotai Ph.D. Assistant Professor Ph.D. School of Biology University of Szeged Faculty of Science and Informatics Department of Biochemistry and Molecular Biology Szeged 2017 1. Introduction As a first step of eukaryotic transcription initiation, the general transcription factor TFIID binds to the promoter region of transcribed genes. TFIID is a multiprotein complex consisting of TBP, which binds to the TATA box region, and several TAF proteins, which associate with TBP. TFIID is evolutionary well- conserved in human and Drosophila cells and it consists of double copies of five TAFs (TAF4, TAF5, TAF6, TAF9 and TAF12), which together create a two-fold symmetric structure. Then TAF8-TAF10 heterodimer joins to this complex and induces conformational changes by abolishing the two-fold symmetry. Further peripheral TAF proteins and TBP bind to the 7 TAF containing TFIID core, forming the functional complex. TAF proteins, however are parts not only the TBP, but the histone acetyl transferase (HAT) SAGA complex, as well. Drosophila dSAGA acetylates histone proteins by transferring acetyl groups from acetyl-coenzyme A to lysine side chains. The HAT enzyme of dSAGA is dGCN5, which on the other hand is also present in another histone acetyltransferase complex as well, that is designated as dATAC in Drosophila. Curiously, while dSAGA and dATAC complexes have very similar HAT modules, in which they share common subunits, such as dGCN5, dSGF29 and dADA3, they regulate different 1 biological processes.
[Show full text]
Molecular Structure of Promoter-Bound Yeast TFIID
ARTICLE DOI: 10.1038/s41467-018-07096-y OPEN Molecular structure of promoter-bound yeast TFIID Olga Kolesnikova 1,2,3,4, Adam Ben-Shem1,2,3,4, Jie Luo5, Jeff Ranish 5, Patrick Schultz 1,2,3,4 & Gabor Papai 1,2,3,4 Transcription preinitiation complex assembly on the promoters of protein encoding genes is nucleated in vivo by TFIID composed of the TATA-box Binding Protein (TBP) and 13 TBP- associate factors (Tafs) providing regulatory and chromatin binding functions. Here we present the cryo-electron microscopy structure of promoter-bound yeast TFIID at a resolu- 1234567890():,; tion better than 5 Å, except for a flexible domain. We position the crystal structures of several subunits and, in combination with cross-linking studies, describe the quaternary organization of TFIID. The compact tri lobed architecture is stabilized by a topologically closed Taf5-Taf6 tetramer. We confirm the unique subunit stoichiometry prevailing in TFIID and uncover a hexameric arrangement of Tafs containing a histone fold domain in the Twin lobe. 1 Department of Integrated Structural Biology, Equipe labellisée Ligue Contre le Cancer, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch 67404, France. 2 Centre National de la Recherche Scientifique, UMR7104, 67404 Illkirch, France. 3 Institut National de la Santé et de la Recherche Médicale, U1258, 67404 Illkirch, France. 4 Université de Strasbourg, Illkirch 67404, France. 5 Institute for Systems Biology, Seattle, WA 98109, USA. These authors contributed equally: Olga Kolesnikova, Adam Ben-Shem. Correspondence and requests for materials should be addressed to P.S. (email: [email protected]) or to G.P.
[Show full text]
Aneuploidy: Using Genetic Instability to Preserve a Haploid Genome?
Health Science Campus FINAL APPROVAL OF DISSERTATION Doctor of Philosophy in Biomedical Science (Cancer Biology) Aneuploidy: Using genetic instability to preserve a haploid genome? Submitted by: Ramona Ramdath In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Science Examination Committee Signature/Date Major Advisor: David Allison, M.D., Ph.D. Academic James Trempe, Ph.D. Advisory Committee: David Giovanucci, Ph.D. Randall Ruch, Ph.D. Ronald Mellgren, Ph.D. Senior Associate Dean College of Graduate Studies Michael S. Bisesi, Ph.D. Date of Defense: April 10, 2009 Aneuploidy: Using genetic instability to preserve a haploid genome? Ramona Ramdath University of Toledo, Health Science Campus 2009 Dedication I dedicate this dissertation to my grandfather who died of lung cancer two years ago, but who always instilled in us the value and importance of education. And to my mom and sister, both of whom have been pillars of support and stimulating conversations. To my sister, Rehanna, especially- I hope this inspires you to achieve all that you want to in life, academically and otherwise. ii Acknowledgements As we go through these academic journeys, there are so many along the way that make an impact not only on our work, but on our lives as well, and I would like to say a heartfelt thank you to all of those people: My Committee members- Dr. James Trempe, Dr. David Giovanucchi, Dr. Ronald Mellgren and Dr. Randall Ruch for their guidance, suggestions, support and confidence in me. My major advisor- Dr. David Allison, for his constructive criticism and positive reinforcement.
[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]
Molecular Mechanisms of Ribosomal Protein Gene Coregulation
Downloaded from genesdev.cshlp.org on October 3, 2021 - Published by Cold Spring Harbor Laboratory Press Molecular mechanisms of ribosomal protein gene coregulation Rohit Reja, Vinesh Vinayachandran, Sujana Ghosh, and B. Franklin Pugh Center for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, Pennsylvania 16802, USA The 137 ribosomal protein genes (RPGs) of Saccharomyces provide a model for gene coregulation. We examined the positional and functional organization of their regulators (Rap1 [repressor activator protein 1], Fhl1, Ifh1, Sfp1, and Hmo1), the transcription machinery (TFIIB, TFIID, and RNA polymerase II), and chromatin at near-base-pair res- olution using ChIP-exo, as RPGs are coordinately reprogrammed. Where Hmo1 is enriched, Fhl1, Ifh1, Sfp1, and Hmo1 cross-linked broadly to promoter DNA in an RPG-specific manner and demarcated by general minor groove widening. Importantly, Hmo1 extended 20–50 base pairs (bp) downstream from Fhl1. Upon RPG repression, Fhl1 remained in place. Hmo1 dissociated, which was coupled to an upstream shift of the +1 nucleosome, as reflected by the Hmo1 extension and core promoter region. Fhl1 and Hmo1 may create two regulatable and positionally distinct barriers, against which chromatin remodelers position the +1 nucleosome into either an activating or a repressive state. Consistent with in vitro studies, we found that specific TFIID subunits, in addition to cross-linking at the core promoter, made precise cross-links at Rap1 sites, which we interpret to reflect native Rap1–TFIID interactions. Our findings suggest how sequence-specific DNA binding regulates nucleosome positioning and transcription complex assembly >300 bp away and how coregulation coevolved with coding sequences.
[Show full text]
The Transition from Primary Colorectal Cancer to Isolated Peritoneal Malignancy
medRxiv preprint doi: https://doi.org/10.1101/2020.02.24.20027318; this version posted February 25, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted medRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license . The transition from primary colorectal cancer to isolated peritoneal malignancy is associated with a hypermutant, hypermethylated state Sally Hallam1, Joanne Stockton1, Claire Bryer1, Celina Whalley1, Valerie Pestinger1, Haney Youssef1, Andrew D Beggs1 1 = Surgical Research Laboratory, Institute of Cancer & Genomic Science, University of Birmingham, B15 2TT. Correspondence to: Andrew Beggs, [email protected] KEYWORDS: Colorectal cancer, peritoneal metastasis ABBREVIATIONS: Colorectal cancer (CRC), Colorectal peritoneal metastasis (CPM), Cytoreductive surgery and heated intraperitoneal chemotherapy (CRS & HIPEC), Disease free survival (DFS), Differentially methylated regions (DMR), Overall survival (OS), TableFormalin fixed paraffin embedded (FFPE), Hepatocellular carcinoma (HCC) ARTICLE CATEGORY: Research article NOTE: This preprint reports new research that has not been certified by peer review and should not be used to guide clinical practice. 1 medRxiv preprint doi: https://doi.org/10.1101/2020.02.24.20027318; this version posted February 25, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted medRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license . NOVELTY AND IMPACT: Colorectal peritoneal metastasis (CPM) are associated with limited and variable survival despite patient selection using known prognostic factors and optimal currently available treatments.
[Show full text]
TAF10 Complex Provides Evidence for Nuclear Holo&Ndash;TFIID Assembly from Preform
ARTICLE Received 13 Aug 2014 | Accepted 2 Dec 2014 | Published 14 Jan 2015 DOI: 10.1038/ncomms7011 OPEN Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules Simon Trowitzsch1,2, Cristina Viola1,2, Elisabeth Scheer3, Sascha Conic3, Virginie Chavant4, Marjorie Fournier3, Gabor Papai5, Ima-Obong Ebong6, Christiane Schaffitzel1,2, Juan Zou7, Matthias Haffke1,2, Juri Rappsilber7,8, Carol V. Robinson6, Patrick Schultz5, Laszlo Tora3 & Imre Berger1,2,9 General transcription factor TFIID is a cornerstone of RNA polymerase II transcription initiation in eukaryotic cells. How human TFIID—a megadalton-sized multiprotein complex composed of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs)— assembles into a functional transcription factor is poorly understood. Here we describe a heterotrimeric TFIID subcomplex consisting of the TAF2, TAF8 and TAF10 proteins, which assembles in the cytoplasm. Using native mass spectrometry, we define the interactions between the TAFs and uncover a central role for TAF8 in nucleating the complex. X-ray crystallography reveals a non-canonical arrangement of the TAF8–TAF10 histone fold domains. TAF2 binds to multiple motifs within the TAF8 C-terminal region, and these interactions dictate TAF2 incorporation into a core–TFIID complex that exists in the nucleus. Our results provide evidence for a stepwise assembly pathway of nuclear holo–TFIID, regulated by nuclear import of preformed cytoplasmic submodules. 1 European Molecular Biology Laboratory, Grenoble Outstation, 6 rue Jules Horowitz, 38042 Grenoble, France. 2 Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble, France. 3 Cellular Signaling and Nuclear Dynamics Program, Institut de Geńe´tique et de Biologie Molećulaire et Cellulaire, UMR 7104, INSERM U964, 1 rue Laurent Fries, 67404 Illkirch, France.
[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]
BET Family Members Bdf1/2 Modulate Global Transcription Initiation and Elongation in Saccharomyces Cerevisiae Rafal Donczew*, Steven Hahn*
RESEARCH ARTICLE BET family members Bdf1/2 modulate global transcription initiation and elongation in Saccharomyces cerevisiae Rafal Donczew*, Steven Hahn* Fred Hutchinson Cancer Research Center, Division of Basic Sciences, Seattle, United States Abstract Human bromodomain and extra-terminal domain (BET) family members are promising targets for therapy of cancer and immunoinflammatory diseases, but their mechanisms of action and functional redundancies are poorly understood. Bdf1/2, yeast homologues of the human BET factors, were previously proposed to target transcription factor TFIID to acetylated histone H4, analogous to bromodomains that are present within the largest subunit of metazoan TFIID. We investigated the genome-wide roles of Bdf1/2 and found that their important contributions to transcription extend beyond TFIID function as transcription of many genes is more sensitive to Bdf1/2 than to TFIID depletion. Bdf1/2 co-occupy the majority of yeast promoters and affect preinitiation complex formation through recruitment of TFIID, Mediator, and basal transcription factors to chromatin. Surprisingly, we discovered that hypersensitivity of genes to Bdf1/2 depletion results from combined defects in transcription initiation and early elongation, a striking functional similarity to human BET proteins, most notably Brd4. Our results establish Bdf1/2 as critical for yeast transcription and provide important mechanistic insights into the function of BET proteins in all eukaryotes. *For correspondence: [email protected] (RD); Introduction [email protected] (SH) Bromodomains (BDs) are reader modules that allow protein targeting to chromatin via interactions with acetylated histone tails. BD-containing factors are usually involved in gene transcription, and Competing interests: The their deregulation has been implicated in a spectrum of cancers and immunoinflammatory and neu- authors declare that no rological conditions (Fujisawa and Filippakopoulos, 2017; Wang et al., 2021).
[Show full text]
(R)-PFI-2 Is a Potent and Selective Inhibitor of SETD7 Methyltransferase Activity in Cells
(R)-PFI-2 is a potent and selective inhibitor of SETD7 methyltransferase activity in cells Dalia Barsyte-Lovejoya,1,2, Fengling Lia,1, Menno J. Oudhoffb,1, John H. Tatlockc,1, Aiping Donga, Hong Zenga, Hong Wua, Spencer A. Freemand, Matthieu Schapiraa,e, Guillermo A. Senisterraa, Ekaterina Kuznetsovaa, Richard Marcellusf, Abdellah Allali-Hassania, Steven Kennedya, Jean-Philippe Lambertg, Amber L. Couzensg, Ahmed Amanf, Anne-Claude Gingrasg,h, Rima Al-Aware,f, Paul V. Fishi,3, Brian S. Gerstenbergerj, Lee Robertsk, Caroline L. Bennl, Rachel L. Grimleyl, Mitchell J. S. Braamb, Fabio M. V. Rossib,m, Marius Sudoln, Peter J. Browna, Mark E. Bunnagek, Dafydd R. Owenk, Colby Zaphb,o, Masoud Vedadia,e,2, and Cheryl H. Arrowsmitha,p,2 aStructural Genomics Consortium, University of Toronto, Toronto, ON, Canada M5G 1L7; bBiomedical Research Centre, University of British Columbia, Vancouver, BC, Canada V6T1Z3; cWorldwide Medicinal Chemistry, Pfizer Worldwide Research and Development, San Diego, CA 92121; dDepartment of Microbiology and Immunology, University of British Columbia, Vancouver, BC, Canada V6T1Z3; eDepartment of Pharmacology and Toxicology, University of Toronto, Toronto, ON, Canada M5S 1A8; fDrug Discovery Program, Ontario Institute for Cancer Research, Toronto, ON, Canada M5G 0A3; gCentre for Systems Biology, Lunenfeld-Tanenbaum Research Institute, Toronto, ON, Canada M5G 1X5; hDepartment of Molecular Genetics, University of Toronto, Toronto, ON, Canada M5S 1A8; iWorldwide Medicinal Chemistry, Pfizer Worldwide Research and Development,
[Show full text]
Granulocyte Colony-Stimulating Factor-Induced TAF9 Modulates P53-TRIAP1-CASP3 Axis to Prevent Retinal Ganglion Cell Death After Optic Nerve Ischemia
Granulocyte Colony-Stimulating Factor-Induced TAF9 Modulates P53-TRIAP1-CASP3 Axis to Prevent Retinal Ganglion Cell Death after Optic Nerve Ischemia Yao-Tseng Wen Buddhist Tzu Chi General Hospital Hualien: Hualien Tzu Chi Hospital Keh-Liang Lin Chung Shan Medical University Hospital Chin-Te Huang Tzu Chi University Rong Kung Tsai ( [email protected] ) Hualien Tzu Chi Hospital https://orcid.org/0000-0001-8760-5739 Research article Keywords: Granulocyte colony-stimulating factor, Rat anterior ischemic optic neuropathy model, Retinal ganglion cell, TBP associated factor 9, TP53, TRIAP1 Posted Date: January 6th, 2021 DOI: https://doi.org/10.21203/rs.3.rs-138908/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/25 Abstract Background Optic nerve head (ONH) infarct can result in progressive retinal ganglion cell (RGC) death. Some evidences indicated that the granulocyte colony-stimulating factor (GCSF) provides positive effects against ischemic damage on RGCs. However, protective mechanisms of the GCSF after ONH infarct are complex and remain unclear. Methods To investigate the complex mechanisms, the transcriptome proles of the GCSF-treated retinas were examined using microarray technology. The retinal mRNA samples on days 3 and 7 post rat anterior ischemic optic neuropathy model (rAION) were analyzed by microarray and bioinformatics analyses. To evaluate the TAF9 function in RGC apoptosis, GCSF plus TAF9 siRNA-treated rats were evaluated using retrograde labeling with FluoroGold assay, TUNEL assay, and Western blotting in a rAION. Results GCSF treatment inuenced 3101 genes and 3332 genes on days 3 and 7 post rAION, respectively.
[Show full text]