PRMT8 Antibody Cat

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PRMT8 Antibody Cat. No.: 56-275 PRMT8 Antibody Western blot analysis of PRMT8 using rabbit polyclonal PRMT8 Antibody using 293 cell lysates (2 Western blot analysis of PRMT8 Antibody in K562 cell line lysates (35ug/lane) ug/lane) either nontransfected (Lane 1) or transiently transfected with the PRMT8 gene (Lane 2). Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human HOMOLOGY: Predicted species reactivity based on immunogen sequence: Mouse This PRMT8 antibody is generated from rabbits immunized with a KLH conjugated IMMUNOGEN: synthetic peptide between 344-373 amino acids from the C-terminal region of human PRMT8. TESTED APPLICATIONS: WB October 1, 2021 1 https://www.prosci-inc.com/prmt8-antibody-56-275.html APPLICATIONS: For WB starting dilution is: 1:1000 PREDICTED MOLECULAR 45 kDa WEIGHT: Properties This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by PURIFICATION: dialysis CLONALITY: Polyclonal ISOTYPE: Rabbit Ig CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: Supplied in PBS with 0.09% (W/V) sodium azide. CONCENTRATION: batch dependent Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies STORAGE CONDITIONS: care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. Additional Info OFFICIAL SYMBOL: PRMT8 Protein arginine N-methyltransferase 8, 211-, Heterogeneous nuclear ribonucleoprotein ALTERNATE NAMES: methyltransferase-like protein 4, PRMT8, HRMT1L3, HRMT1L4 ACCESSION NO.: Q9NR22 PROTEIN GI NO.: 88983969 GENE ID: 56341 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References Protein arginine methylation plays a role in signal transduction, RNA processing, transcriptional regulation, and DNA repair. PRMT8, a protein arginine N- methyltransferase most closely related to PRMT1, methylates the guanidino nitrogens of BACKGROUND: arginyl residues in some proteins. This protein associates with the plasma membrane following myristoylation and exhibits a brain-specific expression pattern, making it unique within this family of enzymes. REFERENCES: 1) Lee,J., J. Biol. Chem. 280 (38), 32890-32896 (2005) October 1, 2021 2 https://www.prosci-inc.com/prmt8-antibody-56-275.html ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. October 1, 2021 3 https://www.prosci-inc.com/prmt8-antibody-56-275.html.

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PRMT8 Antibody (C-Term) Purified Rabbit Polyclonal Antibody (Pab) Catalog # Ap1219b
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 PRMT8 Antibody (C-term) Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP1219b Specification PRMT8 Antibody (C-term) - Product Information Application WB,E Primary Accession Q9NR22 Other Accession Q6PAK3 Reactivity Human Predicted Mouse Host Rabbit Clonality Polyclonal Isotype Rabbit Ig Calculated MW 45291 Antigen Region 344-373 PRMT8 Antibody (C-term) - Additional Information Gene ID 56341 Western blot analysis of lysates from human Other Names brain, mouse brain tissue lysate (from left to Protein arginine N-methyltransferase 8, right), using PRMT8 Antibody (C-term)(Cat. 211-, Heterogeneous nuclear #AP1219b). AP1219b was diluted at 1:1000 ribonucleoprotein methyltransferase-like at each lane. A goat anti-rabbit IgG H&L(HRP) protein 4, PRMT8, HRMT1L3, HRMT1L4 at 1:10000 dilution was used as the Target/Specificity secondary antibody. Lysates at 35ug per This PRMT8 antibody is generated from lane. rabbits immunized with a KLH conjugated synthetic peptide between 344-373 amino acids from the C-terminal region of human PRMT8. Dilution WB~~1:1000 Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. Storage Western blot analysis of PRMT8 Antibody Maintain refrigerated at 2-8°C for up to 2 (C-term) (Cat.#AP1219b) in K562 cell line weeks. For long term storage store at -20°C lysates (35ug/lane). PRMT8 (arrow) was in small aliquots to prevent freeze-thaw detected using the purified Pab. cycles.
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NIH Public Access Author Manuscript ACS Chem Biol
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PRMT1 and PRMT8 Regulate Retinoic Acid Dependent Neuronal
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Datasheet A07980-1 Anti-PRMT8 Antibody
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Proquest Dissertations
mn u Ottawa L'Université canadienne Canada's university FACULTE DES ETUDES SUPERIEURES I=I FACULTY OF GRADUATE AND ETPOSTOCTORALES u Ottawa posdoctoral studies L'Université canadienne Canada's university Marie-Eve Pelletier AUTEUR DE LA THESE / AUTHOR OF THESIS M.Sc. (Cellular and Molecular Medicine) GRADE /DEGREE Department of Cellular and Molecular Medicine FACULTE, ECOLE, DEPARTEMENT / FACULTY, SCHOOL, DEPARTMENT PRMT8: Characterization of a Novel Neuron-Specific Protein Arginine Methyltransferase TITRE DE LA THESE / TITLE OF THESIS Jocelyn Côté DIRECTEUR (DIRECTRICE) DE LA THESE / THESIS SUPERVISOR CO-DIRECTEUR (CO-DI RECTRICE) DE LATHESE /THESIS CO-SUPERVISOR Laura Trinkle Mulcahy Jean-François Couture Gary W. Slater "UeDoyendela Faculté des études supérieures et postdoctorales / Dean of the Faculty of Graduate and Postdoctoral Studies PRMT8: Characterization of a Novel Neuron-Specific Protein Arginine Methyltransferase This thesis is submitted as a partial fulfillment of the M.Sc. program in Cellular and Molecular Medicine Marie-Eve Pelletier January 5, 2010 Faculty of Medicine, University of Ottawa Ottawa, Ontario, Canada ©Marie-Eve Pelletier, Ottawa, Canada, 2010 Library and Archives Bibliothèque et ?F? Canada Archives Canada Published Heritage Direction du Branch Patrimoine de l'édition 395 Wellington Street 395, rue Wellington Ottawa ON K1A 0N4 OttawaONK1A0N4 Canada Canada Your file Votre référence ISBN: 978-0-494-65489-7 Our file Notre référence ISBN: 978-0-494-65489-7 NOTICE: AVIS: The author has granted a non- L'auteur a
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Epigenetic Regulators in Neuroblastoma: Brg1, a Future Therapeutic Target
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Identification and Characterization of Isoform-Selective Inhibitors
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Functional Characterization of the Ewing Sarcoma (EWS) Protein and Its Post-Translational Modifications
Zurich Open Repository and Archive University of Zurich Main Library Strickhofstrasse 39 CH-8057 Zurich www.zora.uzh.ch Year: 2007 Functional characterization of the Ewing sarcoma (EWS) protein and its post-translational modifications Pahlich, Steffen Posted at the Zurich Open Repository and Archive, University of Zurich ZORA URL: https://doi.org/10.5167/uzh-163670 Dissertation Published Version Originally published at: Pahlich, Steffen. Functional characterization of the Ewing sarcoma (EWS) protein and its post-translational modifications. 2007, University of Zurich, Faculty of Science. Functional Characterization of the Ewing Sarcoma (EWS) Protein and its Post-Translational Modifications Dissertation zur Erlangung der naturwissenschaftlichen Doktorwürde (Dr. sc. nat.) vorgelegt der Mathematisch-naturwissenschaftlichen Fakultät der Universität Zürich von Steffen Pahlich aus Deutschland Promotionskomitee Prof. Dr. Peter Sonderegger (Vorsitz) Prof. Dr. Heinz Gehring (Leitung der Dissertation) Zürich, 2007 Die vorliegende Arbeit wurde von der Mathematisch-naturwissenschaftlichen Fakultät der Universität Zürich im Sommersemester 2007 als Dissertation angenommen. Promotionskomitee: Prof. Dr. Peter Sonderegger (Vorsitz) Prof. Dr. Heinz Gehring (Leitung der Dissertation) The results of this work have been or will be published elsewhere: List of Publications Pahlich S, Bschir K, Chiavi C, Belyanskaya L, Gehring H. Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide. Proteins. 2005 Oct 1;61(1):164-75. Pahlich S, Zakaryan RP, Gehring H. Review: Protein arginine methylation: Cellular functions and methods of analysis. Biochim Biophys Acta – Proteins and Proteomics. 2006 Dec;1764(12):1890-903 Pahlich S, Zakaryan RP, Gehring H. Identification of proteins interacting with Protein Arginine Methyltransferase 8: The Ewing Sarcoma (EWS) Protein binds independent of its methylation state.
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