RBM8A 293T Cell Transient Overexpression Lysate(Denatured)

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RBM8A 293T Cell Transient Overexpression Lysate(Denatured) Catalog # : H00009939-T01 規格 : [ 100 uL ] List All Specification Application Image Transfected 293T Western Blot Cell Line: Plasmid: pCMV-RBM8A full-length Host: Human Theoretical MW 19.9 (kDa): Quality Control Transient overexpression cell lysate was tested with Anti-RBM8A Testing: antibody (H00009939-B01) by Western Blots. SDS-PAGE Gel RBM8A transfected lysate. Western Blot Lane 1: RBM8A transfected lysate ( 19.9 KDa) Lane 2: Non-transfected lysate. Storage Buffer: 1X Sample Buffer (50 mM Tris-HCl, 2% SDS, 10% glycerol, 300 mM 2- mercaptoethanol, 0.01% Bromophenol blue) Storage Store at -80°C. Aliquot to avoid repeated freezing and thawing. Instruction: MSDS: Download Applications Page 1 of 2 2016/5/22 Western Blot Gene Information Entrez GeneID: 9939 GeneBank NM_005105 Accession#: Protein NP_005096 Accession#: Gene Name: RBM8A Gene Alias: BOV-1A,BOV-1B,BOV-1C,MDS014,RBM8,RBM8B,Y14,ZNRP,ZRNP1 Gene RNA binding motif protein 8A Description: Omim ID: 605313 Gene Ontology: Hyperlink Gene Summary: This gene encodes a protein with a conserved RNA-binding motif. The protein is found predominantly in the nucleus, although it is also present in the cytoplasm. It is preferentially associated with mRNAs produced by splicing, including both nuclear mRNAs and newly exported cytoplasmic mRNAs. It is thought that the protein remains associated with spliced mRNAs as a tag to indicate where introns had been present, thus coupling pre- and post-mRNA splicing events. Previously, it was thought that two genes encode this protein, RBM8A and RBM8B; it is now thought that the RBM8B locus is a pseudogene. Two alternative start codons result in two forms of the protein, and this gene also uses multiple polyadenylation sites. [provided by RefSeq Other OTTHUMP00000015573,RNA binding motif protein 8B,binder of Designations: OVCA1-1,ribonucleoprotein RBM8 服務條款 | 隱私權政策 | 著作及商標 | 網站地圖 ©2016 亞諾法生技股份有限公司 Abnova Corporation. 版權所有. Page 2 of 2 2016/5/22.

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Thrombocytopenia-Absent Radius Syndrome
Thrombocytopenia-absent radius syndrome Description Thrombocytopenia-absent radius (TAR) syndrome is characterized by the absence of a bone called the radius in each forearm and a shortage (deficiency) of blood cells involved in clotting (platelets). This platelet deficiency (thrombocytopenia) usually appears during infancy and becomes less severe over time; in some cases the platelet levels become normal. Thrombocytopenia prevents normal blood clotting, resulting in easy bruising and frequent nosebleeds. Potentially life-threatening episodes of severe bleeding ( hemorrhages) may occur in the brain and other organs, especially during the first year of life. Hemorrhages can damage the brain and lead to intellectual disability. Affected children who survive this period and do not have damaging hemorrhages in the brain usually have a normal life expectancy and normal intellectual development. The severity of skeletal problems in TAR syndrome varies among affected individuals. The radius, which is the bone on the thumb side of the forearm, is almost always missing in both arms. The other bone in the forearm, which is called the ulna, is sometimes underdeveloped or absent in one or both arms. TAR syndrome is unusual among similar malformations in that affected individuals have thumbs, while people with other conditions involving an absent radius typically do not. However, there may be other abnormalities of the hands, such as webbed or fused fingers (syndactyly) or curved pinky fingers (fifth finger clinodactyly). Some people with TAR syndrome also have skeletal abnormalities affecting the upper arms, legs, or hip sockets. Other features that can occur in TAR syndrome include malformations of the heart or kidneys.
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A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
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RBM8A (Human) Recombinant Protein (P01)
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The Exon Junction Complex Core Represses Caner-Specific Mature Mrna Re-Splicing: a Potential Key Role in Terminating Splicing
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Downloaded from molecularcasestudies.cshlp.org on September 26, 2021 - Published by Cold Spring Harbor Laboratory Press COLD SPRING HARBOR Molecular Case Studies | RESEARCH ARTICLE 1q21.1 deletion and a rare functional polymorphism in siblings with thrombocytopenia-absent radius–like phenotypes Seth A. Brodie,1 Jean Paul Rodriguez-Aulet,2 Neelam Giri,2 Jieqiong Dai,1 Mia Steinberg,1 Joshua J. Waterfall,3 David Roberson,1 Bari J. Ballew,1 Weiyin Zhou,1 Sarah L. Anzick,3 Yuan Jiang,3 Yonghong Wang,3 Yuelin J. Zhu,3 Paul S. Meltzer,3 Joseph Boland,1 Blanche P. Alter,2 and Sharon A. Savage2 1Cancer Genomics Research Laboratory, Leidos Biomedical Research, NCI-Frederick, Rockville, Maryland 20850, USA; 2Clinical Genetics Branch, Division of Cancer Epidemiology and Genetics, 3Genetics Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20859, USA Abstract Thrombocytopenia-absent radii (TAR) syndrome, characterized by neonatal thrombocytopenia and bilateral radial aplasia with thumbs present, is typically caused by the inheritance of a 1q21.1 deletion and a single-nucelotide polymorphism in RBM8A on the nondeleted allele. We evaluated two siblings with TAR-like dysmorphology but lacking thrombocytopenia in infancy. Family NCI-107 participated in an IRB-approved cohort study and underwent comprehensive clinical and genomic evaluations, including aCGH, whole- exome, whole-genome, and targeted sequencing. Gene expression assays and electromo- bility shift assays (EMSAs) were performed to evaluate the variant of interest. The previously identified TAR-associated 1q21.1 deletion was present in the affected siblings and one healthy parent. Multiple sequencing approaches did not identify previously described TAR-associated SNPs or mutations in relevant genes.
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RBM8A Gene RNA Binding Motif Protein 8A
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MOLECULAR MEDICINE REPORTS 9: 163-165, 2014 Prenatal detection of TAR syndrome in a fetus with compound inheritance of an RBM8A SNP and a 334‑kb deletion: A case report IOANNIS PAPOULIDIS1, EIRINI OIKONOMIDOU1, SANDRO ORRU2, ELISAVET SIOMOU1, MARIA KONTODIOU1, MAKARIOS ELEFTHERIADES3, VASILIOS BACOULAS4, JUAN C. CIGUDOSA5, JAVIER SUELA5, LORETTA THOMAIDIS6 and EMMANOUIL MANOLAKOS1,2 1Laboratory of Genetics, Eurogenetica S.A., Thessaloniki 55133, Greece; 2Department of Medical Genetics, University of Cagliari, Binaghi Hospital, Cagliari I‑09126, Italy; 3Embryocare, Fetal Medicine Unit, Athens 11522; 4Fetal Medicine Centre, Athens 10674, Greece; 5NIMGenetics, Madrid 28049, Spain; 6Department of Pediatrics, Aglaia Kyriakou Children's Hospital, University of Athens, Athens 11527, Greece Received May 30, 2013; Accepted October 16, 2013 DOI: 10.3892/mmr.2013.1788 Abstract. Thrombocytopenia-absent radius syndrome identified the presence of a minimally deleted 200‑kb region (TAR) is a rare genetic disorder that is characterized by the at chromosome band 1q21.1 in patients with TAR, but it is not absence of the radius bone in each forearm and a markedly sufficient to cause the phenotype (3,4). A study identified two reduced platelet count that results in life-threatening bleeding rare single nucleotide polymorphisms (SNPs) in the regulatory episodes (thrombocytopenia). Tar syndrome has been associ- region of the RBM8A gene that are involved in TAR syndrome ated with a deletion of a segment of 1q21.1 cytoband. The through the reduction of the expression of the RBM8A-encoded 1q21.1 deletion syndrome phenotype includes Tar and other Y14 protein (4). The first allele (rs139428292 G>A), which is features such as mental retardation, autism and microcephaly.
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International Journal of Molecular Sciences Review Nucleocytoplasmic Transport: Regulatory Mechanisms and the Implications in Neurodegeneration Baojin Ding * and Masood Sepehrimanesh Department of Biology, University of Louisiana at Lafayette, 410 East Saint Mary Boulevard, Lafayette, LA 70503, USA; [email protected] * Correspondence: [email protected] Abstract: Nucleocytoplasmic transport (NCT) across the nuclear envelope is precisely regulated in eukaryotic cells, and it plays critical roles in maintenance of cellular homeostasis. Accumulating evidence has demonstrated that dysregulations of NCT are implicated in aging and age-related neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), Alzheimer’s disease (AD), and Huntington disease (HD). This is an emerging research ﬁeld. The molecular mechanisms underlying impaired NCT and the pathogenesis leading to neurodegener- ation are not clear. In this review, we comprehensively described the components of NCT machinery, including nuclear envelope (NE), nuclear pore complex (NPC), importins and exportins, RanGTPase and its regulators, and the regulatory mechanisms of nuclear transport of both protein and transcript cargos. Additionally, we discussed the possible molecular mechanisms of impaired NCT underlying aging and neurodegenerative diseases, such as ALS/FTD, HD, and AD. Keywords: Alzheimer’s disease; amyotrophic lateral sclerosis; Huntington disease; neurodegenera- tive diseases; nuclear pore complex; nucleocytoplasmic transport; Ran GTPase Citation: Ding, B.; Sepehrimanesh, M. Nucleocytoplasmic Transport: Regulatory Mechanisms and the Implications in Neurodegeneration. 1. Introduction Int. J. Mol. Sci. 2021, 22, 4165. As a hallmark of eukaryotic cells, the genetic materials are separated from the cyto- https://doi.org/10.3390/ijms plasmic contents by a highly regulated membrane, called nuclear envelope (NE), which 22084165 has two concentric bilayer membranes, the inner nuclear membrane (INM), and outer nuclear membrane (ONM).
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Produktinformation Diagnostik & molekulare Diagnostik Laborgeräte & Service Zellkultur & Verbrauchsmaterial Forschungsprodukte & Biochemikalien Weitere Information auf den folgenden Seiten! See the following pages for more information! Lieferung & Zahlungsart Lieferung: frei Haus Bestellung auf Rechnung SZABO-SCANDIC Lieferung: € 10,- HandelsgmbH & Co KG Erstbestellung Vorauskassa Quellenstraße 110, A-1100 Wien T. +43(0)1 489 3961-0 Zuschläge F. +43(0)1 489 3961-7 [email protected] • Mindermengenzuschlag www.szabo-scandic.com • Trockeneiszuschlag • Gefahrgutzuschlag linkedin.com/company/szaboscandic • Expressversand facebook.com/szaboscandic SAN TA C RUZ BI OTEC HNOL OG Y, INC . karyopherin 13 siRNA (h): sc-62521 BACKGROUND STORAGE AND RESUSPENSION Belonging to the importin β family, karyopherin 13 (Kap13), also known as Store lyophilized siRNA duplex at -20° C with desiccant. Stable for at least Importin-13 (IPO13) or Ran-binding protein 13, is a 963 amino acid protein that one year from the date of shipment. Once resuspended, store at -20° C, contains 20 HEAT repeats and one importin N-terminal domain. Localizing to avoid contact with RNAses and repeated freeze thaw cycles. the nucleus as well as the cytoplasm, karyopherin 13 is expressed in fetal Resuspend lyophilized siRNA duplex in 330 µl of the RNAse-free water brain, heart, intestine and kidney. Karyopherin 13 acts as a nuclear transport pro vided. Resuspension of the siRNA duplex in 330 µl of RNAse-free water receptor, participating in nuclear protein import and nuclear localization sig - makes a 10 µM solution in a 10 µM Tris-HCl, pH 8.0, 20 mM NaCl, 1 mM nals (NLS) in cargo substrates, in a Ras-related nuclear protein-GTPase EDTA buffered solution.
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