ARL4D / ARF4L (1-201, His-Tag) Human Protein Product Data

Total Page：16

File Type：pdf, Size：1020Kb

ARL4D / ARF4L (1-201, His-Tag) Human Protein Product Data

OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for AR50077PU-S ARL4D / ARF4L (1-201, His-tag) Human Protein Product data: Product Type: Recombinant Proteins Description: ARL4D / ARF4L (1-201, His-tag) human recombinant protein, 0.1 mg Species: Human Expression Host: E. coli Tag: His-tag Predicted MW: 24.3 kDa Concentration: lot specific Purity: >90% by SDS - PAGE Buffer: Presentation State: Purified State: Liquid purified protein Buffer System: 20 mM Tris-HCl buffer (pH 8.0) containing 2mM DTT, 20% glycerol, 200mM NaCl Preparation: Liquid purified protein Protein Description: Recombinant human ARL4D protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Storage: Store undiluted at 2-8°C for one week or (in aliquots) at -20°C to -80°C for longer. Avoid repeated freezing and thawing. Stability: Shelf life: one year from despatch. RefSeq: NP_001652 Locus ID: 379 UniProt ID: P49703 Cytogenetics: 17q21.31 Synonyms: ARF4L; ARL6 Summary: ADP-ribosylation factor 4D is a member of the ADP-ribosylation factor family of GTP-binding proteins. ARL4D is closely similar to ARL4A and ARL4C and each has a nuclear localization signal and an unusually high guanine nucleotide exchange rate. This protein may play a role in membrane-associated intracellular trafficking. Mutations in this gene have been associated with Bardet-Biedl syndrome (BBS). [provided by RefSeq, Jul 2008] This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 ARL4D / ARF4L (1-201, His-tag) Human Protein – AR50077PU-S Product images: This product is to be used for laboratory only. Not for diagnostic or therapeutic use. ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 2 / 2.

Copy Link

Recommended publications

Anti-ARL4A Antibody (ARG41291)
Product datasheet [email protected] ARG41291 Package: 100 μl anti-ARL4A antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes ARL4A Tested Reactivity Hu, Ms, Rat Tested Application ICC/IF, IHC-P Host Rabbit Clonality Polyclonal Isotype IgG Target Name ARL4A Antigen Species Human Immunogen Recombinant fusion protein corresponding to aa. 121-200 of Human ARL4A (NP_001032241.1). Conjugation Un-conjugated Alternate Names ARL4; ADP-ribosylation factor-like protein 4A Application Instructions Application table Application Dilution ICC/IF 1:50 - 1:200 IHC-P 1:50 - 1:200 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Calculated Mw 23 kDa Properties Form Liquid Purification Affinity purified. Buffer PBS (pH 7.3), 0.02% Sodium azide and 50% Glycerol. Preservative 0.02% Sodium azide Stabilizer 50% Glycerol 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. 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. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Gene Symbol ARL4A Gene Full Name ADP-ribosylation factor-like 4A Background ADP-ribosylation factor-like 4A is a member of the ADP-ribosylation factor family of GTP-binding proteins. ARL4A is similar to ARL4C and ARL4D and each has a nuclear localization signal and an unusually high guaninine nucleotide exchange rate.
[Show full text]
A Database for Human and Yeast Genes Involved in Telomere Maintenance Delia M
Braun et al. BMC Genetics (2018) 19:32 https://doi.org/10.1186/s12863-018-0617-8 DATABASE Open Access TelNet - a database for human and yeast genes involved in telomere maintenance Delia M. Braun, Inn Chung, Nick Kepper, Katharina I. Deeg and Karsten Rippe* Abstract Background: The ends of linear chromosomes, the telomeres, comprise repetitive DNA sequences in complex with proteins that protects them from being processed by the DNA repair machinery. Cancer cells need to counteract the shortening of telomere repeats during replication for their unlimited proliferation by reactivating the reverse transcriptase telomerase or by using the alternative lengthening of telomeres (ALT) pathway. The different telomere maintenance (TM) mechanisms appear to involve hundreds of proteins but their telomere repeat length related activities are only partly understood. Currently, a database that integrates information on TM relevant genes is missing. Description: To provide a resource for studies that dissect TM features, we here introduce the TelNet database at http://www.cancertelsys.org/telnet/. It offers a comprehensive compilation of more than 2000 human and 1100 yeast genes linked to telomere maintenance. These genes were annotated in terms of TM mechanism, associated specific functions and orthologous genes, a TM significance score and information from peer-reviewed literature. This TM information can be retrieved via different search and view modes and evaluated for a set of genes as demonstrated for an exemplary application. Conclusion: TelNet supports the annotation of genes identified from bioinformatics analysis pipelines to reveal possible connections with TM networks. We anticipate that TelNet will be a helpful resource for researchers that study telomeres.
[Show full text]
Temporal Chip-On-Chip of RNA-Polymerase-II to Detect Novel Gene Activation Events During Photoreceptor Maturation
Molecular Vision 2010; 16:252-271 <http://www.molvis.org/molvis/v16/a32> © 2010 Molecular Vision Received 12 July 2009 | Accepted 10 February 2010 | Published 17 February 2010 Temporal ChIP-on-Chip of RNA-Polymerase-II to detect novel gene activation events during photoreceptor maturation Padmaja Tummala, Raghuveer S. Mali, Eduardo Guzman, Xiao Zhang, Kenneth P. Mitton (The first two authors contributed equally to this work.) Eye Research Institute, Oakland University, Rochester, MI Purpose: During retinal development, post-mitotic neural progenitor cells must activate thousands of genes to complete synaptogenesis and terminal maturation. While many of these genes are known, others remain beyond the sensitivity of expression microarray analysis. Some of these elusive gene activation events can be detected by mapping changes in RNA polymerase-II (Pol-II) association around transcription start sites. Methods: High-resolution (35 bp) chromatin immunoprecipitation (ChIP)-on-chip was used to map changes in Pol-II binding surrounding 26,000 gene transcription start sites during photoreceptor maturation of the mouse neural retina, comparing postnatal age 25 (P25) to P2. Coverage was 10–12 kb per transcription start site, including 2.5 kb downstream. Pol-II-active regions were mapped to the mouse genomic DNA sequence by using computational methods (Tiling Analysis Software-TAS program), and the ratio of maximum Pol-II binding (P25/P2) was calculated for each gene. A validation set of 36 genes (3%), representing a full range of Pol-II signal ratios (P25/P2), were examined with quantitative ChIP assays for transcriptionally active Pol-II. Gene expression assays were also performed for 19 genes of the validation set, again on independent samples.
[Show full text]
1 UST College of Science Department of Biological Sciences
UST College of Science Department of Biological Sciences 1 Pharmacogenomics of Myofascial Pain Syndrome An Undergraduate Thesis Submitted to the Department of Biological Sciences College of Science University of Santo Tomas In Partial Fulfillment of the Requirements for the Degree of Bachelor of Science in Biology Jose Marie V. Lazaga Marc Llandro C. Fernandez May 2021 UST College of Science Department of Biological Sciences 2 PANEL APPROVAL SHEET This undergraduate research manuscript entitled: Pharmacogenomics of Myofascial Pain Syndrome prepared and submitted by Jose Marie V. Lazaga and Marc Llandro C. Fernandez, was checked and has complied with the revisions and suggestions requested by panel members after thorough evaluation. This final version of the manuscript is hereby approved and accepted for submission in partial fulfillment of the requirements for the degree of Bachelor of Science in Biology. Noted by: Asst. Prof. Marilyn G. Rimando, PhD Research adviser, Bio/MicroSem 602-603 Approved by: Bio/MicroSem 603 panel member Bio/MicroSem 603 panel member Date: Date: UST College of Science Department of Biological Sciences 3 DECLARATION OF ORIGINALITY We hereby affirm that this submission is our own work and that, to the best of our knowledge and belief, it contains no material previously published or written by another person nor material to which a substantial extent has been accepted for award of any other degree or diploma of a university or other institute of higher learning, except where due acknowledgement is made in the text. We also declare that the intellectual content of this undergraduate research is the product of our work, even though we may have received assistance from others on style, presentation, and language expression.
[Show full text]
Genomic and Transcriptome Analysis Revealing an Oncogenic Functional Module in Meningiomas
Neurosurg Focus 35 (6):E3, 2013 ©AANS, 2013 Genomic and transcriptome analysis revealing an oncogenic functional module in meningiomas XIAO CHANG, PH.D.,1 LINGLING SHI, PH.D.,2 FAN GAO, PH.D.,1 JONATHAN RUssIN, M.D.,3 LIYUN ZENG, PH.D.,1 SHUHAN HE, B.S.,3 THOMAS C. CHEN, M.D.,3 STEVEN L. GIANNOTTA, M.D.,3 DANIEL J. WEISENBERGER, PH.D.,4 GAbrIEL ZADA, M.D.,3 KAI WANG, PH.D.,1,5,6 AND WIllIAM J. MAck, M.D.1,3 1Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, California; 2GHM Institute of CNS Regeneration, Jinan University, Guangzhou, China; 3Department of Neurosurgery, Keck School of Medicine, University of Southern California, Los Angeles, California; 4USC Epigenome Center, Keck School of Medicine, University of Southern California, Los Angeles, California; 5Department of Psychiatry, Keck School of Medicine, University of Southern California, Los Angeles, California; and 6Division of Bioinformatics, Department of Preventive Medicine, Keck School of Medicine, University of Southern California, Los Angeles, California Object. Meningiomas are among the most common primary adult brain tumors. Although typically benign, roughly 2%–5% display malignant pathological features. The key molecular pathways involved in malignant trans- formation remain to be determined. Methods. Illumina expression microarrays were used to assess gene expression levels, and Illumina single- nucleotide polymorphism arrays were used to identify copy number variants in benign, atypical, and malignant me- ningiomas (19 tumors, including 4 malignant ones). The authors also reanalyzed 2 expression data sets generated on Affymetrix microarrays (n = 68, including 6 malignant ones; n = 56, including 3 malignant ones).
[Show full text]
Nº Ref Uniprot Proteína Péptidos Identificados Por MS/MS 1 P01024
Document downloaded from http://www.elsevier.es, day 26/09/2021. This copy is for personal use. Any transmission of this document by any media or format is strictly prohibited. Nº Ref Uniprot Proteína Péptidos identificados 1 P01024 CO3_HUMAN Complement C3 OS=Homo sapiens GN=C3 PE=1 SV=2 por 162MS/MS 2 P02751 FINC_HUMAN Fibronectin OS=Homo sapiens GN=FN1 PE=1 SV=4 131 3 P01023 A2MG_HUMAN Alpha-2-macroglobulin OS=Homo sapiens GN=A2M PE=1 SV=3 128 4 P0C0L4 CO4A_HUMAN Complement C4-A OS=Homo sapiens GN=C4A PE=1 SV=1 95 5 P04275 VWF_HUMAN von Willebrand factor OS=Homo sapiens GN=VWF PE=1 SV=4 81 6 P02675 FIBB_HUMAN Fibrinogen beta chain OS=Homo sapiens GN=FGB PE=1 SV=2 78 7 P01031 CO5_HUMAN Complement C5 OS=Homo sapiens GN=C5 PE=1 SV=4 66 8 P02768 ALBU_HUMAN Serum albumin OS=Homo sapiens GN=ALB PE=1 SV=2 66 9 P00450 CERU_HUMAN Ceruloplasmin OS=Homo sapiens GN=CP PE=1 SV=1 64 10 P02671 FIBA_HUMAN Fibrinogen alpha chain OS=Homo sapiens GN=FGA PE=1 SV=2 58 11 P08603 CFAH_HUMAN Complement factor H OS=Homo sapiens GN=CFH PE=1 SV=4 56 12 P02787 TRFE_HUMAN Serotransferrin OS=Homo sapiens GN=TF PE=1 SV=3 54 13 P00747 PLMN_HUMAN Plasminogen OS=Homo sapiens GN=PLG PE=1 SV=2 48 14 P02679 FIBG_HUMAN Fibrinogen gamma chain OS=Homo sapiens GN=FGG PE=1 SV=3 47 15 P01871 IGHM_HUMAN Ig mu chain C region OS=Homo sapiens GN=IGHM PE=1 SV=3 41 16 P04003 C4BPA_HUMAN C4b-binding protein alpha chain OS=Homo sapiens GN=C4BPA PE=1 SV=2 37 17 Q9Y6R7 FCGBP_HUMAN IgGFc-binding protein OS=Homo sapiens GN=FCGBP PE=1 SV=3 30 18 O43866 CD5L_HUMAN CD5 antigen-like OS=Homo
[Show full text]
Lin28a/Let-7 Pathway Modulates the Hox Code Via Polycomb Regulation
RESEARCH ARTICLE Lin28a/let-7 pathway modulates the Hox code via Polycomb regulation during axial patterning in vertebrates Tempei Sato1,2,3, Kensuke Kataoka1,3, Yoshiaki Ito1,4, Shigetoshi Yokoyama2,5, Masafumi Inui2,6, Masaki Mori1,7, Satoru Takahashi8, Keiichi Akita9, Shuji Takada2, Hiroe Ueno-Kudoh2,10, Hiroshi Asahara1,2,11,12* 1Department of Systems BioMedicine, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University, Tokyo, Japan; 2Department of Systems BioMedicine, National Research Institute for Child Health and Development, Tokyo, Japan; 3Research Fellow of Japan Society for the Promotion of Science, Tokyo, Japan; 4Research Core, Tokyo Medical and Dental University, Tokyo, Japan; 5Laboratory of Metabolism, National Institutes of Health, Bethesda, United States; 6Laboratory of Animal Regeneration Systemology, Meiji University, Kanagawa, Japan; 7Department of Medical Chemistry, Shiga University of Medical Science, Shiga, Japan; 8Department of Anatomy and Embryology, University of Tsukuba, Ibaraki, Japan; 9Department of Clinical Anatomy, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University, Tokyo, Japan; 10Reproduction Center, Yokohama City University, Yokohama, Japan; 11AMED- CREST, Japan Agency for Medical Research and Development (AMED), Tokyo, Japan; 12Department of Molecular Medicine, The Scripps Research Institute, La Jolla, United States Abstract The body plan along the anteroposterior axis and regional identities are specified by *For correspondence: the spatiotemporal expression of Hox genes. Multistep controls are required for their unique [email protected] expression patterns; however, the molecular mechanisms behind the tight control of Hox genes are not fully understood. In this study, we demonstrated that the Lin28a/let-7 pathway is critical for Competing interests: The axial elongation.
[Show full text]
ARL4D CRISPR/Cas9 KO Plasmid (M): Sc-429859
SANTA CRUZ BIOTECHNOLOGY, INC. ARL4D CRISPR/Cas9 KO Plasmid (m): sc-429859 BACKGROUND APPLICATIONS The Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR) and ARL4D CRISPR/Cas9 KO Plasmid (m) is recommended for the disruption of CRISPR-associated protein (Cas9) system is an adaptive immune response gene expression in mouse cells. defense mechanism used by archea and bacteria for the degradation of foreign genetic material (4,6). This mechanism can be repurposed for other 20 nt non-coding RNA sequence: guides Cas9 functions, including genomic engineering for mammalian systems, such as to a speciﬁc target location in the genomic DNA gene knockout (KO) (1,2,3,5). CRISPR/Cas9 KO Plasmid products enable the U6 promoter: drives gRNA scaffold: helps Cas9 identification and cleavage of specific genes by utilizing guide RNA (gRNA) expression of gRNA bind to target DNA sequences derived from the Genome-scale CRISPR Knock-Out (GeCKO) v2 library developed in the Zhang Laboratory at the Broad Institute (3,5). Termination signal Green Fluorescent Protein: to visually REFERENCES verify transfection CRISPR/Cas9 Knockout Plasmid CBh (chicken β-Actin 1. Cong, L., et al. 2013. Multiplex genome engineering using CRISPR/Cas hybrid) promoter: drives systems. Science 339: 819-823. 2A peptide: expression of Cas9 allows production of both Cas9 and GFP from the 2. Mali, P., et al. 2013. RNA-guided human genome engineering via Cas9. same CBh promoter Science 339: 823-826. Nuclear localization signal 3. Ran, F.A., et al. 2013. Genome engineering using the CRISPR-Cas9 system. Nuclear localization signal SpCas9 ribonuclease Nat. Protoc. 8: 2281-2308.
[Show full text]
Integrative Systems Biology Applied to Toxicology
Integrative Systems Biology Applied to Toxicology Kristine Grønning Kongsbak PhD Thesis January 2015 Integrative Systems Biology Applied to Toxicology Kristine Grønning Kongsbak Søborg 2015 FOOD-PHD-2015 PhD Thesis 2015 Supervisors Professor Anne Marie Vinggaard Senior Scientist Niels Hadrup Division of Toxicology and Risk Assessment National Food Institute Technical University of Denmark Associate Professor Aron Charles Eklund Center for Biological Sequence Analysis Department for Systems Biology Technical University of Denmark Associate Professor Karine Audouze Molécules Thérapeutiques In Silico Paris Diderot University Funding This project was supported financially by the Ministry of Food, Agriculture and Fisheries of Denmark and the Technical University of Denmark. ©Kristine Grønning Kongsbak FOOD-PHD: ISBN 978-87-93109-30-8 Division of Toxicology and Risk Assessment National Food Institute Technical University of Denmark DK-2860 Søborg, Denmark www.food.dtu.dk 4 Summary Humans are exposed to various chemical agents through food, cosmetics, pharma- ceuticals and other sources. Exposure to chemicals is suspected of playing a main role in the development of some adverse health effects in humans. Additionally, European regulatory authorities have recognized the risk associated with combined exposure to multiple chemicals. Testing all possible combinations of the tens of thousands environmental chemicals is impractical. This PhD project was launched to apply existing computational systems biology methods to toxicological research. In this thesis, I present in three projects three different approaches to using com- putational toxicology to aid classical toxicological investigations. In project I, we predicted human health effects of five pesticides using publicly available data. We obtained a grouping of the chemical according to their potential human health ef- fects that were in concordance with their effects in experimental animals.
[Show full text]
Endoglin Integrates BMP and Wnt Signalling to Induce Haematopoiesis Through JDP2
ARTICLE Received 22 Jul 2015 | Accepted 2 Sep 2016 | Published 7 Oct 2016 DOI: 10.1038/ncomms13101 OPEN Endoglin integrates BMP and Wnt signalling to induce haematopoiesis through JDP2 June Baik1, Alessandro Magli1, Naoyuki Tahara2,3, Scott A. Swanson4, Naoko Koyano-Nakagawa1, Luciene Borges1, Ron Stewart4, Daniel J. Garry1, Yasuhiko Kawakami2,3, James A. Thomson4 & Rita C.R. Perlingeiro1 Mechanisms of haematopoietic and cardiac patterning remain poorly understood. Here we show that the BMP and Wnt signalling pathways are integrated in an endoglin (Eng)-dependent manner in cardiac and haematopoietic lineage speciﬁcation. Eng is expressed in early mesoderm and marks both haematopoietic and cardiac progenitors. In the absence of Eng, yolk sacs inappropriately express the cardiac marker, Nkx2.5. Conversely, high levels of Eng in vitro and in vivo increase haematopoiesis and inhibit cardiogenesis. Levels of Eng determine the activation of both BMP and Wnt pathways, which are integrated downstream of Eng by phosphorylation of Smad1 by Gsk3. By interrogating Eng-dependent Wnt-mediated transcriptional changes, we identify Jdp2 as a key Eng-dependent Wnt target, sufﬁcient to establish haematopoietic fate in early mesoderm when BMP and Wnt crosstalk is disturbed. These studies provide mechanistic insight into the integration of BMP and Wnt signalling in the establishment of haematopoietic and cardiac progenitors during embryogenesis. 1 Department of Medicine, Lillehei Heart Institute, University of Minnesota, Minneapolis, Minnesota 55455, USA. 2 Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota 55455, USA. 3 Stem Cell Institute, University of Minnesota, Minneapolis, Minnesota 55455, USA. 4 Regerative Biology, Morgridge Institute for Research, Madison, Wisconsin 53715, USA.
[Show full text]
ARL4D (H-2): Sc-271274
SANTA CRUZ BIOTECHNOLOGY, INC. ARL4D (H-2): sc-271274 BACKGROUND APPLICATIONS ADP-ribosylation factors (ARFs) are highly conserved guanine nucleotide- ARL4D (H-2) is recommended for detection of ARL4D of mouse, rat and binding proteins that enhance the ADP-ribosyltransferase activity of cholera human origin by Western Blotting (starting dilution 1:100, dilution range toxin. ARF’s are important in eukaryotic vesicular trafficking pathways and 1:100-1:1000), immunoprecipitation [1-2 µg per 100-500 µg of total protein activating phospholipase D. ARL4D (ADP-ribosylation factor-like 4D), also (1 ml of cell lysate)], immunofluorescence (starting dilution 1:50, dilution known as ARL6 or ARF4L, is a 201 amino acid nuclear protein that is a mem- range 1:50-1:500) and solid phase ELISA (starting dilution 1:30, dilution range ber of the ADP-ribosylation factor family of GTP-binding proteins. ARL4D may 1:30-1:3000). play a role in membrane-associated intracellular trafficking and may promote Suitable for use as control antibody for ARL4D siRNA (h): sc-94138, ARL4D ARF6 activation and modulate actin remodeling by regulating ARNO. It is siRNA (m): sc-141243, ARL4D shRNA Plasmid (h): sc-94138-SH, ARL4D suggested that mutations of ARL4D is associated with Bardet-Biedl syndrome. shRNA Plasmid (m): sc-141243-SH, ARL4D shRNA (h) Lentiviral Particles: sc-94138-V and ARL4D shRNA (m) Lentiviral Particles: sc-141243-V. REFERENCES Molecular Weight of ARL4D: 20 kDa. 1. Smith, S.A., et al. 1995. Isolation and mapping of a gene encoding a novel human ADP-ribosylation factor on chromosome 17q12-q21.
[Show full text]
Regulatory Elements Inserted Into Aavs Confer Preferential Activity in Cortical Interneurons
Research Article: Methods/New Tools Novel Tools and Methods Regulatory Elements Inserted into AAVs Confer Preferential Activity in Cortical Interneurons Anna N. Rubin,1,* Ruchi Malik,2,* Kathleen K. A. Cho,2 Kenneth J. Lim,1 Susan Lindtner,1 Sarah E. Robinson Schwartz,2 Daniel Vogt,1 Vikaas S. Sohal,2 and John L. R. Rubenstein1 https://doi.org/10.1523/ENEURO.0211-20.2020 1Nina Ireland Laboratory of Developmental Neurobiology, Department of Psychiatry, University of California San Francisco Weill Institute for Neurosciences, University of California San Francisco, San Francisco, CA 94158 and 2Center for Integrative Neuroscience, Department of Psychiatry, University of California San Francisco Weill Institute for Neurosciences, Kavli Institute for Fundamental Neuroscience, University of California San Francisco, San Francisco, CA 94158 Abstract Cortical interneuron (CIN) dysfunction is thought to play a major role in neuropsychiatric conditions like epi- lepsy, schizophrenia and autism. It is therefore essential to understand how the development, physiology, and functions of CINs influence cortical circuit activity and behavior in model organisms such as mice and prima- tes. While transgenic driver lines are powerful tools for studying CINs in mice, this technology is limited in other species. An alternative approach is to use viral vectors such as AAV, which can be used in multiple spe- cies including primates and also have potential for therapeutic use in humans. Thus, we sought to discover gene regulatory enhancer elements (REs) that can be used in viral vectors to drive expression in specific cell types. The present study describes the systematic genome-wide identification of putative REs (pREs) that are preferentially active in immature CINs by histone modification chromatin immunoprecipitation and sequencing (ChIP-seq).
[Show full text]