VARS Rabbit Pab

Leader in Biomolecular Solutions for Life Science VARS Rabbit pAb Catalog No.: A4182 1 Publications Basic Information Background Catalog No. Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate A4182 amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first Observed MW proteins that appeared in evolution. The protein encoded by this gene belongs to class-I 140kDa aminoacyl-tRNA synthetase family and is located in the class III region of the major histocompatibility complex. Calculated MW 33kDa/140kDa Category Primary antibody Applications WB, IHC, IF Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 7407 P26640 IHC 1:50 - 1:100 Immunogen 1:50 - 1:100 IF Recombinant fusion protein containing a sequence corresponding to amino acids 1-280 of human VARS (NP_006286.1). Synonyms VARS;G7A;VARS1;VARS2 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 VARS antibody (A4182) at 1:1000 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 Basic Kit (RM00020). Exposure time: 30s. Immunohistochemistry of paraffin- Immunohistochemistry of paraffin- Immunohistochemistry of paraffin- embedded rat brain using VARS antibody embedded human breast cancer using embedded mouse brain using VARS (A4182) at dilution of 1:100 (40x lens). VARS antibody (A4182) at dilution of 1:100 antibody (A4182) at dilution of 1:100 (40x (40x lens). lens). Immunofluorescence analysis of L929 cells using VARS Polyclonal Antibody (A4182) at dilution of 1:100 (40x lens). Blue: DAPI for nuclear staining. 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..

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Strains Used in Whole Organism Plasmodium Falciparum Vaccine Trials Differ in 2 Genome Structure, Sequence, and Immunogenic Potential 3 4 Authors: Kara A
bioRxiv preprint doi: https://doi.org/10.1101/684175; this version posted June 27, 2019. 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 Title: Strains used in whole organism Plasmodium falciparum vaccine trials differ in 2 genome structure, sequence, and immunogenic potential 3 4 Authors: Kara A. Moser1‡, Elliott F. Drábek1, Ankit Dwivedi1, Jonathan Crabtree1, Emily 5 M. Stucke2, Antoine Dara2, Zalak Shah2, Matthew Adams2, Tao Li3, Priscila T. 6 Rodrigues4, Sergey Koren5, Adam M. Phillippy5, Amed Ouattara2, Kirsten E. Lyke2, Lisa 7 Sadzewicz1, Luke J. Tallon1, Michele D. Spring6, Krisada Jongsakul6, Chanthap Lon6, 8 David L. Saunders6¶, Marcelo U. Ferreira4, Myaing M. Nyunt2§, Miriam K. Laufer2, Mark 9 A. Travassos2, Robert W. Sauerwein7, Shannon Takala-Harrison2, Claire M. Fraser1, B. 10 Kim Lee Sim3, Stephen L. Hoffman3, Christopher V. Plowe2§, Joana C. Silva1,8 11 12 Corresponding author: Joana C. Silva, [email protected] 13 Affiliations: 14 1 Institute for Genome Sciences, University of Maryland School of Medicine, Baltimore, 15 MD, 21201 16 2 Center for Vaccine Development and Global Health, University of Maryland School of 17 Medicine, Baltimore, MD, 21201 18 3 Sanaria, Inc. Rockville, Maryland, 20850 19 4 Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, 20 São Paulo, Brazil 21 5 Genome Informatics Section, Computational and Statistical Genomics Branch, 22 National Human
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Aminoacyl-Trna Synthetase Deficiencies in Search of Common Themes
© American College of Medical Genetics and Genomics ARTICLE Aminoacyl-tRNA synthetase deficiencies in search of common themes Sabine A. Fuchs, MD, PhD1, Imre F. Schene, MD1, Gautam Kok, BSc1, Jurriaan M. Jansen, MSc1, Peter G. J. Nikkels, MD, PhD2, Koen L. I. van Gassen, PhD3, Suzanne W. J. Terheggen-Lagro, MD, PhD4, Saskia N. van der Crabben, MD, PhD5, Sanne E. Hoeks, MD6, Laetitia E. M. Niers, MD, PhD7, Nicole I. Wolf, MD, PhD8, Maaike C. de Vries, MD9, David A. Koolen, MD, PhD10, Roderick H. J. Houwen, MD, PhD11, Margot F. Mulder, MD, PhD12 and Peter M. van Hasselt, MD, PhD1 Purpose: Pathogenic variations in genes encoding aminoacyl- with unreported compound heterozygous pathogenic variations in tRNA synthetases (ARSs) are increasingly associated with human IARS, LARS, KARS, and QARS extended the common phenotype disease. Clinical features of autosomal recessive ARS deficiencies with lung disease, hypoalbuminemia, anemia, and renal tubulo- appear very diverse and without apparent logic. We searched for pathy. common clinical patterns to improve disease recognition, insight Conclusion: We propose a common clinical phenotype for recessive into pathophysiology, and clinical care. ARS deficiencies, resulting from insufficient aminoacylation activity Methods: Symptoms were analyzed in all patients with recessive to meet translational demand in specific organs or periods of life. ARS deficiencies reported in literature, supplemented with Assuming residual ARS activity, adequate protein/amino acid supply unreported patients evaluated in our hospital. seems essential instead of the traditional replacement of protein by Results: In literature, we identified 107 patients with AARS, glucose in patients with metabolic diseases. DARS, GARS, HARS, IARS, KARS, LARS, MARS, RARS, SARS, VARS, YARS, and QARS deficiencies.
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Anti-VARS (Aa 994-1102) Polyclonal Antibody (DPAB-DC3179) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Anti-VARS (aa 994-1102) polyclonal antibody (DPAB-DC3179) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Antigen Description Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. The protein encoded by this gene belongs to class-I aminoacyl-tRNA synthetase family and is located in the class III region of the major histocompatibility complex. Immunogen VARS (NP_006286, 994 a.a. ~ 1102 a.a) partial recombinant protein with GST tag. The sequence is AVRLSNQGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVG LRLLSPFMPFVTEELFQRLPRRMPQAPPSLCVTPYPEPSECSWKDP Source/Host Mouse Species Reactivity Human Conjugate Unconjugated Applications WB (Recombinant protein), ELISA, Size 50 μl Buffer 50 % glycerol Preservative None Storage Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. GENE INFORMATION Gene Name VARS valyl-tRNA synthetase [ Homo sapiens (human) ] Official Symbol VARS Synonyms VARS; valyl-tRNA synthetase; G7A; VARS1; VARS2; valine--tRNA ligase; valRS; protein G7a; valyl-tRNA synthetase 2; valine tRNA ligase 1, cytoplasmic; 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Entrez Gene ID 7407 Protein Refseq NP_006286 UniProt ID A0A024RCN6 Chromosome Location 6p21.3 Pathway Aminoacyl-tRNA biosynthesis; Cytosolic tRNA aminoacylation; tRNA Aminoacylation; Function ATP binding; aminoacyl-tRNA editing activity; valine-tRNA ligase activity; 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 2 © Creative Diagnostics All Rights Reserved.
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Cancer Biol Med 2020. doi: 10.20892/j.issn.2095-3941.2019.0164 ORIGINAL ARTICLE Downregulation of SNRPG induces cell cycle arrest and sensitizes human glioblastoma cells to temozolomide by targeting Myc through a p53-dependent signaling pathway Yulong Lan1,2*, Jiacheng Lou2*, Jiliang Hu1, Zhikuan Yu1, Wen Lyu1, Bo Zhang1,2 1Department of Neurosurgery, Shenzhen People’s Hospital, Second Clinical Medical College of Jinan University, The First Affiliated Hospital of Southern University of Science and Technology, Shenzhen 518020, China;2 Department of Neurosurgery, The Second Affiliated Hospital of Dalian Medical University, Dalian 116023, China ABSTRACT Objective: Temozolomide (TMZ) is commonly used for glioblastoma multiforme (GBM) chemotherapy. However, drug resistance limits its therapeutic effect in GBM treatment. RNA-binding proteins (RBPs) have vital roles in posttranscriptional events. While disturbance of RBP-RNA network activity is potentially associated with cancer development, the precise mechanisms are not fully known. The SNRPG gene, encoding small nuclear ribonucleoprotein polypeptide G, was recently found to be related to cancer incidence, but its exact function has yet to be elucidated. Methods: SNRPG knockdown was achieved via short hairpin RNAs. Gene expression profiling and Western blot analyses were used to identify potential glioma cell growth signaling pathways affected by SNRPG. Xenograft tumors were examined to determine the carcinogenic effects of SNRPG on glioma tissues. Results: The SNRPG-mediated inhibitory effect on glioma cells might be due to the targeted prevention of Myc and p53. In addition, the effects of SNRPG loss on p53 levels and cell cycle progression were found to be Myc-dependent. Furthermore, SNRPG was increased in TMZ-resistant GBM cells, and downregulation of SNRPG potentially sensitized resistant cells to TMZ, suggesting that SNRPG deficiency decreases the chemoresistance of GBM cells to TMZ via the p53 signaling pathway.
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bioRxiv preprint doi: https://doi.org/10.1101/260224; this version posted February 5, 2018. 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. New insights on human essential genes based on integrated multi- omics analysis Hebing Chen1,2, Zhuo Zhang1,2, Shuai Jiang 1,2, Ruijiang Li1, Wanying Li1, Hao Li1,* and Xiaochen Bo1,* 1Beijing Institute of Radiation Medicine, Beijing 100850, China. 2 Co-first author *Correspondence: [email protected]; [email protected] Abstract Essential genes are those whose functions govern critical processes that sustain life in the organism. Comprehensive understanding of human essential genes could enable breakthroughs in biology and medicine. Recently, there has been a rapid proliferation of technologies for identifying and investigating the functions of human essential genes. Here, according to gene essentiality, we present a global analysis for comprehensively and systematically elucidating the genetic and regulatory characteristics of human essential genes. We explain why these genes are essential from the genomic, epigenomic, and proteomic perspectives, and we discuss their evolutionary and embryonic developmental properties. Importantly, we find that essential human genes can be used as markers to guide cancer treatment. We have developed an interactive web server, the Human Essential Genes Interactive Analysis Platform (HEGIAP) (http://sysomics.com/HEGIAP/), which integrates abundant analytical tools to give a global, multidimensional interpretation of gene essentiality. bioRxiv preprint doi: https://doi.org/10.1101/260224; this version posted February 5, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder.
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University of Vermont ScholarWorks @ UVM Graduate College Dissertations and Theses Dissertations and Theses 2018 Secondary Functions And Novel Inhibitors Of Aminoacyl-Trna Synthetases Patrick Wiencek University of Vermont Follow this and additional works at: https://scholarworks.uvm.edu/graddis Part of the Biochemistry Commons Recommended Citation Wiencek, Patrick, "Secondary Functions And Novel Inhibitors Of Aminoacyl-Trna Synthetases" (2018). Graduate College Dissertations and Theses. 941. https://scholarworks.uvm.edu/graddis/941 This Thesis is brought to you for free and open access by the Dissertations and Theses at ScholarWorks @ UVM. It has been accepted for inclusion in Graduate College Dissertations and Theses by an authorized administrator of ScholarWorks @ UVM. For more information, please contact [email protected]. SECONDARY FUNCTIONS AND NOVEL INHIBITORS OF AMINOACYL-TRNA SYNTHETASES A Thesis Presented by Patrick Wiencek to The Faculty of the Graduate College of The University of Vermont In Partial Fulfillment of the Requirements for the Degree of Master of Science Specializing in Biochemistry October, 2018 Defense Date: June 29, 2018 Thesis Examination Committee: Christopher S. Francklyn, Ph.D., Advisor Karen M. Lounsbury, Ph.D., Chairperson Robert J. Hondal, Ph.D. Jay Silveira, Ph.D. Cynthia J. Forehand, Ph.D., Dean of the Graduate College ABSTRACT The aminoacyl-tRNA synthetases are a family of enzymes involved in the process of translation, more specifically, ligating amino acids to their cognate tRNA molecules. Recent evidence suggests that aminoacyl-tRNA synthetases are capable of aminoacylating proteins, some of which are involved in the autophagy pathway. Here, we test the conditions under which E. coli and human threonyl-tRNA synthetases, as well as hisidyl-tRNA synthetase aminoacylate themselves.
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Supporting Information
Supporting Information Poulogiannis et al. 10.1073/pnas.1009941107 SI Materials and Methods Loss of Heterozygosity (LOH) Analysis of PARK2. Seven microsatellite Bioinformatic Analysis of Genome and Transcriptome Data. The markers (D6S1550, D6S253, D6S305, D6S955, D6S980, D6S1599, aCGH package in R was used to identify significant DNA copy and D6S396) were amplified for LOH analysis within the PARK2 number (DCN) changes in our collection of 100 sporadic CRCs locus using primers that were previously described (8). (1) (Gene Expression Omnibus, accession no. GSE12520). The MSP of the PARK2 Promoter. CpG sites within the PARK2 promoter aCGH analysis of cell lines and liver metastases was derived region were detected using the Methprimer software (http://www. from published data (2, 3). Chromosome 6 tiling-path array- urogene.org/methprimer/index.html). Methylation-specificand CGH was used to identify the smallest and most frequently al- control primers were designed using the Primo MSP software tered regions of DNA copy number change on chromosome 6. (http://www.changbioscience.com/primo/primom.html); bisulfite An integrative approach was used to correlate expression pro- modification of genomic DNA was performed as described pre- files with genomic copy number data from a SNP array from the viously (9). All tumor DNA samples from primary CRC tumors same tumors (n = 48) (4) (GSE16125), using Pearson’s corre- (n = 100) and CRC lines (n = 5), as well as those from the leukemia lation coefficient analysis to identify the relationships between cell lines KG-1a (acute myeloid leukemia, AML), U937 (acute DNA copy number changes and gene expression of those genes lymphoblastic leukemia, ALL), and Raji (Burkitt lymphoma, BL) SssI located within the small frequently altered regions of DCN were screened as part of this analysis.
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Package 'Canprot'
Package ‘canprot’ October 19, 2020 Date 2020-10-19 Version 1.1.0 Title Compositional Analysis of Differentially Expressed Proteins in Cancer Maintainer Jeffrey Dick <[email protected]> Depends R (>= 3.1.0) Imports xtable, MASS, rmarkdown Suggests CHNOSZ (>= 1.3.0), knitr, testthat Description Compositional analysis of differentially expressed proteins in cancer and cell culture proteomics experiments. The data include lists of up- and down-regulated proteins in different cancer types (breast, colorectal, liver, lung, pancreatic, prostate) and laboratory conditions (hypoxia, hyperosmotic stress, high glucose, 3D cell culture, and proteins secreted in hypoxia), together with amino acid compositions computed for protein sequences obtained from UniProt. Functions are provided to calculate compositional metrics including protein length, carbon oxidation state, and stoichiometric hydration state. In addition, phylostrata (evolutionary ages) of protein-coding genes are compiled using data from Liebeskind et al. (2016) <doi:10.1093/gbe/evw113> or Trigos et al. (2017) <doi:10.1073/pnas.1617743114>. The vignettes contain plots of compositional differences, phylostrata for human proteins, and references for all datasets. Encoding UTF-8 License GPL (>= 2) BuildResaveData no VignetteBuilder knitr URL https://github.com/jedick/canprot NeedsCompilation no Author Jeffrey Dick [aut, cre] (<https://orcid.org/0000-0002-0687-5890>), Ben Bolker [ctb] (<https://orcid.org/0000-0002-2127-0443>) Repository CRAN Date/Publication 2020-10-19 04:30:02 UTC 1 2 canprot-package R topics documented: canprot-package . .2 check_IDs . .3 cleanup . .4 CLES ............................................6 diffplot . .8 get_comptab . 10 human . 12 metrics . 13 mkvig . 16 pdat_ . 17 protcomp . 19 PS.............................................. 20 qdist . 21 xsummary . 22 Index 24 canprot-package Compositional Analysis of Differentially Expressed Proteins Description canprot is a package for analysis of the chemical compositions of proteins from their amino acid compositions.
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New Var Reconstruction Algorithm Exposes High Var Sequence Diversity in a Single Geographic Location in Mali Antoine Dara1†, Elliott F
Dara et al. Genome Medicine (2017) 9:30 DOI 10.1186/s13073-017-0422-4 RESEARCH Open Access New var reconstruction algorithm exposes high var sequence diversity in a single geographic location in Mali Antoine Dara1†, Elliott F. Drábek2†, Mark A. Travassos1, Kara A. Moser2, Arthur L. Delcher2,QiSu2, Timothy Hostelley2, Drissa Coulibaly3, Modibo Daou3ˆ, Ahmadou Dembele3, Issa Diarra3, Abdoulaye K. Kone3, Bourema Kouriba3, Matthew B. Laurens1, Amadou Niangaly3, Karim Traore3, Youssouf Tolo3, Claire M. Fraser2,4,5, Mahamadou A. Thera3, Abdoulaye A. Djimde3, Ogobara K. Doumbo3, Christopher V. Plowe1 and Joana C. Silva2,4* Abstract Background: Encoded by the var gene family, highly variable Plasmodium falciparum erythrocyte membrane protein-1 (PfEMP1) proteins mediate tissue-specific cytoadherence of infected erythrocytes, resulting in immune evasion and severe malaria disease. Sequencing and assembling the 40–60 var gene complement for individual infections has been notoriously difficult, impeding molecular epidemiological studies and the assessment of particular var elements as subunit vaccine candidates. Methods: We developed and validated a novel algorithm, Exon-Targeted Hybrid Assembly (ETHA), to perform targeted assembly of var gene sequences, based on a combination of Pacific Biosciences and Illumina data. Results: Using ETHA, we characterized the repertoire of var genes in 12 samples from uncomplicated malaria infections in children from a single Malian village and showed them to be as genetically diverse as vars from isolates from around the globe. The gene var2csa, a member of the var family associated with placental malaria pathogenesis, was present in each genome, as were vars previously associated with severe malaria. Conclusion: ETHA, a tool to discover novel var sequences from clinical samples, will aid the understanding of malaria pathogenesis and inform the design of malaria vaccines based on PfEMP1.
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Drosophila Models of Pathogenic Copy-Number Variant Genes Show Global and Non-Neuronal Defects During Development
bioRxiv preprint doi: https://doi.org/10.1101/855338; this version posted November 26, 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 4.0 International license. 1 Drosophila models of pathogenic copy-number variant genes show global and 2 non-neuronal defects during development 3 4 Tanzeen Yusuff1,4, Matthew Jensen1,4, Sneha Yennawar1,4, Lucilla Pizzo1, Siddharth 5 Karthikeyan1, Dagny J. Gould1, Avik Sarker1, Yurika Matsui1,2, Janani Iyer1, Zhi-Chun Lai1,2, 6 and Santhosh Girirajan1,3* 7 8 1. Department of Biochemistry and Molecular Biology, Pennsylvania State University, 9 University Park, PA 16802 10 2. Department of Biology, Pennsylvania State University, University Park, PA 16802 11 3. Department of Anthropology, Pennsylvania State University, University Park, PA 16802 12 13 4 contributed equally to work 14 15 16 *Correspondence: 17 Santhosh Girirajan, MBBS, PhD 18 205A Life Sciences Building 19 Pennsylvania State University 20 University Park, PA 16802 21 E-mail: [email protected] 22 Phone: 814-865-0674 23 1 bioRxiv preprint doi: https://doi.org/10.1101/855338; this version posted November 26, 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 4.0 International license. 24 ABSTRACT 25 While rare pathogenic CNVs are associated with both neuronal and non-neuronal phenotypes, 26 functional studies evaluating these regions have focused on the molecular basis of neuronal 27 defects.
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