UPF3A Antibody Cat

Total Page：16

File Type：pdf, Size：1020Kb

UPF3A Antibody Cat. No.: 16-307 UPF3A Antibody Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Mouse Recombinant fusion protein containing a sequence corresponding to amino acids 327-476 IMMUNOGEN: of human UPF3A (NP_075387.1). TESTED APPLICATIONS: WB APPLICATIONS: WB: ,1:500 - 1:2000 POSITIVE CONTROL: 1) Mouse testis PREDICTED MOLECULAR Observed: 55kDa WEIGHT: Properties PURIFICATION: Affinity purification CLONALITY: Polyclonal ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid September 23, 2021 1 https://www.prosci-inc.com/upf3a-antibody-16-307.html 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: UPF3A UPF3A, UPF3 regulator of nonsense transcripts homolog A, OTTHUMP00000018789, UPF3, ALTERNATE NAMES: RENT3A, HUPF3A, UPF3 regulator of nonsense transcripts homolog A (yeast), UPF3A GENE ID: 65110 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References This gene encodes a protein that is part of a post-splicing multiprotein complex involved in both mRNA nuclear export and mRNA surveillance. The encoded protein is one of two functional homologs to yeast Upf3p. mRNA surveillance detects exported mRNAs with truncated open reading frames and initiates nonsense-mediated mRNA decay (NMD). When translation ends upstream from the last exon-exon junction, this triggers NMD to BACKGROUND: degrade mRNAs containing premature stop codons. This protein binds to the mRNA and remains bound after nuclear export, acting as a nucleocytoplasmic shuttling protein. It forms with Y14 a complex that binds specifically 20 nt upstream of exon-exon junctions. This gene is located on the long arm of chromosome 13. Two splice variants encoding different isoforms have been found for this gene. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 23, 2021 2 https://www.prosci-inc.com/upf3a-antibody-16-307.html.

Copy Link

Recommended publications

A Upf3b-Mutant Mouse Model with Behavioral and Neurogenesis Defects
HHS Public Access Author manuscript Author ManuscriptAuthor Manuscript Author Mol Psychiatry Manuscript Author . Author Manuscript Author manuscript; available in PMC 2018 September 27. Published in final edited form as: Mol Psychiatry. 2018 August ; 23(8): 1773–1786. doi:10.1038/mp.2017.173. A Upf3b-mutant mouse model with behavioral and neurogenesis defects L Huang1, EY Shum1, SH Jones1, C-H Lou1, J Dumdie1, H Kim1, AJ Roberts2, LA Jolly3,4, J Espinoza1, DM Skarbrevik1, MH Phan1, H Cook-Andersen1, NR Swerdlow5, J Gecz3,4, and MF Wilkinson1,6 1Department of Reproductive Medicine, School of Medicine, University of California, San Diego, La Jolla, California, USA 2Department of Molecular and Cellular Neuroscience, The Scripps Research Institute, 10550 North Torrey Pines Road, MB6, La Jolla, CA 92037, USA 3School Adelaide Medical School and Robison Research Institute, University of Adelaide, Adelaide, SA 5005, Australia 4South Australian Health and Medical Research Institute, Adelaide, SA, 5005, Australia 5Department of Psychiatry, School of Medicine, University of California, San Diego, La Jolla, California, USA 6Institute of Genomic Medicine, University of California, San Diego, La Jolla, CA Abstract Nonsense-mediated RNA decay (NMD) is a highly conserved and selective RNA degradation pathway that acts on RNAs terminating their reading frames in specific contexts. NMD is regulated in a tissue-specific and developmentally controlled manner, raising the possibility that it influences developmental events. Indeed, loss or depletion of NMD factors have been shown to disrupt developmental events in organisms spanning the phylogenetic scale. In humans, mutations in the NMD factor gene, UPF3B, cause intellectual disability (ID) and are strongly associated with autism spectrum (ASD), attention deficit hyperactivity disorder (ADHD), and schizophrenia (SCZ).
[Show full text]
HHS Public Access Author Manuscript
HHS Public Access Author manuscript Author Manuscript Author ManuscriptGenet Epidemiol Author Manuscript. Author Author Manuscript manuscript; available in PMC 2016 June 01. Published in final edited form as: Genet Epidemiol. 2015 December ; 39(8): 664–677. doi:10.1002/gepi.21932. Multiple SNP-sets Analysis for Genome-wide Association Studies through Bayesian Latent Variable Selection Zhaohua Lu, Hongtu Zhu, Rebecca C Knickmeyer, Patrick F. Sullivan, Williams N. Stephanie, and Fei Zou for the Alzheimer’s Disease Neuroimaging Initiative* Departments of Biostatistics, Psychiatry, and Genetics and Biomedical Research Imaging Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA Abstract The power of genome-wide association studies (GWAS) for mapping complex traits with single SNP analysis may be undermined by modest SNP effect sizes, unobserved causal SNPs, correlation among adjacent SNPs, and SNP-SNP interactions. Alternative approaches for testing the association between a single SNP-set and individual phenotypes have been shown to be promising for improving the power of GWAS. We propose a Bayesian latent variable selection (BLVS) method to simultaneously model the joint association mapping between a large number of SNP-sets and complex traits. Compared to single SNP-set analysis, such joint association mapping not only accounts for the correlation among SNP-sets, but also is capable of detecting causal SNP- sets that are marginally uncorrelated with traits. The spike-slab prior assigned to the effects of SNP-sets can greatly reduce the dimension of effective SNP-sets, while speeding up computation. An efficient MCMC algorithm is developed. Simulations demonstrate that BLVS outperforms several competing variable selection methods in some important scenarios.
[Show full text]
UPF3A Rabbit Pab
Leader in Biomolecular Solutions for Life Science UPF3A Rabbit pAb Catalog No.: A15893 Basic Information Background Catalog No. This gene encodes a protein that is part of a post-splicing multiprotein complex involved A15893 in both mRNA nuclear export and mRNA surveillance. The encoded protein is one of two functional homologs to yeast Upf3p. mRNA surveillance detects exported mRNAs with Observed MW truncated open reading frames and initiates nonsense-mediated mRNA decay (NMD). 55kDa When translation ends upstream from the last exon-exon junction, this triggers NMD to degrade mRNAs containing premature stop codons. This protein binds to the mRNA and Calculated MW remains bound after nuclear export, acting as a nucleocytoplasmic shuttling protein. It 17kDa/51kDa/54kDa forms with Y14 a complex that binds specifically 20 nt upstream of exon-exon junctions. This gene is located on the long arm of chromosome 13. Two splice variants encoding Category different isoforms have been found for this gene. Primary antibody Applications WB,IF Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 65110 Q9H1J1 IF 1:50 - 1:200 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 327-476 of human UPF3A (NP_075387.1). Synonyms UPF3A;HUPF3A;RENT3A;UPF3 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 mouse testis, using UPF3A antibody (A15893) at 1:1000 dilution.
[Show full text]
UC Berkeley UC Berkeley Electronic Theses and Dissertations
UC Berkeley UC Berkeley Electronic Theses and Dissertations Title Networks of Splice Factor Regulation by Unproductive Splicing Coupled With NMD Permalink https://escholarship.org/uc/item/4md923q7 Author Desai, Anna Publication Date 2017 Peer reviewed|Thesis/dissertation eScholarship.org Powered by the California Digital Library University of California Networks of Splice Factor Regulation by Unproductive Splicing Coupled With NMD by Anna Maria Desai A dissertation submitted in partial satisfaction of the requirements for the degree of Doctor of Philosophy in Comparative Biochemistry in the Graduate Division of the University of California, Berkeley Committee in charge: Professor Steven E. Brenner, Chair Professor Donald Rio Professor Lin He Fall 2017 Abstract Networks of Splice Factor Regulation by Unproductive Splicing Coupled With NMD by Anna Maria Desai Doctor of Philosophy in Comparative Biochemistry University of California, Berkeley Professor Steven E. Brenner, Chair Virtually all multi-exon genes undergo alternative splicing (AS) to generate multiple protein isoforms. Alternative splicing is regulated by splicing factors, such as the serine/arginine rich (SR) protein family and the heterogeneous nuclear ribonucleoproteins (hnRNPs). Splicing factors are essential and highly conserved. It has been shown that splicing factors modulate alternative splicing of their own transcripts and of transcripts encoding other splicing factors. However, the extent of this alternative splicing regulation has not yet been determined. I hypothesize that the splicing factor network extends to many SR and hnRNP proteins, and is regulated by alternative splicing coupled to the nonsense mediated mRNA decay (NMD) surveillance pathway. The NMD pathway has a role in preventing accumulation of erroneous transcripts with dominant negative phenotypes.
[Show full text]
ALS Mutations of FUS Suppress Protein Translation and Disrupt the Regulation of Nonsense-Mediated Decay
ALS mutations of FUS suppress protein translation and disrupt the regulation of nonsense-mediated decay Marisa Kamelgarna, Jing Chenb, Lisha Kuangb, Huan Jina, Edward J. Kasarskisa,c, and Haining Zhua,b,d,1 aDepartment of Toxicology and Cancer Biology, College of Medicine, University of Kentucky, Lexington, KY 40536; bDepartment of Molecular and Cellular Biochemistry, College of Medicine, University of Kentucky, Lexington, KY 40536; cDepartment of Neurology, College of Medicine, University of Kentucky, Lexington, KY 40536; and dLexington VA Medical Center, Research and Development, Lexington, KY 40502 Edited by Gregory A. Petsko, Weill Cornell Medical College, New York, NY, and approved October 22, 2018 (received for review June 16, 2018) Amyotrophic lateral sclerosis (ALS) is an incurable neurodegener- This study started with testing the hypothesis that the identi- ative disease characterized by preferential motor neuron death. fication of proteins associated with mutant FUS-dependent cy- Approximately 15% of ALS cases are familial, and mutations in the toplasmic granules is likely to provide critical insights into the fused in sarcoma (FUS) gene contribute to a subset of familial ALS toxic mechanism of mutant FUS. We developed a protocol to cases. FUS is a multifunctional protein participating in many RNA capture the dynamic mutant FUS-positive granules (3, 4) by metabolism pathways. ALS-linked mutations cause a liquid–liquid membrane filtration and identified protein components by pro- phase separation of FUS protein in vitro, inducing the formation of teomic approaches. The bioinformatics analysis of proteins cytoplasmic granules and inclusions. However, it remains elusive identified in wild-type (WT) and mutant FUS granules revealed what other proteins are sequestered into the inclusions and how multiple RNA metabolism pathways, among which protein such a process leads to neuronal dysfunction and degeneration.
[Show full text]
Messenger-Rna-Binding Proteins and the Messages They Carry
REVIEWS MESSENGER-RNA-BINDING PROTEINS AND THE MESSAGES THEY CARRY Gideon Dreyfuss*, V.Narry Kim‡ and Naoyuki Kataoka* From sites of transcription in the nucleus to the outreaches of the cytoplasm, messenger RNAs are associated with RNA-binding proteins. These proteins influence pre-mRNA processing as well as the transport, localization, translation and stability of mRNAs. Recent discoveries have shown that one group of these proteins marks exon–exon junctions and has a role in mRNA export. These proteins communicate crucial information to the translation machinery for the surveillance of nonsense mutations and for mRNA localization and translation. PRE-mRNA To function properly, eukaryotic messenger RNAs must Recent discoveries showed that this mature mRNP The primary transcript of the contain, in addition to a string of codons, information contains proteins that it acquired strictly in the wake of genomic DNA, which contains that specifies their nuclear export, subcellular localiza- the splicing reaction. These proteins, which are exons, introns and other tion, translation and stability. An important theme to arranged in the form of a complex called the exon–exon sequences. emerge over the past few years is that much of this infor- junction complex (EJC), mark the position of SPLICING mation is provided by specific RNA-binding proteins. exon–exon junctions. EJC proteins have a role in the The removal of introns from the These proteins — collectively referred to as heteroge- nuclear export of mRNAs that are produced by splicing, pre-mRNA. neous nuclear ribonucleoproteins (hnRNP proteins) and several of the mRNP’s components persist in the or mRNA–protein complex proteins (mRNP pro- same position after export of the mRNP to the cyto- TERMINATION CODONS The stop signals for translation: teins) — are PRE-mRNA/mRNA-binding proteins that plasm.
[Show full text]
UPF3A and UPF3B Are Redundant and Modular Activators of Nonsense-Mediated Mrna Decay in Human Cells
bioRxiv preprint doi: https://doi.org/10.1101/2021.07.07.451444; this version posted July 13, 2021. 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 4.0 International license. 1 UPF3A and UPF3B are redundant and modular activators of 2 nonsense-mediated mRNA decay in human cells 3 4 Damaris Wallmeroth1,2, Volker Boehm1,2, Jan-Wilm Lackmann3, Janine Altmüller4,5, Christoph 5 Dieterich6,7, Niels H. Gehring1,2 6 7 1 Institute for Genetics, University of Cologne, 50674 Cologne, Germany 8 2 Center for Molecular Medicine Cologne (CMMC), University of Cologne, 50937 Cologne, 9 Germany 10 3 CECAD Research Center, University of Cologne, Joseph-Stelzmann-Str. 26, 50931 11 Cologne, Germany 12 4 Cologne Center for Genomics (CCG), University of Cologne, 50931 Cologne, Germany 13 5 Present address: Berlin Institute of Health at Charité – Universitätsmedizin Berlin, Core 14 Facility Genomics, Charitéplatz 1, 10117 Berlin, Germany and Max Delbrück Center for 15 Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany 16 6 Section of Bioinformatics and Systems Cardiology, Department of Internal Medicine III and 17 Klaus Tschira Institute for Integrative Computational Cardiology, Heidelberg University 18 Hospital, 69120 Heidelberg, Germany 19 7 DZHK (German Centre for Cardiovascular Research), Partner site Heidelberg/Mannheim, 20 69120 Heidelberg, Germany 21 22 *Correspondence: [email protected] (V.B.), [email protected] (N.H.G.) 23 24 Keywords 25 Nonsense-mediated mRNA decay, gene paralogs, mRNA turnover, UPF3 26 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.07.07.451444; this version posted July 13, 2021.
[Show full text]
RNA-Seq Analysis Reveals Localization-Associated Alternative Splicing Across 13 Cell Lines
G C A T T A C G G C A T genes Article RNA-Seq Analysis Reveals Localization-Associated Alternative Splicing across 13 Cell Lines Chao Zeng 1,2,* and Michiaki Hamada 1,2,3,4,* 1 AIST-Waseda University Computational Bio Big-Data Open Innovation Laboratory (CBBD-OIL), Tokyo 169-8555, Japan 2 Faculty of Science and Engineering, Waseda University, Tokyo 169-8555, Japan 3 Institute for Medical-oriented Structural Biology, Waseda University, Tokyo 162-8480, Japan 4 Graduate School of Medicine, Nippon Medical School, Tokyo 113-8602, Japan * Correspondence: [email protected] (C.Z.); [email protected] (M.H.) Received: 19 June 2020; Accepted: 17 July 2020; Published: 18 July 2020 Abstract: Alternative splicing, a ubiquitous phenomenon in eukaryotes, is a regulatory mechanism for the biological diversity of individual genes. Most studies have focused on the effects of alternative splicing for protein synthesis. However, the transcriptome-wide influence of alternative splicing on RNA subcellular localization has rarely been studied. By analyzing RNA-seq data obtained from subcellular fractions across 13 human cell lines, we identified 8720 switching genes between the cytoplasm and the nucleus. Consistent with previous reports, intron retention was observed to be enriched in the nuclear transcript variants. Interestingly, we found that short and structurally stable introns were positively correlated with nuclear localization. Motif analysis reveals that fourteen RNA-binding protein (RBPs) are prone to be preferentially bound with such introns. To our knowledge, this is the first transcriptome-wide study to analyze and evaluate the effect of alternative splicing on RNA subcellular localization.
[Show full text]
Harnessing Gene Discovery and Cellular Models to Understand the Genetics Underlying Neurodevelopmental Disorders Dr
February 2016 Harnessing Gene Discovery and Cellular Models to Understand the Genetics Underlying Neurodevelopmental Disorders Dr. Lachlan Jolly and his team at the University of Adelaide are applying functional genomic methods to identify the role of UPF3B and HCFC1 in intellectual disability. Introduction Living in Australia, Lachlan Jolly, PhD, takes advantage of everything the outdoors has to offer. When Dr. Jolly is not cycling, surfing, hiking, or playing basketball, he’s involved with equally expansive research programs to identify and study genes responsible for neurological disorders. To discover novel gene variants and describe their role in intellectual disability, Dr. Jolly integrates cell-based models with a multitude of genetic and functional genomic technologies. As an Australian Research Council Fellow at the University of Adelaide, Dr. Jolly has a leading role in the Neurogenetics Research Program. While other groups identify gene variants underlying neurodevelopmental disorders, Dr. Jolly directs research to discover Lachlan Jolly, Ph.D. is an Australian Research Council Fellow at the effects of genetic change. “We want to know what functional effect the University of Adelaide, where he focuses on understanding gene variants have in the development of the brain,” Dr. Jolly said. “We the genetic networks involved in brain development and function. know that they cause human disorders, but we want to know how they affect the way the cells behave and communicate.” The group genomics assays suggested involvement of a noncoding variant in the uses next-generation sequencing (NGS) to identify novel mutations, HCFC1 gene.3 and cell culture models of embryonic neural development to gain insight into novel genetic networks important for brain development Q: What can we learn about brain development from using different and function.
[Show full text]
Rules That Govern UPF1 Binding to Mrna 3′ Utrs
Rules that govern UPF1 binding to mRNA 3′ UTRs Tatsuaki Kurosaki and Lynne E. Maquat1 Department of Biochemistry and Biophysics, School of Medicine and Dentistry, and Center for RNA Biology, University of Rochester, Rochester, NY 14642 Edited by James L. Manley, Columbia University, New York, NY, and approved January 18, 2013 (received for review November 14, 2012) Nonsense-mediated mRNA decay (NMD), which degrades tran- recruits protein phosphatase 2A to return UPF1 to its steady-state scripts harboring a premature termination codon (PTC), depends hypophosphorylated status (19–22). on the helicase up-frameshift 1 (UPF1). However, mRNAs that are The importance of NMD in human pathologies is underscored not NMD targets also bind UPF1. What governs the timing, position, by the many genetically inherited diseases (23–25) that are due to and function of UPF1 binding to mRNAs remains unclear. We provide a PTC-containing mRNA. Read-through therapies have shown evidence that (i) multiple UPF1 molecules accumulate on the 3′-un- promise in generating full-length proteins without concomitantly translated region (3′ UTR) of PTC-containing mRNAs and to an ex- stabilizing PTC-bearing mRNAs (26, 27). However, a deeper tent that is greater per unit 3′ UTR length if the mRNA is an NMD understanding of how such transcripts are recognized and selec- target; (ii) UPF1 binding begins ≥35 nt downstream of the PTC; (iii) tively degraded by NMD is needed considering that UPF1 has enhanced UPF1 binding to the 3′ UTR of PTC-containing mRNA rel- been reported to bind to many mammalian mRNAs regardless of ative to its PTC-free counterpart depends on translation; and (iv)the PTC status (12, 28).
[Show full text]
And Post-Symptomatic Frontotemporal Dementia-Like Mice with TDP-43
Wu et al. Acta Neuropathologica Communications (2019) 7:50 https://doi.org/10.1186/s40478-019-0674-x RESEARCH Open Access Transcriptomopathies of pre- and post- symptomatic frontotemporal dementia-like mice with TDP-43 depletion in forebrain neurons Lien-Szu Wu1†, Wei-Cheng Cheng1†, Chia-Ying Chen2, Ming-Che Wu1, Yi-Chi Wang3, Yu-Hsiang Tseng2, Trees-Juen Chuang2* and C.-K. James Shen1* Abstract TAR DNA-binding protein (TDP-43) is a ubiquitously expressed nuclear protein, which participates in a number of cellular processes and has been identified as the major pathological factor in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Here we constructed a conditional TDP-43 mouse with depletion of TDP-43 in the mouse forebrain and find that the mice exhibit a whole spectrum of age-dependent frontotemporal dementia-like behaviour abnormalities including perturbation of social behaviour, development of dementia-like behaviour, changes of activities of daily living, and memory loss at a later stage of life. These variations are accompanied with inflammation, neurodegeneration, and abnormal synaptic plasticity of the mouse CA1 neurons. Importantly, analysis of the cortical RNA transcripts of the conditional knockout mice at the pre−/post-symptomatic stages and the corresponding wild type mice reveals age-dependent alterations in the expression levels and RNA processing patterns of a set of genes closely associated with inflammation, social behaviour, synaptic plasticity, and neuron survival. This study not only supports the scenario that loss-of-function of TDP-43 in mice may recapitulate key behaviour features of the FTLD diseases, but also provides a list of TDP-43 target genes/transcript isoforms useful for future therapeutic research.
[Show full text]
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.
[Show full text]