PRPF19 Antibody Cat

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PRPF19 Antibody Cat. No.: 29-843 PRPF19 Antibody Antibody used in WB on mouse Antibody used in WB on Human Jurkat 2.5 ug/ml. brain at 1:1000 (Lane 1: 5ug mouse brain cytoplasm Lane 2: 5ug mouse brain nucleus ). Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Dog, Human, Mouse, Rat, Zebrafish Antibody produced in rabbits immunized with a synthetic peptide corresponding a region IMMUNOGEN: of human PRPF19. TESTED APPLICATIONS: ELISA, IHC, WB PRPF19 antibody can be used for detection of PRPF19 by ELISA at 1:1562500. PRPF19 APPLICATIONS: antibody can be used for detection of PRPF19 by western blot at 2.5 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 - 100,000. POSITIVE CONTROL: 1) Cat. No. 1205 - Jurkat Cell Lysate PREDICTED MOLECULAR 55 kDa WEIGHT: September 23, 2021 1 https://www.prosci-inc.com/prpf19-antibody-29-843.html Properties PURIFICATION: Antibody is purified by protein A chromatography method. CLONALITY: Polyclonal CONJUGATE: Unconjugated PHYSICAL STATE: Liquid Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% BUFFER: sucrose. CONCENTRATION: batch dependent For short periods of storage (days) store at 4˚C. For longer periods of storage, store STORAGE CONDITIONS: PRPF19 antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles. Additional Info OFFICIAL SYMBOL: PRPF19 ALTERNATE NAMES: PRPF19, NMP200, PRP19, PSO4, UBOX4, hPSO4, SNEV ACCESSION NO.: NP_055317 PROTEIN GI NO.: 7657381 GENE ID: 27339 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References PRPF19 plays a role in DNA double-strand break (DSB) repair and pre-mRNA splicing reaction. It binds double-stranded DNA in a sequence-nonspecific manner. PRPF19 acts as a structural component of the nuclear framework. It may also serve as a support for spliceosome binding and activity. It is essential for spliceosome assembly in a oligomerization-dependent manner and might also be important for spliceosome BACKGROUND: stability. It also may have E3 ubiquitin ligase activity. The PSO4 complex is required in the DNA interstrand cross-links (ICLs) repair process. Overexpression of PRPF19 might extend the cellular life span by increasing the resistance to stress or by improving the DNA repair capacity of the cells.In S. cerevisiae, Pso4 has pleiotropic functions in DNA recombination and in error-prone nonhomologous end-joining DNA repair. REFERENCES: 1) Voglauer, R., (2006) Exp. Cell Res. 312 (6), 746-759. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 23, 2021 2 https://www.prosci-inc.com/prpf19-antibody-29-843.html.

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Supplemental Material Table of Contents
Supplemental material Table of Contents Detailed Materials and Methods ......................................................................................................... 2 Perioperative period ........................................................................................................................... 2 Ethical aspects ................................................................................................................................... 4 Evaluation of heart failure ................................................................................................................. 4 Sample preparation for ANP mRNA expression .................................................................................. 5 Sample preparation for validative qRT-PCR (Postn, Myh7, Gpx3, Tgm2) ............................................ 6 Tissue fibrosis .................................................................................................................................... 7 Ventricular remodeling and histological tissue preservation ................................................................ 8 Evaluation of the histological preservation of cardiac tissue ................................................................ 9 Sample preparation and quantitative label-free proteomics analyses .................................................. 10 Statistical methods ........................................................................................................................... 12 References ........................................................................................................................................
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Datasheet: VPA00331KT Product Details
Datasheet: VPA00331KT Description: PRPF19 ANTIBODY WITH CONTROL LYSATE Specificity: PRPF19 Format: Purified Product Type: PrecisionAb™ Polyclonal Isotype: Polyclonal IgG Quantity: 2 Westerns Product Details Applications This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit www.bio-rad-antibodies.com/protocols. Yes No Not Determined Suggested Dilution Western Blotting 1/1000 PrecisionAb antibodies have been extensively validated for the western blot application. The antibody has been validated at the suggested dilution. Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Further optimization may be required dependant on sample type. Target Species Human Species Cross Reacts with: Mouse, Rat Reactivity N.B. Antibody reactivity and working conditions may vary between species. Product Form Purified IgG - liquid Preparation 20μl Rabbit polyclonal antibody purified by affinity chromatography Buffer Solution Phosphate buffered saline Preservative 0.09% Sodium Azide (NaN ) Stabilisers 3 Immunogen KLH-conjugated synthetic peptide corresponding to aa 4-33 of human PRPF19 External Database Links UniProt: Q9UMS4 Related reagents Entrez Gene: 27339 PRPF19 Related reagents Synonyms NMP200, PRP19, SNEV Page 1 of 3 Specificity Rabbit anti Human PRPF19 antibody recognizes PRPF19, also known as PRP19/PSO4 homolog, PRP19/PSO4 pre-mRNA processing factor 19 homolog, nuclear matrix protein 200, nuclear matrix protein NMP200 related to splicing factor PRP19, psoralen 4 and senescence evasion factor. The PRPF19 gene is the human homolog of yeast Pso4, a gene essential for cell survival and DNA repair (Beck et al.
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A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
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Nuclear PTEN Safeguards Pre-Mrna Splicing to Link Golgi Apparatus for Its Tumor Suppressive Role
ARTICLE DOI: 10.1038/s41467-018-04760-1 OPEN Nuclear PTEN safeguards pre-mRNA splicing to link Golgi apparatus for its tumor suppressive role Shao-Ming Shen1, Yan Ji2, Cheng Zhang1, Shuang-Shu Dong2, Shuo Yang1, Zhong Xiong1, Meng-Kai Ge1, Yun Yu1, Li Xia1, Meng Guo1, Jin-Ke Cheng3, Jun-Ling Liu1,3, Jian-Xiu Yu1,3 & Guo-Qiang Chen1 Dysregulation of pre-mRNA alternative splicing (AS) is closely associated with cancers. However, the relationships between the AS and classic oncogenes/tumor suppressors are 1234567890():,; largely unknown. Here we show that the deletion of tumor suppressor PTEN alters pre-mRNA splicing in a phosphatase-independent manner, and identify 262 PTEN-regulated AS events in 293T cells by RNA sequencing, which are associated with significant worse outcome of cancer patients. Based on these findings, we report that nuclear PTEN interacts with the splicing machinery, spliceosome, to regulate its assembly and pre-mRNA splicing. We also identify a new exon 2b in GOLGA2 transcript and the exon exclusion contributes to PTEN knockdown-induced tumorigenesis by promoting dramatic Golgi extension and secretion, and PTEN depletion significantly sensitizes cancer cells to secretion inhibitors brefeldin A and golgicide A. Our results suggest that Golgi secretion inhibitors alone or in combination with PI3K/Akt kinase inhibitors may be therapeutically useful for PTEN-deficient cancers. 1 Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine (SJTU-SM), Shanghai 200025, China. 2 Institute of Health Sciences, Shanghai Institutes for Biological Sciences of Chinese Academy of Sciences and SJTU-SM, Shanghai 200025, China.
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Human Prefoldin Modulates Co-Transcriptional Pre-Mrna Splicing
bioRxiv preprint doi: https://doi.org/10.1101/2020.06.14.150466; this version posted July 22, 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. BIOLOGICAL SCIENCES: Biochemistry Human prefoldin modulates co-transcriptional pre-mRNA splicing Payán-Bravo L 1,2, Peñate X 1,2 *, Cases I 3, Pareja-Sánchez Y 1, Fontalva S 1,2, Odriozola Y 1,2, Lara E 1, Jimeno-González S 2,5, Suñé C 4, Reyes JC 5, Chávez S 1,2. 1 Instituto de Biomedicina de Sevilla, Universidad de Sevilla-CSIC-Hospital Universitario V. del Rocío, Seville, Spain. 2 Departamento de Genética, Facultad de Biología, Universidad de Sevilla, Seville, Spain. 3 Centro Andaluz de Biología del Desarrollo, CSIC-Universidad Pablo de Olavide, Seville, Spain. 4 Department of Molecular Biology, Institute of Parasitology and Biomedicine "López Neyra" IPBLN-CSIC, PTS, Granada, Spain. 5 Andalusian Center of Molecular Biology and Regenerative Medicine-CABIMER, Junta de Andalucia-University of Pablo de Olavide-University of Seville-CSIC, Seville, Spain. Correspondence: Sebastián Chávez, IBiS, campus HUVR, Avda. Manuel Siurot s/n, Sevilla, 41013, Spain. Phone: +34-955923127: e-mail: [email protected]. * Co- corresponding; [email protected]. bioRxiv preprint doi: https://doi.org/10.1101/2020.06.14.150466; this version posted July 22, 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. Abstract Prefoldin is a heterohexameric complex conserved from archaea to humans that plays a cochaperone role during the cotranslational folding of actin and tubulin monomers.
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Haruki Iino (Autor) Functional analysis of the nuclear basket and protein Tpr https://cuvillier.de/de/shop/publications/7587 Copyright: Cuvillier Verlag, Inhaberin Annette Jentzsch-Cuvillier, Nonnenstieg 8, 37075 Göttingen, Germany Telefon: +49 (0)551 54724-0, E-Mail: [email protected], Website: https://cuvillier.de 2. Abstract A large coiled-coil protein, Tpr (Translocated promoter region) is located at the nuclear side of the nuclear pore complex (NPC), and plays an important role in the architecture of the nuclear basket (NB). Although its contribution to the NB structure has been characterized, little is known about the function of Tpr. In this work, we investigated whether and how Tpr contributes to the surveillance of mRNA export, especially, to the quality control (QC) of certain un-spliced mRNAs. To answer these questions, we established a series of different reporter cell lines, allowing us to monitor the occurrence of un-spliced and spliced reporter transcripts. In the analysis of most of these reporter cell lines, the depletion of Tpr did not cause any obvious leakage of un-spliced reporter mRNAs. However, when the coding sequence of the HIV (Human immunodeficiency virus) Gag protein was used as a readout, the cytoplasmic levels of the un-spliced HIV-gag mRNAs were highly enhanced in the absence of Tpr. Such phenotype was only observed when a viral RNA export enhancer element, the CTE (the constitutive transport element), that recruits the general mRNA export receptor, NXF1/TAP, was part of the HIV-gag reporter gene. Intriguingly, a slight reduction in the cellular Tpr levels already caused the breakdown of a retention mechanism that normally keeps these HIV-gag transcripts in the nucleus.
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An Optimized Streptavidin-Binding RNA Aptamer for Purification Of
Published online 23 October 2013 Nucleic Acids Research, 2014, Vol. 42, No. 2 e13 doi:10.1093/nar/gkt956 An optimized streptavidin-binding RNA aptamer for purification of ribonucleoprotein complexes identifies novel ARE-binding proteins Kathrin Leppek1,2,3 and Georg Stoecklin1,2,3,* 1Helmholtz Junior Research Group Posttranscriptional Control of Gene Expression, German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120 Heidelberg, Germany, 2Zentrum fu¨ r Molekulare Biologie der Universita¨ t Heidelberg (ZMBH), Im Neuenheimer Feld 282, 69120 Heidelberg, Germany and 3DKFZ-ZMBH Downloaded from https://academic.oup.com/nar/article-abstract/42/2/e13/1030103 by guest on 11 March 2019 Alliance Received June 19, 2013; Revised September 6, 2013; Accepted September 27, 2013 ABSTRACT degradation (1,2). The fate of any given mRNA is essen- tially determined by the messenger ribonucleoprotein Determining the composition of messenger (mRNP) complex, i.e. the ensemble of proteins and regu- ribonucleoprotein (mRNP) particles is essential for latory RNAs an mRNA interacts with. Although decades a comprehensive understanding of the complex of research have uncovered speciﬁc functions of numerous mechanisms underlying mRNA regulation, but is RNA-binding proteins (RNA-BPs), surprisingly little is technically challenging. Here we present an RNA- known about the composition, heterogeneity and based method to identify RNP components using a dynamics of whole mRNPs. modified streptavidin (SA)-binding RNA aptamer There are essentially two strategies to explore the termed S1m. By optimizing the RNA aptamer S1 in content of mRNPs. On one hand, protein-based structure and repeat conformation, we improved its approaches rely on the puriﬁcation of a particular RNA- affinity for SA and found a 4-fold repeat of S1m BP by immunoprecipitation together with its associated mRNAs, whose identity can then be determined by (4ÂS1m) to be more efficient than the established cDNA cloning, microarray analysis (RIP-Chip) or deep MS2 and PP7 systems from bacteriophages.
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Functional Splicing Network Reveals Extensive Regulatory Potential of the Core Spliceosomal Machinery Panagiotis Papasaikas,1,2,4 J. Ramo´ n Tejedor,1,2,4 Luisa Vigevani,1,2 and Juan Valca´ rcel1,2,3,* 1Centre de Regulacio´ Geno` mica, Dr. Aiguader 88, 08003 Barcelona, Spain 2Universitat Pompeu Fabra, Dr. Aiguader 88, 08003 Barcelona, Spain 3Institucio´ Catalana de Recerca i Estudis Avanc¸ ats, Passeig Lluis Companys 23, 08010 Barcelona, Spain 4Co-first authors SUMMARY quent binding of preassembled U4/5/6 tri-snRNP forms complex B, which after a series of conformational changes forms com- Pre-mRNA splicing relies on the poorly plexes Bact and C, concomitant with the activation of the two understood dynamic interplay between >150 catalytic steps that generate splicing intermediates and prod- protein compo- nents of the spliceosome. The ucts. Transition between spliceosomal subcomplexes involves steps at which splicing can be regulated remain profound dynamic changes in protein composition as well as largely unknown. We sys- tematically analyzed extensive rearrangements of base-pairing interactions between the effect of knocking down the components of snRNAs and between snRNAs and splice site sequences (Wahl the splicing machinery on alterna- tive splicing et al., 2009). RNA structures contributed by base-pairing interac- events relevant for cell proliferation and apoptosis tions between U2 and U6 snRNAs serve to coordinate metal ions and used this information to reconstruct a critical for splicing catalysis (Fica et al., 2013), implying that the network of functional interactions. The network spliceosome is an RNA enzyme whose catalytic center is only accurately captures known physical and established upon assembly of its individual components.
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7058–7069 Nucleic Acids Research, 2015, Vol. 43, No. 14 Published online 29 June 2015 doi: 10.1093/nar/gkv643 CTNNBL1 facilitates the association of CWC15 with CDC5L and is required to maintain the abundance of the Prp19 spliceosomal complex Febe van Maldegem1,*, Sarah Maslen1, Christopher M. Johnson1, Anita Chandra1, Karuna Ganesh2, Mark Skehel1 and Cristina Rada1,* 1MRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK and 2Department of Medicine and Cancer Biology & Genetics Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA Received November 18, 2014; Revised June 04, 2015; Accepted June 09, 2015 ABSTRACT CDC5L, PLRG1 and SPF27 (the product of the BCAS2 gene), and a sub-complex that includes CTNNBL1 and In order to catalyse the splicing of messenger RNA, CWC15, as well as the chaperone protein HSP7C (en- multiple proteins and RNA components associate coded by the HSPA8 gene) (2). As part of a bigger com- and dissociate in a dynamic highly choreographed plex of more than 30 associated proteins (3), the Prp19 process. The Prp19 complex is a conserved essential complex aids the progression of the core snRNP compo- part of the splicing machinery thought to facilitate the nents through several steps of catalysis and recycling and conformational changes the spliceosome undergoes is therefore essential for splicing (4). The core complex during catalysis. Dynamic protein interactions often has remarkable conservation of function, being essential involve highly disordered regions that are difﬁcult to in both Saccharomyces cerevisiae and Schizosaccharomyces study by structural methods. Using amine crosslink- pombe––known as the NineTeen Complex or NTC (5).
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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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ADAR-Deficiency Perturbs the Global Splicing Landscape in Mouse Tissues
Downloaded from genome.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press 1 ADAR-deficiency perturbs the global splicing 2 landscape in mouse tissues 3 Running Title: A-to-I RNA editing impacts pre-mRNA splicing 4 5 Authors: 1* 1* 1,2 6 Utkarsh Kapoor , Konstantin Licht , Fabian Amman , Tobias 3 1 3 1 7 Jakobi , David Martin , Christoph Dieterich and Michael F. Jantsch 8 9 10 1. Center of Anatomy & Cell Biology, 11 Department of Cell and Developmental Biology, 12 Medical University of Vienna 13 Schwarzspanierstrasse 17 14 A-1090 Vienna, Austria 15 16 2. Institute of Theoretical Biochemistry 17 University of Vienna 18 Währingerstrasse 17 19 A-1090 Vienna, Austria 20 21 3. Department of Internal Medicine III and Klaus Tschira Institute for 22 Computational Cardiology, 23 Section of Bioinformatics and Systems Cardiology, 24 Im Neuenheimer Feld 669, 25 University Hospital 26 D-96120 Heidelberg, Germany. 27 28 *) equal contribution 29 30 Correspondence to: 31 Michael F. Jantsch 32 Center for Anatomy and Cell Biology 33 Division of Cell- and Developmental Biology 34 Schwarzspanierstrasse 17 35 A-1090 Vienna, Austria 36 Email: [email protected] 37 Tel: +43-1-40160 37510 Downloaded from genome.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press 1 Abstract 2 Adenosine to inosine RNA-editing and pre-mRNA splicing largely occur co-transcriptionally 3 and influence each other. Here we use mice deficient in either one of the two editing 4 enzymes ADAR (ADAR1) or ADARB1 (ADAR2) to determine the transcriptome-wide impact of 5 RNA-editing on splicing across different tissues.
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