IPO7 Antibody (F54822)

IPO7 Antibody / Importin 7 (F54822) Catalog No. Formulation Size F54822-0.4ML In 1X PBS, pH 7.4, with 0.09% sodium azide 0.4 ml F54822-0.08ML In 1X PBS, pH 7.4, with 0.09% sodium azide 0.08 ml Bulk quote request Availability 1-3 business days Species Reactivity Human, Mouse Format Purified Clonality Polyclonal (rabbit origin) Isotype Rabbit Ig Purity Antigen affinity purified UniProt O95373 Localization Cytoplasmic, nuclear Applications Immunohistochemistry (FFPE) : 1:50-1:100 Western blot : 1:500-1:1000 Limitations This IPO7 antibody is available for research use only. Western blot testing of human HeLa cell lysate with IPO7 antibody. Predicted molecular weight ~120 kDa. Western blot testing of human NCI-H460 cell lysate with IPO7 antibody. Predicted molecular weight ~120 kDa. Western blot testing of mouse NIH 3T3 cell lysate with IPO7 antibody. Predicted molecular weight ~120 kDa. IHC testing of FFPE human cervix tissue with IPO7 antibody. HIER: steam section in pH6 citrate buffer for 20 min and allow to cool prior to staining. Description The importin-alpha/beta complex and the GTPase Ran mediate nuclear import of proteins with a classical nuclear localization signal. The protein encoded by this gene is a member of a class of approximately 20 potential Ran targets that share a sequence motif related to the Ran-binding site of importin-beta. Similar to importin-beta, this protein prevents the activation of Ran's GTPase by RanGAP1 and inhibits nucleotide exchange on RanGTP, and also binds directly to nuclear pore complexes where it competes for binding sites with importin-beta and transportin. This protein has a Ran-dependent transport cycle and it can cross the nuclear envelope rapidly and in both directions. At least four importin beta-like transport receptors, namely importin beta itself, transportin, RanBP5 and RanBP7, directly bind and import ribosomal proteins. Application Notes The stated application concentrations are suggested starting points. Titration of the IPO7 antibody may be required due to differences in protocols and secondary/substrate sensitivity. Immunogen A portion of amino acids 142-169 from the human protein was used as the immunogen for the IPO7 antibody. Storage Aliquot the IPO7 antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles. Ordering: Phone:858.663.9055 | Fax:1.267.821.0800 | Email:[email protected] Copyright © NSJ Bioreagents. All rights reserved.

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1 Supporting Information for a Microrna Network Regulates
Supporting Information for A microRNA Network Regulates Expression and Biosynthesis of CFTR and CFTR-ΔF508 Shyam Ramachandrana,b, Philip H. Karpc, Peng Jiangc, Lynda S. Ostedgaardc, Amy E. Walza, John T. Fishere, Shaf Keshavjeeh, Kim A. Lennoxi, Ashley M. Jacobii, Scott D. Rosei, Mark A. Behlkei, Michael J. Welshb,c,d,g, Yi Xingb,c,f, Paul B. McCray Jr.a,b,c Author Affiliations: Department of Pediatricsa, Interdisciplinary Program in Geneticsb, Departments of Internal Medicinec, Molecular Physiology and Biophysicsd, Anatomy and Cell Biologye, Biomedical Engineeringf, Howard Hughes Medical Instituteg, Carver College of Medicine, University of Iowa, Iowa City, IA-52242 Division of Thoracic Surgeryh, Toronto General Hospital, University Health Network, University of Toronto, Toronto, Canada-M5G 2C4 Integrated DNA Technologiesi, Coralville, IA-52241 To whom correspondence should be addressed: Email: [email protected] (M.J.W.); yi- [email protected] (Y.X.); Email: [email protected] (P.B.M.) This PDF file includes: Materials and Methods References Fig. S1. miR-138 regulates SIN3A in a dose-dependent and site-specific manner. Fig. S2. miR-138 regulates endogenous SIN3A protein expression. Fig. S3. miR-138 regulates endogenous CFTR protein expression in Calu-3 cells. Fig. S4. miR-138 regulates endogenous CFTR protein expression in primary human airway epithelia. Fig. S5. miR-138 regulates CFTR expression in HeLa cells. Fig. S6. miR-138 regulates CFTR expression in HEK293T cells. Fig. S7. HeLa cells exhibit CFTR channel activity. Fig. S8. miR-138 improves CFTR processing. Fig. S9. miR-138 improves CFTR-ΔF508 processing. Fig. S10. SIN3A inhibition yields partial rescue of Cl- transport in CF epithelia.
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Supplementary Materials
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Anti-IPO7 Mouse Mab
Anti-IPO7 Mouse mAb Catalog # PTM-5910 General Information Images Host species Mouse WB Clonality Recombinant monoclonal Blocking buffer: 5% NFDM/TBST Clone number JMMR-1765 Primary ab dilution: 1:1000 Primary ab incubation condition: room Synonym RANBP7 temperature 2h Immunogen UniProt MW (kDa) Applications Secondary ab: Goat Anti-Mouse IgG H&L species (HRP) Human O95373 120 WB, IHC-P Lysate: HeLa, K562, N2a, Rat brain Protein loading quantity: 20 μg Product Usage Information Exposure time: 60 s Predicted MW: 120 kDa Application Dilution Recommended species Observed MW: 120 kDa WB 1:500-1:1000 Human, Mouse, Rat IHC-P IHC-P 1:50-1:100 Human Tissue: Human breast cancer Section type: Formalin fixed & Paraffin - Properties embedded section Storage Store at -20°C. Avoid freeze / thaw cycles. Retrieval method: High temperature and high pressure Stability Stable for 12 months from date of receipt / reconstitution Retrieval buffer: Tris/EDTA buffer, pH 9.0 Primary ab dilution: 1:100 Constituents PBS, Glycerol, BSA Primary ab incubation condition: 1 hour at Purity Protein G purified room temperature Secondary ab: Anti-Rabbit and Mouse Isotype IgG1/Kappa Polymer HRP (Ready to use) Counter stain: Hematoxylin (Blue) Target Information Comment: Color brown is the positive signal for PTM-5910 Function Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter- Research Use like protein in association with the importin-beta subunit For research use only, not for use in diagnostic procedures. KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran- dependent mechanism.
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bioRxiv preprint doi: https://doi.org/10.1101/2021.07.30.454526; this version posted August 4, 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 4.0 International license. A Master Autoantigen-ome Links Alternative Splicing, Female Predilection, and COVID-19 to Autoimmune Diseases Julia Y. Wang1*, Michael W. Roehrl1, Victor B. Roehrl1, and Michael H. Roehrl2* 1 Curandis, New York, USA 2 Department of Pathology, Memorial Sloan Kettering Cancer Center, New York, USA * Correspondence: [email protected] or [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.07.30.454526; this version posted August 4, 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 4.0 International license. Abstract Chronic and debilitating autoimmune sequelae pose a grave concern for the post-COVID-19 pandemic era. Based on our discovery that the glycosaminoglycan dermatan sulfate (DS) displays peculiar affinity to apoptotic cells and autoantigens (autoAgs) and that DS-autoAg complexes cooperatively stimulate autoreactive B1 cell responses, we compiled a database of 751 candidate autoAgs from six human cell types. At least 657 of these have been found to be affected by SARS-CoV-2 infection based on currently available multi-omic COVID data, and at least 400 are confirmed targets of autoantibodies in a wide array of autoimmune diseases and cancer.
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888.267.4436 [email protected] www.origene.com Name:Goat Polyclonal Antibody against IPO7 Catalog: TA302815 Product Data Sheet - ANTIBODY Components: • Goat Polyclonal Antibody against IPO7 (TA302815) Amount: 100ug Immunogen: Peptide with sequence C-SSFNFGGPAPGMN, from the C Terminus of the protein sequence according to NP_006382.1. Host: Goat Isotype: Goat IgG Species Reactivity: Human Guaranteed WB Applications: Suggested ELISA: 1:32,000. WB 0.1-1µg/ml. Dilutions: Concentration: 0.5 mg/ml Buffer: Supplied at 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin. Purification: Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide. Supplied at 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin. Aliquot and store at -20°C. Minimize freezing and thawing. Storage Condition: Shipped at -20C. Upon delivery store at -20C. Dilute in PBS (pH7.3) if necessary. Stable for 12 months from date of receipt. Avoid repeated freeze-thaws. Target Target Name: Homo sapiens importin 7 (IPO7) Alternative Name: Imp7; RANBP7 Database Link: NP_006382 Function: The importin-alpha/beta complex and the GTPase Ran mediate nuclear import of proteins with a classical nuclear localization signal. The protein encoded by this gene is a member of a class of approximately 20 potential Ran targets that share a sequence motif related to the Ran-binding site of importin-beta. Similar to importin-beta, this protein prevents the activation of Ran's GTPase by RanGAP1 This product is to be used for laboratory only.
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Bioinformatics Tools for the Analysis of Gene-Phenotype Relationships Coupled with a Next Generation Chip-Sequencing Data Processing Pipeline
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A High-Throughput Approach to Uncover Novel Roles of APOBEC2, a Functional Orphan of the AID/APOBEC Family
Rockefeller University Digital Commons @ RU Student Theses and Dissertations 2018 A High-Throughput Approach to Uncover Novel Roles of APOBEC2, a Functional Orphan of the AID/APOBEC Family Linda Molla Follow this and additional works at: https://digitalcommons.rockefeller.edu/ student_theses_and_dissertations Part of the Life Sciences Commons A HIGH-THROUGHPUT APPROACH TO UNCOVER NOVEL ROLES OF APOBEC2, A FUNCTIONAL ORPHAN OF THE AID/APOBEC FAMILY A Thesis Presented to the Faculty of The Rockefeller University in Partial Fulfillment of the Requirements for the degree of Doctor of Philosophy by Linda Molla June 2018 © Copyright by Linda Molla 2018 A HIGH-THROUGHPUT APPROACH TO UNCOVER NOVEL ROLES OF APOBEC2, A FUNCTIONAL ORPHAN OF THE AID/APOBEC FAMILY Linda Molla, Ph.D. The Rockefeller University 2018 APOBEC2 is a member of the AID/APOBEC cytidine deaminase family of proteins. Unlike most of AID/APOBEC, however, APOBEC2’s function remains elusive. Previous research has implicated APOBEC2 in diverse organisms and cellular processes such as muscle biology (in Mus musculus), regeneration (in Danio rerio), and development (in Xenopus laevis). APOBEC2 has also been implicated in cancer. However the enzymatic activity, substrate or physiological target(s) of APOBEC2 are unknown. For this thesis, I have combined Next Generation Sequencing (NGS) techniques with state-of-the-art molecular biology to determine the physiological targets of APOBEC2. Using a cell culture muscle differentiation system, and RNA sequencing (RNA-Seq) by polyA capture, I demonstrated that unlike the AID/APOBEC family member APOBEC1, APOBEC2 is not an RNA editor. Using the same system combined with enhanced Reduced Representation Bisulfite Sequencing (eRRBS) analyses I showed that, unlike the AID/APOBEC family member AID, APOBEC2 does not act as a 5-methyl-C deaminase.
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Genomic Fossils As a Snapshot of the Human Transcriptome
Genomic fossils as a snapshot of the human transcriptome Ronen Shemesh*†, Amit Novik*†, Sarit Edelheit*, and Rotem Sorek*‡§ *Compugen Ltd., 72 Pinchas Rosen Street, Tel Aviv 69512, Israel; and ‡Department of Human Genetics and Molecular Medicine, Sackler Faculty of Medicine, Tel Aviv University, Ramat Aviv 69978, Israel Edited by Francisco J. Ayala, University of California, Irvine, CA, and approved December 5, 2005 (received for review October 26, 2005) Processed pseudogenes (PPGs) are cDNA sequences that were We propose a different source for full-length transcripts infor- generated through reverse transcription of mature, spliced mRNAs mation: processed pseudogenes (PPGs). PPGs (or retropseudo- and have subsequently been reinserted at a new genomic location. genes) are generated by reverse transcription of a spliced, mature These cDNA sequences are usually no longer transcribed and are mRNA, presumably by a virus or retrotransposon-encoded reverse considered ‘‘dead on arrival.’’ Here we show that PPGs can be used transcriptase (12–16). Their cDNA is then incorporated back into to generate a map of the transcriptome. By analyzing thousands of the genome (17). Most PPGs lack promoter and regulatory ele- human PPGs, we were able to discover hundreds of transcript ments, and are therefore not transcribed. Because pseudogenes are variants so far unidentified. An experimental verification of a usually nonfunctional, they can rapidly accumulate substitutions, subset of these variants by RT-PCR indicates that most of them are insertions, and deletions (18, 19). With the limitation of post still active in the human transcriptome. Furthermore, we demon- pseudogenization sequence changes, PPGs represent the mature strate that PPGs can enable the identification of ancient splice form of the spliced mRNA from which they originated (20, 21), and variants that were expressed ancestrally but are now extinct.
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Barr Virus Maintains Lymphomas Via Its Mirnas
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Proteomic-Based Evaluation of Nuclear Transport of NLS-Tagged Trastuzumab-Emtansine With
bioRxiv preprint doi: https://doi.org/10.1101/769588; this version posted September 14, 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 4.0 International license. Proteomic-based evaluation of nuclear transport of NLS-tagged trastuzumab-emtansine with enhanced cytotoxic potency Vincent Lacasse1, Simon Beaudoin1, Steve Jean2, and Jeffrey V. Leyton1,3,4 1Department of Nuclear Medicine and Radiobiology, Faculty of Medicine and Health Sciences, Centre Hospitalier Universitaire de Sherbrooke (CHUS), Université de Sherbrooke (UdeS), Sherbrooke, Québec, Canada 2Department of Anatomy and Cellular Biology, Faculty of Medicine and Health Sciences, CHUS, UdeS, Sherbrooke, Québec, Canada 3Sherbrooke Molecular Imaging Centre (CIMS), Centre de Recherche du CHUS, UdeS, Sherbrooke, Québec, Canada 4Sherbrooke Pharmacology Institute, Sherbrooke, Québec, Canada Running title: Novel proteomic tool for nuclear transport regulation Corresponding author: Jeffrey V. Leyton; [email protected]; 819-346-1110 x14907 Significant abbreviations: Antibody-drug conjugate (ADC); trastuzumab-emtansine (T-DM1); trastuzumab (Tmab); Human epidermal growth factor receptor 2 (HER2); Nuclear localization sequence (NLS); Cell accumulator (Accum); Nuclear transport receptor (NTR); SAINT score (STSc); GeneMANIA (GM); Gene Set Enrichment Analysis (GSEA) 1 bioRxiv preprint doi: https://doi.org/10.1101/769588; this version posted September 14, 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 4.0 International license.
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