RPS4X Monoclonal Antibody (M01A), Clone 3E10

Total Page：16

File Type：pdf, Size：1020Kb

RPS4X monoclonal antibody (M01A), clone 3E10 Catalog # : H00006191-M01A 規格 : [ 200 uL ] List All Specification Application Image Product Mouse monoclonal antibody raised against a partial recombinant ELISA Description: RPS4X. Immunogen: RPS4X (NP_000998, 74 a.a. ~ 177 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. Sequence: GKVRTDITYPAGFMDVISIDKTGENFRLIYDTKGRFAVHRITPEEAKYKLC KVRKIFVGTKGIPHLVTHDARTIRYPDPLIKVNDTIQIDLETGKITDFIKFDT Host: Mouse Reactivity: Human Isotype: IgM Kappa Quality Control Antibody Reactive Against Recombinant Protein. Testing: Storage Buffer: In ascites fluid Storage Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. Instruction: MSDS: Download Datasheet: Download Applications ELISA Gene Information Entrez GeneID: 6191 GeneBank NM_001007 Accession#: Protein NP_000998 Accession#: Gene Name: RPS4X Gene Alias: CCG2,DXS306,FLJ40595,SCAR,SCR10 Gene ribosomal protein S4, X-linked Description: Omim ID: 312760 Gene Ontology: Hyperlink Page 1 of 2 2020/6/25 Gene Summary: Cytoplasmic ribosomes, organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes ribosomal protein S4, a component of the 40S subunit. Ribosomal protein S4 is the only ribosomal protein known to be encoded by more than one gene, namely this gene and ribosomal protein S4, Y-linked (RPS4Y). The 2 isoforms encoded by these genes are not identical, but are functionally equivalent. Ribosomal protein S4 belongs to the S4E family of ribosomal proteins. This gene is not subject to X-inactivation. It has been suggested that haploinsufficiency of the ribosomal protein S4 genes plays a role in Turner syndrome; however, this hypothesis is controversial. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. [provided by RefSeq Other 40S ribosomal protein S4, X isoform,OTTHUMP00000023537,cell cycle Designations: gene 2,ribosomal protein S4X isoform,single-copy abundant mRNA Gene Pathway Ribosome 服務條款 | 隱私權政策 | 著作及商標 | 網站地圖 ©2020 亞諾法生技股份有限公司 Abnova Corporation. 版權所有. Page 2 of 2 2020/6/25.

Copy Link

Recommended publications

Different Genetic Mechanisms Mediate Spontaneous Versus UVR-Induced
RESEARCH ARTICLE Different genetic mechanisms mediate spontaneous versus UVR-induced malignant melanoma Blake Ferguson1, Herlina Y Handoko1, Pamela Mukhopadhyay1, Arash Chitsazan1, Lois Balmer2,3, Grant Morahan2, Graeme J Walker1†* 1Drug Discovery Group, QIMR Berghofer Medical Research Institute, Herston, Australia; 2Centre for Diabetes Research, Harry Perkins Institute of Medical Research, Perth, Australia; 3School of Medical and Health Sciences, Edith Cowan University, Joondalup, Australia Abstract Genetic variation conferring resistance and susceptibility to carcinogen-induced tumorigenesis is frequently studied in mice. We have now turned this idea to melanoma using the collaborative cross (CC), a resource of mouse strains designed to discover genes for complex diseases. We studied melanoma-prone transgenic progeny across seventy CC genetic backgrounds. We mapped a strong quantitative trait locus for rapid onset spontaneous melanoma onset to Prkdc, a gene involved in detection and repair of DNA damage. In contrast, rapid onset UVR-induced melanoma was linked to the ribosomal subunit gene Rrp15. Ribosome biogenesis was upregulated in skin shortly after UVR exposure. Mechanistically, variation in the ‘usual suspects’ by which UVR may exacerbate melanoma, defective DNA repair, melanocyte proliferation, or inflammatory cell infiltration, did not explain melanoma susceptibility or resistance across the CC. *For correspondence: [email protected] Instead, events occurring soon after exposure, such as dysregulation of ribosome function, which alters many aspects of cellular metabolism, may be important. † Present address: Experimental DOI: https://doi.org/10.7554/eLife.42424.001 Dermatology Group, The University of Queensland Diamantina Institute, Woolloongabba, Australia Introduction Competing interests: The Cutaneous malignant melanoma (MM) is well known to be associated with high levels of sun expo- authors declare that no sure.
[Show full text]
Anti-MRPS17 Monoclonal Antibody, Clone FQS23694 (DCABH-6110) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Anti-MRPS17 monoclonal antibody, clone FQS23694 (DCABH-6110) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Rabbit monoclonal to MRPS17 Antigen Description Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein that belongs to the ribosomal protein S17P family. The encoded protein is moderately conserved between human mitochondrial and prokaryotic ribosomal proteins. Pseudogenes corresponding to this gene are found on chromosomes 1p, 3p, 6q, 14p, 18q, and Xq. Immunogen Recombinant fragment within Human MRPS17. The exact sequence is proprietary.Database link: Q9Y2R5 Isotype IgG Source/Host Rabbit Species Reactivity Human Clone FQS23694 Purity Tissue culture supernatant Conjugate Unconjugated Applications IHC-P, WB, ICC/IF, IP Positive Control HeLa, HepG2 and U937 cell lysate; Human kidney and liver tissue; HeLa cells Format Liquid Size 100 μl Buffer pH: 7.2; Preservative: 0.01% Sodium azide; Constituents: 49% PBS, 0.05% BSA, 50% Glycerol 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Preservative 0.01% Sodium Azide Storage Store at +4°C short term (1-2 weeks).
[Show full text]
Micrornas Mediated Regulation of the Ribosomal Proteins and Its Consequences on the Global Translation of Proteins
cells Review microRNAs Mediated Regulation of the Ribosomal Proteins and Its Consequences on the Global Translation of Proteins Abu Musa Md Talimur Reza 1,2 and Yu-Guo Yuan 1,3,* 1 Jiangsu Co-Innovation Center of Prevention and Control of Important Animal Infectious Diseases and Zoonoses, College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China; [email protected] 2 Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawi´nskiego5a, 02-106 Warsaw, Poland 3 Jiangsu Key Laboratory of Zoonosis/Joint International Research Laboratory of Agriculture and Agri-Product Safety, The Ministry of Education of China, Yangzhou University, Yangzhou 225009, China * Correspondence: [email protected]; Tel.: +86-514-8797-9228 Abstract: Ribosomal proteins (RPs) are mostly derived from the energy-consuming enzyme families such as ATP-dependent RNA helicases, AAA-ATPases, GTPases and kinases, and are important structural components of the ribosome, which is a supramolecular ribonucleoprotein complex, composed of Ribosomal RNA (rRNA) and RPs, coordinates the translation and synthesis of proteins with the help of transfer RNA (tRNA) and other factors. Not all RPs are indispensable; in other words, the ribosome could be functional and could continue the translation of proteins instead of lacking in some of the RPs. However, the lack of many RPs could result in severe defects in the biogenesis of ribosomes, which could directly inﬂuence the overall translation processes and global expression of the proteins leading to the emergence of different diseases including cancer. While microRNAs (miRNAs) are small non-coding RNAs and one of the potent regulators of the post-transcriptional 0 gene expression, miRNAs regulate gene expression by targeting the 3 untranslated region and/or coding region of the messenger RNAs (mRNAs), and by interacting with the 50 untranslated region, Citation: Reza, A.M.M.T.; Yuan, Y.-G.
[Show full text]
Mitochondrial Translation and Its Impact on Protein Homeostasis And
Mitochondrial translation and its impact on protein homeostasis and aging Tamara Suhm Academic dissertation for the Degree of Doctor of Philosophy in Biochemistry at Stockholm University to be publicly defended on Friday 15 February 2019 at 09.00 in Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B. Abstract Besides their famous role as powerhouse of the cell, mitochondria are also involved in many signaling processes and metabolism. Therefore, it is unsurprising that mitochondria are no isolated organelles but are in constant crosstalk with other parts of the cell. Due to the endosymbiotic origin of mitochondria, they still contain their own genome and gene expression machinery. The mitochondrial genome of yeast encodes eight proteins whereof seven are core subunits of the respiratory chain and ATP synthase. These subunits need to be assembled with subunits imported from the cytosol to ensure energy supply of the cell. Hence, coordination, timing and accuracy of mitochondrial gene expression is crucial for cellular energy production and homeostasis. Despite the central role of mitochondrial translation surprisingly little is known about the molecular mechanisms. In this work, I used baker’s yeast Saccharomyces cerevisiae to study different aspects of mitochondrial translation. Exploiting the unique possibility to make directed modifications in the mitochondrial genome of yeast, I established a mitochondrial encoded GFP reporter. This reporter allows monitoring of mitochondrial translation with different detection methods and enables more detailed studies focusing on timing and regulation of mitochondrial translation. Furthermore, employing insights gained from bacterial translation, we showed that mitochondrial translation efficiency directly impacts on protein homeostasis of the cytoplasm and lifespan by affecting stress handling.
[Show full text]
The Role of Human Ribosomal Proteins in the Maturation of Rrna and Ribosome Production
JOBNAME: RNA 14#9 2008 PAGE: 1 OUTPUT: Friday August 8 17:34:50 2008 csh/RNA/164293/rna11320 Downloaded from rnajournal.cshlp.org on September 27, 2021 - Published by Cold Spring Harbor Laboratory Press The role of human ribosomal proteins in the maturation of rRNA and ribosome production SARA ROBLEDO,1,3 RACHEL A. IDOL,1,3 DAN L. CRIMMINS,2 JACK H. LADENSON,2 PHILIP J. MASON,1,4 and MONICA BESSLER1,4 1Department of Internal Medicine, Division of Hematology, Washington University School of Medicine, St. Louis, Missouri 63110, USA 2Department of Pathology and Immunology, Division of Laboratory and Genomic Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA ABSTRACT Production of ribosomes is a fundamental process that occurs in all dividing cells. It is a complex process consisting of the coordinated synthesis and assembly of four ribosomal RNAs (rRNA) with about 80 ribosomal proteins (r-proteins) involving more than 150 nonribosomal proteins and other factors. Diamond Blackfan anemia (DBA) is an inherited red cell aplasia caused by mutations in one of several r-proteins. How defects in r-proteins, essential for proliferation in all cells, lead to a human disease with a specific defect in red cell development is unknown. Here, we investigated the role of r-proteins in ribosome biogenesis in order to find out whether those mutated in DBA have any similarities. We depleted HeLa cells using siRNA for several individual r-proteins of the small (RPS6, RPS7, RPS15, RPS16, RPS17, RPS19, RPS24, RPS25, RPS28) or large subunit (RPL5, RPL7, RPL11, RPL14, RPL26, RPL35a) and studied the effect on rRNA processing and ribosome production.
[Show full text]
Analyzing Ribosome Remodeling in Health and Disease Aleksandra A
Analyzing ribosome remodeling in health and disease Aleksandra A. Petelski,1;2;3 & Nikolai Slavov1;2;3; 1Department of Bioengineering, Northeastern University, Boston, MA 02115, USA 2Barnett Institute, Northeastern University, Boston, MA 02115, USA 3Department of Biology, Northeastern University, Boston, MA 02115, USA Correspondence: [email protected] or [email protected] Increasing evidence suggests that ribosomes actively regulate protein synthesis. However, much of this evidence is indirect, leaving this layer of gene regulation largely unexplored, in part due to methodological limitations. Indeed, we review evidence demonstrating that commonly used methods, such as transcriptomics, are inadequate because the variability in mRNAs coding for ribosomal proteins (RP) does not necessarily correspond to RP variability. Thus protein remodeling of ribosomes should be investigated by methods that allow direct quantiﬁcation of RPs, ideally of isolated ribosomes. We review such methods, focusing on mass spectrometry and emphasizing method-speciﬁc biases and approaches to control these biases. We argue that using multiple complementary methods can help reduce the danger of interpreting reproducible systematic biases as evidence for ribosome remodeling. Introduction The control of gene expression is crucial for all biological processes, from developmental stages and homeostasis maintenance to regeneration processes. This regulation occurs at multiple layers, both transcriptional and post-transcriptional levels. Historically, transcription has been studied more extensively than translation, in large part because of the accessibility of technologies for nucleic acid analysis. However, gene regulation via translation was appreciated as early as the late arXiv:2007.05839v2 [q-bio.QM] 2 Aug 2020 1960’s. For example, the production of insulin was linked to the increased number of polysomes and protein synthesis [1].
[Show full text]
History of the Ribosome and the Origin of Translation
History of the ribosome and the origin of translation Anton S. Petrova,1, Burak Gulena, Ashlyn M. Norrisa, Nicholas A. Kovacsa, Chad R. Berniera, Kathryn A. Laniera, George E. Foxb, Stephen C. Harveyc, Roger M. Wartellc, Nicholas V. Huda, and Loren Dean Williamsa,1 aSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332; bDepartment of Biology and Biochemistry, University of Houston, Houston, TX, 77204; and cSchool of Biology, Georgia Institute of Technology, Atlanta, GA 30332 Edited by David M. Hillis, The University of Texas at Austin, Austin, TX, and approved November 6, 2015 (received for review May 18, 2015) We present a molecular-level model for the origin and evolution of building up of the functional centers, proceeds to the establishment the translation system, using a 3D comparative method. In this model, of the common core, and continues to the development of large the ribosome evolved by accretion, recursively adding expansion metazoan rRNAs. segments, iteratively growing, subsuming, and freezing the rRNA. Incremental evolution of function is mapped out by stepwise Functions of expansion segments in the ancestral ribosome are accretion of rRNA. In the extant ribosome, specific segments of assigned by correspondence with their functions in the extant rRNA perform specific functions including peptidyl transfer, ribosome. The model explains the evolution of the large ribosomal subunit association, decoding, and energy-driven translocation subunit, the small ribosomal subunit, tRNA, and mRNA. Prokaryotic (11). The model assumes that the correlations of rRNA segments ribosomes evolved in six phases, sequentially acquiring capabilities with their functions have been reasonably maintained over the for RNA folding, catalysis, subunit association, correlated evolution, broad course of ribosomal evolution.
[Show full text]
RPSA Gene Ribosomal Protein SA
RPSA gene ribosomal protein SA Normal Function The RPSA gene provides instructions for making a protein called ribosomal protein SA, which is one of approximately 80 different ribosomal proteins. These proteins come together to form structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins. Each ribosome is made up of two parts (subunits) called the large subunit and the small subunit. Ribosomal protein SA is part of the small subunit. The specific roles of each of the ribosomal proteins within the ribosome are not entirely understood. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Research suggests that ribosomal protein SA helps the ribosome control the production of certain proteins, many of which are likely important for development before birth. Health Conditions Related to Genetic Changes Isolated congenital asplenia At least 20 RPSA gene mutations have been identified in individuals with isolated congenital asplenia. People with this condition do not have a spleen but have no other developmental abnormalities. The spleen plays an important role in the immune system. Without this organ, affected individuals are highly susceptible to bacterial infections, which can be life-threatening. RPSA gene mutations are thought to reduce the amount of functional ribosomal protein SA. A shortage of the normal protein likely impairs the assembly of ribosomes, but the specific effects of the mutations
[Show full text]
Cell-Type-Specific Isolation of Ribosome-Associated Mrna from Complex Tissues
Cell-type-specific isolation of ribosome-associated mRNA from complex tissues Elisenda Sanza, Linghai Yanga, Thomas Sua, David R. Morrisb, G. Stanley McKnighta, and Paul S. Amieuxa,1 Departments of bBiochemistry and aPharmacology, University of Washington, Seattle, WA 98195 Communicated by Richard D. Palmiter, University of Washington School of Medicine, Seattle, WA, June 26, 2009 (received for review May 1, 2009) Gene profiling techniques allow the assay of transcripts from noprecipitation. Messenger RNA transcripts found in the target organs, tissues, and cells with an unprecedented level of coverage. cell population can be isolated from the immunoprecipitated However, most of these approaches are still limited by the fact that polyribosomes and analyzed using standard genomic profiling organs and tissues are composed of multiple cell types that are technologies such as quantitative RT-PCR (qRT-PCR) or mi- each unique in their patterns of gene expression. To identify the croarray. The advantages of this approach are the widespread transcriptome from a single cell type in a complex tissue, investi- availability of well-characterized Cre recombinase-expressing gators have relied upon physical methods to separate cell types or mouse lines and the robust expression of the epitope-tagged in situ hybridization and immunohistochemistry. Here, we describe ribosomal protein subunit from the endogenous allele. a strategy to rapidly and efficiently isolate ribosome-associated mRNA transcripts from any cell type in vivo. We have created a Results mouse line, called RiboTag, which carries an Rpl22 allele with a Selection of Ribosomal Proteins for Epitope Tagging and Design of the floxed wild-type C-terminal exon followed by an identical C- Targeting Vector.
[Show full text]
Mrna Stem-Loops Can Pause the Ribosome by Hindering A-Site Trna
RESEARCH ARTICLE mRNA stem-loops can pause the ribosome by hindering A-site tRNA binding Chen Bao1†, Sarah Loerch2†, Clarence Ling1, Andrei A Korostelev3,4, Nikolaus Grigorieff2,4*, Dmitri N Ermolenko1* 1Department of Biochemistry and Biophysics at School of Medicine and Dentistry and Center for RNA Biology, University of Rochester, Rochester, United States; 2Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States; 3Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, United States; 4RNA Therapeutics Institute, University of Massachusetts Medical School, Worcester, United States Abstract Although the elongating ribosome is an efficient helicase, certain mRNA stem-loop structures are known to impede ribosome movement along mRNA and stimulate programmed ribosome frameshifting via mechanisms that are not well understood. Using biochemical and single- molecule Fo¨ rster resonance energy transfer (smFRET) experiments, we studied how frameshift- inducing stem-loops from E. coli dnaX mRNA and the gag-pol transcript of Human Immunodeficiency Virus (HIV) perturb translation elongation. We find that upon encountering the ribosome, the stem-loops strongly inhibit A-site tRNA binding and ribosome intersubunit rotation *For correspondence: that accompanies translation elongation. Electron cryo-microscopy (cryo-EM) reveals that the HIV [email protected] (NG); stem-loop docks into the A site of the ribosome. Our results suggest that mRNA stem-loops can Dmitri_Ermolenko@urmc. transiently escape the ribosome helicase by binding to the A site. Thus, the stem-loops can rochester.edu (DNE) modulate gene expression by sterically hindering tRNA binding and inhibiting translation †These authors contributed elongation. equally to this work Competing interest: See page 22 Introduction Funding: See page 22 During translation elongation, the ribosome moves along mRNA in a codon-by-codon manner while Received: 06 February 2020 the mRNA is threaded through the mRNA channel of the small ribosomal subunit.
[Show full text]
Elabscience.Com ® E-Mail:[email protected] Elabscience Elabscience Biotechnology Inc
Tel:240-252-7368(USA) Fax:240-252-7376(USA) www.elabscience.com ® E-mail:[email protected] Elabscience Elabscience Biotechnology Inc. MRPL20 Polyclonal Antibody Catalog No. E-AB-18777 Reactivity H,M Storage Store at -20℃. Avoid freeze / thaw cycles. Host Rabbit Applications WB,IHC,ELISA Isotype IgG Note: Centrifuge before opening to ensure complete recovery of vial contents. Images Immunogen Information Immunogen Fusion protein of human MRPL20 Gene Accession BC009515 Swissprot Q9BYC9 Synonyms 39S ribosomal protein L20,mitochondrial,L20mt,MG C4779,MGC74465,Mitochondrial ribosomal protein L20,MRPL 20 Western blot analysis of RAW264.7 Product Information cell lysate using MRPL20 Polyclonal Calculated MW 17 kDa Antibody at dilution of 1:900 Observed MW Refer to figures Buffer PBS with 0.05% NaN3 and 40% Glycerol,pH7.4 Purify Antigen affinity purification Dilution WB 1:500-1:2000, IHC 1:50-1:200, ELISA 1:5000-1:10000 Background MRPL20 is one of more than 70 protein components of mitochondrial Immunohistochemistry of paraffin- ribosomes that are encoded by the nuclear genome. MRPL20 is a subunit embedded Human liver cancer tissue of the 39S mitochondrial ribosome. Mitochondrial ribosomes using MRPL20 Polyclonal Antibody at (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. dilution of 1:60(×200) They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology.
[Show full text]
An Update on Mitochondrial Ribosome Biology: the Plant Mitoribosome in the Spotlight
cells Review An Update on Mitochondrial Ribosome Biology: The Plant Mitoribosome in the Spotlight Artur Tomal y , Malgorzata Kwasniak-Owczarek y and Hanna Janska * Department of Cellular Molecular Biology, Faculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland; [email protected] (A.T.); [email protected] (M.K.-O.) * Correspondence: [email protected]; Tel.: +0048-713-756-249; Fax: +0048-713-756-234 These authors contributed equally to this work. y Received: 31 October 2019; Accepted: 1 December 2019; Published: 3 December 2019 Abstract: Contrary to the widely held belief that mitochondrial ribosomes (mitoribosomes) are highly similar to bacterial ones, recent experimental evidence reveals that mitoribosomes do differ significantly from their bacterial counterparts. This review is focused on plant mitoribosomes, but we also highlight the most striking similarities and differences between the plant and non-plant mitoribosomes. An analysis of the composition and structure of mitoribosomes in trypanosomes, yeast, mammals and plants uncovers numerous organism-specific features. For the plant mitoribosome, the most striking feature is the enormous size of the small subunit compared to the large one. Apart from the new structural information, possible functional peculiarities of different types of mitoribosomes are also discussed. Studies suggest that the protein composition of mitoribosomes is dynamic, especially during development, giving rise to a heterogeneous populations of ribosomes fulfilling specific functions. Moreover, convincing data shows that mitoribosomes interact with components involved in diverse mitochondrial gene expression steps, forming large expressosome-like structures. Keywords: mitochondrial ribosome; ribosomal proteins; ribosomal rRNA; PPR proteins; translation; plant mitoribosome 1.
[Show full text]