DHX38 Antibody Cat

DHX38 Antibody Cat. No.: 19-349 DHX38 Antibody Immunohistochemistry of paraffin-embedded human gastric cancer using DHX38 antibody (19-349) at dilution of 1:150 (40x lens). Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human, Mouse, Rat Recombinant fusion protein containing a sequence corresponding to amino acids IMMUNOGEN: 1133-1227 of human DHX38 (NP_054722.2). TESTED APPLICATIONS: IHC, WB WB: ,1:1000 - 1:2000 APPLICATIONS: IHC: ,1:50 - 1:200 POSITIVE CONTROL: 1) HeLa 2) SKOV3 September 27, 2021 1 https://www.prosci-inc.com/dhx38-antibody-19-349.html 3) U-87MG 4) MCF7 5) DU145 6) Mouse testis PREDICTED MOLECULAR Observed: 140kDa WEIGHT: Properties PURIFICATION: Affinity purification CLONALITY: Polyclonal ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: PBS with 0.02% sodium azide, 50% glycerol, pH7.3. STORAGE CONDITIONS: Store at -20˚C. Avoid freeze / thaw cycles. Additional Info OFFICIAL SYMBOL: DHX38 DDX38, PRP16, PRPF16, RP84, pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16, ATP-dependent RNA helicase DHX38, DEAD/H (Asp-Glu-Ala-Asp/His) box ALTERNATE NAMES: polypeptide 38, DEAH (Asp-Glu-Ala-His) box polypeptide 38, DEAH box protein 38, PRP16 homolog of S.cerevisiae GENE ID: 9785 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their BACKGROUND: distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. The protein encoded by this gene is a member of the DEAD/H box family of splicing factors. This protein resembles yeast Prp16 more closely than other DEAD/H family members. It is an ATPase and essential for the catalytic step II in pre-mRNA splicing process. September 27, 2021 2 https://www.prosci-inc.com/dhx38-antibody-19-349.html ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 27, 2021 3 https://www.prosci-inc.com/dhx38-antibody-19-349.html.

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DHX38 Antibody - Middle Region Rabbit Polyclonal Antibody Catalog # AI10980
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 DHX38 antibody - middle region Rabbit Polyclonal Antibody Catalog # AI10980 Specification DHX38 antibody - middle region - Product Information Application WB Primary Accession Q92620 Other Accession NM_014003, NP_054722 Reactivity Human, Mouse, Rat, Rabbit, Zebrafish, Pig, Horse, Bovine, Dog Predicted Human, Rat, WB Suggested Anti-DHX38 Antibody Rabbit, Zebrafish, Titration: 1.0 μg/ml Pig, Chicken Positive Control: OVCAR-3 Whole Cell Host Rabbit Clonality Polyclonal Calculated MW 140kDa KDa DHX38 antibody - middle region - Additional Information Gene ID 9785 Alias Symbol DDX38, KIAA0224, PRP16, PRPF16 Other Names Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16, 3.6.4.13, ATP-dependent RNA helicase DHX38, DEAH box protein 38, DHX38, DDX38, KIAA0224, PRP16 Format Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose. Reconstitution & Storage Add 50 ul of distilled water. Final anti-DHX38 antibody concentration is 1 mg/ml in PBS buffer with 2% sucrose. For longer periods of storage, store at 20°C. Avoid repeat freeze-thaw cycles. Precautions Page 1/2 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 DHX38 antibody - middle region is for research use only and not for use in diagnostic or therapeutic procedures. DHX38 antibody - middle region - Protein Information Name DHX38 Synonyms DDX38, KIAA0224, PRP16 Function Probable ATP-binding RNA helicase (Probable). Involved in pre-mRNA splicing as component of the spliceosome (PubMed:<a href="http://www.uniprot.org/c itations/29301961" target="_blank">29301961</a>, PubMed:<a href="http://www.uniprot.org/ci tations/9524131" target="_blank">9524131</a>).
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CRNKL1 Is a Highly Selective Regulator of Intron-Retaining HIV-1 and Cellular Mrnas
bioRxiv preprint doi: https://doi.org/10.1101/2020.02.04.934927; this version posted February 11, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 CRNKL1 is a highly selective regulator of intron-retaining HIV-1 and cellular mRNAs 2 3 4 Han Xiao1, Emanuel Wyler2#, Miha Milek2#, Bastian Grewe3, Philipp Kirchner4, Arif Ekici4, Ana Beatriz 5 Oliveira Villela Silva1, Doris Jungnickl1, Markus Landthaler2,5, Armin Ensser1, and Klaus Überla1* 6 7 1 Institute of Clinical and Molecular Virology, University Hospital Erlangen, Friedrich-Alexander 8 Universität Erlangen-Nürnberg, Erlangen, Germany 9 2 Berlin Institute for Medical Systems Biology, Max-Delbrück-Center for Molecular Medicine in the 10 Helmholtz Association, Robert-Rössle-Strasse 10, 13125, Berlin, Germany 11 3 Department of Molecular and Medical Virology, Ruhr-University, Bochum, Germany 12 4 Institute of Human Genetics, University Hospital Erlangen, Friedrich-Alexander Universität Erlangen- 13 Nürnberg, Erlangen, Germany 14 5 IRI Life Sciences, Institute für Biologie, Humboldt Universität zu Berlin, Philippstraße 13, 10115, Berlin, 15 Germany 16 # these two authors contributed equally 17 18 19 *Corresponding author: 20 Prof. Dr. Klaus Überla 21 Institute of Clinical and Molecular Virology, University Hospital Erlangen 22 Friedrich-Alexander Universität Erlangen-Nürnberg 23 Schlossgarten 4, 91054 Erlangen 24 Germany 25 Tel: (+49) 9131-8523563 26 e-mail: [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.02.04.934927; this version posted February 11, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder.
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Essential Genes and Their Role in Autism Spectrum Disorder
University of Pennsylvania ScholarlyCommons Publicly Accessible Penn Dissertations 2017 Essential Genes And Their Role In Autism Spectrum Disorder Xiao Ji University of Pennsylvania, [email protected] Follow this and additional works at: https://repository.upenn.edu/edissertations Part of the Bioinformatics Commons, and the Genetics Commons Recommended Citation Ji, Xiao, "Essential Genes And Their Role In Autism Spectrum Disorder" (2017). Publicly Accessible Penn Dissertations. 2369. https://repository.upenn.edu/edissertations/2369 This paper is posted at ScholarlyCommons. https://repository.upenn.edu/edissertations/2369 For more information, please contact [email protected]. Essential Genes And Their Role In Autism Spectrum Disorder Abstract Essential genes (EGs) play central roles in fundamental cellular processes and are required for the survival of an organism. EGs are enriched for human disease genes and are under strong purifying selection. This intolerance to deleterious mutations, commonly observed haploinsufficiency and the importance of EGs in pre- and postnatal development suggests a possible cumulative effect of deleterious variants in EGs on complex neurodevelopmental disorders. Autism spectrum disorder (ASD) is a heterogeneous, highly heritable neurodevelopmental syndrome characterized by impaired social interaction, communication and repetitive behavior. More and more genetic evidence points to a polygenic model of ASD and it is estimated that hundreds of genes contribute to ASD. The central question addressed in this dissertation is whether genes with a strong effect on survival and fitness (i.e. EGs) play a specific oler in ASD risk. I compiled a comprehensive catalog of 3,915 mammalian EGs by combining human orthologs of lethal genes in knockout mice and genes responsible for cell-based essentiality.
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Structural Basis for DEAH-Helicase Activation by G-Patch Proteins
Structural basis for DEAH-helicase activation by G-patch proteins Michael K. Studera, Lazar Ivanovica, Marco E. Webera, Sabrina Martia, and Stefanie Jonasa,1 aInstitute of Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology (ETH) Zürich, 8093 Zürich, Switzerland Edited by Joseph D. Puglisi, Stanford University School of Medicine, Stanford, CA, and approved February 21, 2020 (received for review August 12, 2019) RNA helicases of the DEAH/RHA family are involved in many essential RNA bases are stacked in the RNA binding channel between a long cellular processes, such as splicing or ribosome biogenesis, where β-hairpin in RecA2 (β14 to β15 in hsDHX15/scPrp43; SI Appendix, they remodel large RNA–protein complexes to facilitate transitions Fig. S1) and a conserved loop in RecA1 (termed “Hook-turn”). to the next intermediate. DEAH helicases couple adenosine tri- This means that during progression into the open state, the phosphate (ATP) hydrolysis to conformational changes of their β-hairpin and two other RNA-binding patches in RecA2 (termed catalytic core. This movement results in translocation along RNA, “Hook-loop” and “motif V”; SI Appendix, Fig. S1) have to shift 1 which is held in place by auxiliary C-terminal domains. The activity nucleotide (nt) toward the 5′ end of the RNA. Thus, when the of DEAH proteins is strongly enhanced by the large and diverse RecA domains close back up, at the start of the next hydrolysis class of G-patch activators. Despite their central roles in RNA me- cycle, the RNA is pushed by 1 nt through the RNA channel.
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Exploring the Relationship Between Gut Microbiota and Major Depressive Disorders
E3S Web of Conferences 271, 03055 (2021) https://doi.org/10.1051/e3sconf/202127103055 ICEPE 2021 Exploring the Relationship between Gut Microbiota and Major Depressive Disorders Catherine Tian1 1Shanghai American School, Shanghai, China Abstract. Major Depressive Disorder (MDD) is a psychiatric disorder accompanied with a high rate of suicide, morbidity and mortality. With the symptom of an increasing or decreasing appetite, there is a possibility that MDD may have certain connections with gut microbiota, the colonies of microbes which reside in the human digestive system. In recent years, more and more studies started to demonstrate the links between MDD and gut microbiota from animal disease models and human metabolism studies. However, this relationship is still largely understudied, but it is very innovative since functional dissection of this relationship would furnish a new train of thought for more effective treatment of MDD. In this study, by using multiple genetic analytic tools including Allen Brain Atlas, genetic function analytical tools, and MicrobiomeAnalyst, I explored the genes that shows both expression in the brain and the digestive system to affirm that there is a connection between gut microbiota and the MDD. My approach finally identified 7 MDD genes likely to be associated with gut microbiota, implicating 3 molecular pathways: (1) Wnt Signaling, (2) citric acid cycle in the aerobic respiration, and (3) extracellular exosome signaling. These findings may shed light on new directions to understand the mechanism of MDD, potentially facilitating the development of probiotics for better psychiatric disorder treatment. 1 Introduction 1.1 Major Depressive Disorder Major Depressive Disorder (MDD) is a mood disorder that will affect the mood, behavior and other physical parts.
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The Alter Retina: Alternative Splicing of Retinal Genes in Health and Disease
International Journal of Molecular Sciences Review The Alter Retina: Alternative Splicing of Retinal Genes in Health and Disease Izarbe Aísa-Marín 1,2 , Rocío García-Arroyo 1,3 , Serena Mirra 1,2 and Gemma Marfany 1,2,3,* 1 Departament of Genetics, Microbiology and Statistics, Avda. Diagonal 643, Universitat de Barcelona, 08028 Barcelona, Spain; [email protected] (I.A.-M.); [email protected] (R.G.-A.); [email protected] (S.M.) 2 Centro de Investigación Biomédica en Red Enfermedades Raras (CIBERER), Instituto de Salud Carlos III (ISCIII), Universitat de Barcelona, 08028 Barcelona, Spain 3 Institute of Biomedicine (IBUB, IBUB-IRSJD), Universitat de Barcelona, 08028 Barcelona, Spain * Correspondence: [email protected] Abstract: Alternative splicing of mRNA is an essential mechanism to regulate and increase the diversity of the transcriptome and proteome. Alternative splicing frequently occurs in a tissue- or time-specific manner, contributing to differential gene expression between cell types during development. Neural tissues present extremely complex splicing programs and display the highest number of alternative splicing events. As an extension of the central nervous system, the retina constitutes an excellent system to illustrate the high diversity of neural transcripts. The retina expresses retinal specific splicing factors and produces a large number of alternative transcripts, including exclusive tissue-specific exons, which require an exquisite regulation. In fact, a current challenge in the genetic diagnosis of inherited retinal diseases stems from the lack of information regarding alternative splicing of retinal genes, as a considerable percentage of mutations alter splicing Citation: Aísa-Marín, I.; or the relative production of alternative transcripts. Modulation of alternative splicing in the retina García-Arroyo, R.; Mirra, S.; Marfany, is also instrumental in the design of novel therapeutic approaches for retinal dystrophies, since it G.
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Human Proteins That Interact with RNA/DNA Hybrids
Downloaded from genome.cshlp.org on October 4, 2021 - Published by Cold Spring Harbor Laboratory Press Resource Human proteins that interact with RNA/DNA hybrids Isabel X. Wang,1,2 Christopher Grunseich,3 Jennifer Fox,1,2 Joshua Burdick,1,2 Zhengwei Zhu,2,4 Niema Ravazian,1 Markus Hafner,5 and Vivian G. Cheung1,2,4 1Howard Hughes Medical Institute, Chevy Chase, Maryland 20815, USA; 2Life Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109, USA; 3Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, NIH, Bethesda, Maryland 20892, USA; 4Department of Pediatrics, University of Michigan, Ann Arbor, Michigan 48109, USA; 5Laboratory of Muscle Stem Cells and Gene Regulation, National Institute of Arthritis and Musculoskeletal and Skin Diseases, Bethesda, Maryland 20892, USA RNA/DNA hybrids form when RNA hybridizes with its template DNA generating a three-stranded structure known as the R-loop. Knowledge of how they form and resolve, as well as their functional roles, is limited. Here, by pull-down assays followed by mass spectrometry, we identified 803 proteins that bind to RNA/DNA hybrids. Because these proteins were identified using in vitro assays, we confirmed that they bind to R-loops in vivo. They include proteins that are involved in a variety of functions, including most steps of RNA processing. The proteins are enriched for K homology (KH) and helicase domains. Among them, more than 300 proteins preferred binding to hybrids than double-stranded DNA. These proteins serve as starting points for mechanistic studies to elucidate what RNA/DNA hybrids regulate and how they are regulated.
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A Study of Alterations in DNA Epigenetic Modifications (5Mc and 5Hmc) and Gene Expression Influenced by Simulated Microgravity I
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Digital Repository @ Iowa State University Genome Informatics Facility Publications Genome Informatics Facility 1-28-2016 A Study of Alterations in DNA Epigenetic Modifications (5mC and 5hmC) and Gene Expression Influenced by Simulated Microgravity in Human Lymphoblastoid Cells Basudev Chowdhury Purdue University Arun S. Seetharam Iowa State University, [email protected] Zhiping Wang Indiana University School of Medicine Yunlong Liu Indiana University School of Medicine Amy C. Lossie Purdue University See next page for additional authors Follow this and additional works at: https://lib.dr.iastate.edu/genomeinformatics_pubs Part of the Bioinformatics Commons, Genetics Commons, and the Genomics Commons Recommended Citation Chowdhury, Basudev; Seetharam, Arun S.; Wang, Zhiping; Liu, Yunlong; Lossie, Amy C.; Thimmapuram, Jyothi; and Irudayaraj, Joseph, "A Study of Alterations in DNA Epigenetic Modifications (5mC and 5hmC) and Gene Expression Influenced by Simulated Microgravity in Human Lymphoblastoid Cells" (2016). Genome Informatics Facility Publications. 4. https://lib.dr.iastate.edu/genomeinformatics_pubs/4 This Article is brought to you for free and open access by the Genome Informatics Facility at Iowa State University Digital Repository. It has been accepted for inclusion in Genome Informatics Facility Publications by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. A Study of Alterations in DNA Epigenetic Modifications (5mC and 5hmC) and Gene Expression Influenced by Simulated Microgravity in Human Lymphoblastoid Cells Abstract Cells alter their gene expression in response to exposure to various environmental changes. Epigenetic mechanisms such as DNA methylation are believed to regulate the alterations in gene expression patterns.
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Variation in Protein Coding Genes Identifies Information Flow
bioRxiv preprint doi: https://doi.org/10.1101/679456; this version posted June 21, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Animal complexity and information flow 1 1 2 3 4 5 Variation in protein coding genes identifies information flow as a contributor to 6 animal complexity 7 8 Jack Dean, Daniela Lopes Cardoso and Colin Sharpe* 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 Institute of Biological and Biomedical Sciences 25 School of Biological Science 26 University of Portsmouth, 27 Portsmouth, UK 28 PO16 7YH 29 30 * Author for correspondence 31 [email protected] 32 33 Orcid numbers: 34 DLC: 0000-0003-2683-1745 35 CS: 0000-0002-5022-0840 36 37 38 39 40 41 42 43 44 45 46 47 48 49 Abstract bioRxiv preprint doi: https://doi.org/10.1101/679456; this version posted June 21, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Animal complexity and information flow 2 1 Across the metazoans there is a trend towards greater organismal complexity. How 2 complexity is generated, however, is uncertain. Since C.elegans and humans have 3 approximately the same number of genes, the explanation will depend on how genes are 4 used, rather than their absolute number.
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Figure S1. Gene Ontology Classification of Abeliophyllum Distichum Leaves Extract-Induced Degs
Figure S1. Gene ontology classification of Abeliophyllum distichum leaves extract-induced DEGs. The results are summarized in three main categories: Biological process, Cellular component and Molecular function. Figure S2. KEGG pathway enrichment analysis using Abeliophyllum distichum leaves extract-DEGs (A). Venn diagram analysis of DEGs involved in PI3K/Akt signaling pathway and Rap1 signaling pathway (B). Figure S3. The expression (A) and protein levels (B) of Akt3 in AL-treated SK-MEL2 cells. Values with different superscripted letters are significantly different (p < 0.05). Table S1. Abeliophyllum distichum leaves extract-induced DEGs. log2 Fold Gene name Gene description Change A2ML1 alpha-2-macroglobulin-like protein 1 isoform 2 [Homo sapiens] 3.45 A4GALT lactosylceramide 4-alpha-galactosyltransferase [Homo sapiens] −1.64 ABCB4 phosphatidylcholine translocator ABCB4 isoform A [Homo sapiens] −1.43 ABCB5 ATP-binding cassette sub-family B member 5 isoform 1 [Homo sapiens] −2.99 ABHD17C alpha/beta hydrolase domain-containing protein 17C [Homo sapiens] −1.62 ABLIM2 actin-binding LIM protein 2 isoform 1 [Homo sapiens] −2.53 ABTB2 ankyrin repeat and BTB/POZ domain-containing protein 2 [Homo sapiens] −1.48 ACACA acetyl-CoA carboxylase 1 isoform 1 [Homo sapiens] −1.76 ACACB acetyl-CoA carboxylase 2 precursor [Homo sapiens] −2.03 ACSM1 acyl-coenzyme A synthetase ACSM1, mitochondrial [Homo sapiens] −3.05 disintegrin and metalloproteinase domain-containing protein 19 preproprotein [Homo ADAM19 −1.65 sapiens] disintegrin and metalloproteinase
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Biology of the Mrna Splicing Machinery and Its Dysregulation in Cancer Providing Therapeutic Opportunities
International Journal of Molecular Sciences Review Biology of the mRNA Splicing Machinery and Its Dysregulation in Cancer Providing Therapeutic Opportunities Maxime Blijlevens †, Jing Li † and Victor W. van Beusechem * Medical Oncology, Amsterdam UMC, Cancer Center Amsterdam, Vrije Universiteit Amsterdam, de Boelelaan 1117, 1081 HV Amsterdam, The Netherlands; [email protected] (M.B.); [email protected] (J.L.) * Correspondence: [email protected]; Tel.: +31-2044-421-62 † Shared ﬁrst author. Abstract: Dysregulation of messenger RNA (mRNA) processing—in particular mRNA splicing—is a hallmark of cancer. Compared to normal cells, cancer cells frequently present aberrant mRNA splicing, which promotes cancer progression and treatment resistance. This hallmark provides opportunities for developing new targeted cancer treatments. Splicing of precursor mRNA into mature mRNA is executed by a dynamic complex of proteins and small RNAs called the spliceosome. Spliceosomes are part of the supraspliceosome, a macromolecular structure where all co-transcriptional mRNA processing activities in the cell nucleus are coordinated. Here we review the biology of the mRNA splicing machinery in the context of other mRNA processing activities in the supraspliceosome and present current knowledge of its dysregulation in lung cancer. In addition, we review investigations to discover therapeutic targets in the spliceosome and give an overview of inhibitors and modulators of the mRNA splicing process identiﬁed so far. Together, this provides insight into the value of targeting the spliceosome as a possible new treatment for lung cancer. Citation: Blijlevens, M.; Li, J.; van Beusechem, V.W. Biology of the Keywords: alternative splicing; splicing dysregulation; splicing factors; NSCLC mRNA Splicing Machinery and Its Dysregulation in Cancer Providing Therapeutic Opportunities.
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Mouse Dhx38 Knockout Project (CRISPR/Cas9)
https://www.alphaknockout.com Mouse Dhx38 Knockout Project (CRISPR/Cas9) Objective: To create a Dhx38 knockout Mouse model (C57BL/6J) by CRISPR/Cas-mediated genome engineering. Strategy summary: The Dhx38 gene (NCBI Reference Sequence: NM_178380 ; Ensembl: ENSMUSG00000037993 ) is located on Mouse chromosome 8. 27 exons are identified, with the ATG start codon in exon 2 and the TGA stop codon in exon 27 (Transcript: ENSMUST00000042601). Exon 2~19 will be selected as target site. Cas9 and gRNA will be co-injected into fertilized eggs for KO Mouse production. The pups will be genotyped by PCR followed by sequencing analysis. Note: Exon 2 starts from the coding region. Exon 2~19 covers 70.66% of the coding region. The size of effective KO region: ~8636 bp. The KO region does not have any other known gene. Page 1 of 8 https://www.alphaknockout.com Overview of the Targeting Strategy Wildtype allele 5' gRNA region gRNA region 3' 17 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 18 19 27 Legends Exon of mouse Dhx38 Knockout region Page 2 of 8 https://www.alphaknockout.com Overview of the Dot Plot (up) Window size: 15 bp Forward Reverse Complement Sequence 12 Note: The 2000 bp section upstream of Exon 2 is aligned with itself to determine if there are tandem repeats. Tandem repeats are found in the dot plot matrix. The gRNA site is selected outside of these tandem repeats. Overview of the Dot Plot (down) Window size: 15 bp Forward Reverse Complement Sequence 12 Note: The 594 bp section downstream of Exon 19 is aligned with itself to determine if there are tandem repeats.
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