MRPS26 Rabbit Pab 产品说明书

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正能生物 MRPS26 Rabbit pAb 货号：385013 Size 100ul 50ul Antibody type Primary antibody Conjugation Unconjugated Modification Unmodification Isotype Rabbit IgG Host Rabbit Application WB , ICC/IF Purification Affinity purified Cross reactivity Human Gene name MRPS26 Alternative names GI008; MRPS13; RPMS13; MRP-S13; MRP-S26; NY-BR-87; C20orf193; dJ534B8.3 Gene symbol GI008; MRPS13; RPMS13; MRP-S13; MRP-S26; NY-BR-87; C20orf193; dJ534B8.3 Description Swiss-Prot Acc.Q9BYN8.28S ribosomal protein S26, mitochondrial Immunogen Recombinant protein of human MRPS26 Clonality Polyclonal antibody Antigen name 28S ribosomal protein S26, mitochondrial Gene ID 64949 Unigene 64949 Formulation Supplied in 50nM Tris-Glycine(pH 7.4), 0.15M Nacl, 40%Glycerol, 0.01% sodium azide and 0.05% BSA. Subcellular location Mitochondrion Storage Store at -20°C. Stable for 12 months from date of receipt. Dilution WB: 1/1000; ICC/IF: 1/50 Target description 28S ribosomal protein S26, mitochondrial Gene fullname mitochondrial ribosomal protein S26 SwissProt ID Q9BYN8 Molecular Weight Calculated MW: 24 kDa; Observed MW: 24 kDa Gene summary 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. This gene lies adjacent to and downstream of the gonadotropin-releasing hormone precursor gene. [provided by RefSeq, Jul 2008] Application image Western blot detection of MRPS26 in K562,Hela cell lysates using MRPS26 Rabbit pAb(1:1000 diluted).Predicted band size:24kDa.Observed band size:24kDa. Immunocytochemistry of MRPS26(green) in Hela cells using MRPS26 Rabbit pAb at dilution 1/50, and DAPI(blue) 联系电话： 4008-863-973 传真： 028-85739596 公司地址：成都市高新区科园南路9号附1号爱斯特大厦一层销售邮箱： [email protected].

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MRPS26 Rabbit Pab
Leader in Biomolecular Solutions for Life Science MRPS26 Rabbit pAb Catalog No.: A4940 Basic Information Background Catalog No. Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in A4940 protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% Observed MW protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is 24kDa reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins Calculated MW comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical 24kDa properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein. This gene lies adjacent to and downstream of the gonadotropin- Category releasing hormone precursor gene. Primary antibody Applications WB, IHC Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 64949 Q9BYN8 IHC 1:100 - 1:200 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 1-205 of human MRPS26 (NP_110438.1). Synonyms MRPS26;C20orf193;GI008;MRP-S13;MRP-S26;MRPS13;NY-BR-87;RPMS13;dJ534B8.3 Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using MRPS26 antibody (A4940) at 1:3000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution.
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Supplementary Dataset S2
mitochondrial translational termination MRPL28 MRPS26 6 MRPS21 PTCD3 MTRF1L 4 MRPL50 MRPS18A MRPS17 2 MRPL20 MRPL52 0 MRPL17 MRPS33 MRPS15 −2 MRPL45 MRPL30 MRPS27 AURKAIP1 MRPL18 MRPL3 MRPS6 MRPS18B MRPL41 MRPS2 MRPL34 GADD45GIP1 ERAL1 MRPL37 MRPS10 MRPL42 MRPL19 MRPS35 MRPL9 MRPL24 MRPS5 MRPL44 MRPS23 MRPS25 ITB ITB ITB ITB ICa ICr ITL original ICr ICa ITL ICa ITL original ICr ITL ICr ICa mitochondrial translational elongation MRPL28 MRPS26 6 MRPS21 PTCD3 MRPS18A 4 MRPS17 MRPL20 2 MRPS15 MRPL45 MRPL52 0 MRPS33 MRPL30 −2 MRPS27 AURKAIP1 MRPS10 MRPL42 MRPL19 MRPL18 MRPL3 MRPS6 MRPL24 MRPS35 MRPL9 MRPS18B MRPL41 MRPS2 MRPL34 MRPS5 MRPL44 MRPS23 MRPS25 MRPL50 MRPL17 GADD45GIP1 ERAL1 MRPL37 ITB ITB ITB ITB ICa ICr original ICr ITL ICa ITL ICa ITL original ICr ITL ICr ICa translational termination MRPL28 MRPS26 6 MRPS21 PTCD3 C12orf65 4 MTRF1L MRPL50 MRPS18A 2 MRPS17 MRPL20 0 MRPL52 MRPL17 MRPS33 −2 MRPS15 MRPL45 MRPL30 MRPS27 AURKAIP1 MRPL18 MRPL3 MRPS6 MRPS18B MRPL41 MRPS2 MRPL34 GADD45GIP1 ERAL1 MRPL37 MRPS10 MRPL42 MRPL19 MRPS35 MRPL9 MRPL24 MRPS5 MRPL44 MRPS23 MRPS25 ITB ITB ITB ITB ICa ICr original ICr ITL ICa ITL ICa ITL original ICr ITL ICr ICa translational elongation DIO2 MRPS18B MRPL41 6 MRPS2 MRPL34 GADD45GIP1 4 ERAL1 MRPL37 2 MRPS10 MRPL42 MRPL19 0 MRPL30 MRPS27 AURKAIP1 −2 MRPL18 MRPL3 MRPS6 MRPS35 MRPL9 EEF2K MRPL50 MRPS5 MRPL44 MRPS23 MRPS25 MRPL24 MRPS33 MRPL52 EIF5A2 MRPL17 SECISBP2 MRPS15 MRPL45 MRPS18A MRPS17 MRPL20 MRPL28 MRPS26 MRPS21 PTCD3 ITB ITB ITB ITB ICa ICr ICr ITL original ITL ICa ICa ITL ICr ICr ICa original
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C6orf203 Controls OXPHOS Function Through Modulation of Mitochondrial Protein Biosynthesis
bioRxiv preprint doi: https://doi.org/10.1101/704403; this version posted July 17, 2019. 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. C6orf203 controls OXPHOS function through modulation of mitochondrial protein biosynthesis number of characters excluding Materials and Methods: 40,651 Sara Palacios-Zambrano1,2, Luis Vázquez-Fonseca1,2, Cristina González-Páramos1,2, Laura Mamblona1,2, Laura Sánchez-Caballero3, Leo Nijtmans3, Rafael Garesse1,2 and Miguel Angel Fernández-Moreno1,2,* 1 Departamento de Bioquímica, Instituto de Investigaciones Biomédicas “Alberto Sols” UAM CSIC and Centro de Investigación Biomédica en Red en Enfermedades Raras (CIBERER). Facultad de Medicina, Universidad Autónoma de Madrid. Madrid 28029, Spain. 2 Instituto de Investigación Sanitaria Hospital 12 de Octubre (imas12), Madrid 28041, Spain. 3 Department of Pediatrics, Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, Nijmegen, The Netherlands. * To whom correspondence should be addressed. Tel:+34 91 497 31 29; Email: [email protected] Running title “C6orf203 controls mt-proteins synthesis” bioRxiv preprint doi: https://doi.org/10.1101/704403; this version posted July 17, 2019. 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 Mitochondria are essential organelles present in the vast majority of eukaryotic cells. Their central function is to produce cellular energy through the OXPHOS system, and functional alterations provoke so-called mitochondrial OXPHOS diseases. It is estimated that several hundred mitochondrial proteins have unknown functions. Very recently, C6orf203 was described to participate in mitochondrial transcription under induced mitochondrial DNA depletion stress conditions.
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Transcriptomic and Proteomic Landscape of Mitochondrial
TOOLS AND RESOURCES Transcriptomic and proteomic landscape of mitochondrial dysfunction reveals secondary coenzyme Q deficiency in mammals Inge Ku¨ hl1,2†*, Maria Miranda1†, Ilian Atanassov3, Irina Kuznetsova4,5, Yvonne Hinze3, Arnaud Mourier6, Aleksandra Filipovska4,5, Nils-Go¨ ran Larsson1,7* 1Department of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, Cologne, Germany; 2Department of Cell Biology, Institute of Integrative Biology of the Cell (I2BC) UMR9198, CEA, CNRS, Univ. Paris-Sud, Universite´ Paris-Saclay, Gif- sur-Yvette, France; 3Proteomics Core Facility, Max Planck Institute for Biology of Ageing, Cologne, Germany; 4Harry Perkins Institute of Medical Research, The University of Western Australia, Nedlands, Australia; 5School of Molecular Sciences, The University of Western Australia, Crawley, Australia; 6The Centre National de la Recherche Scientifique, Institut de Biochimie et Ge´ne´tique Cellulaires, Universite´ de Bordeaux, Bordeaux, France; 7Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden Abstract Dysfunction of the oxidative phosphorylation (OXPHOS) system is a major cause of human disease and the cellular consequences are highly complex. Here, we present comparative *For correspondence: analyses of mitochondrial proteomes, cellular transcriptomes and targeted metabolomics of five [email protected] knockout mouse strains deficient in essential factors required for mitochondrial DNA gene (IKu¨ ); expression, leading to OXPHOS dysfunction. Moreover,
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OXA1L Mutations Cause Mitochondrial Encephalopathy and a Combined Oxidative Phosphorylation Defect
Research Article OXA1L mutations cause mitochondrial encephalopathy and a combined oxidative phosphorylation defect Kyle Thompson1, Nicole Mai1, Monika Oláhová1, Filippo Scialó2, Luke E Formosa3, David A Stroud4, Madeleine Garrett3, Nichola Z Lax1, Fiona M Robertson1, Cristina Jou5, Andres Nascimento6, Carlos Ortez6, Cecilia Jimenez-Mallebrera6, Steven A Hardy1, Langping He1, Garry K Brown7, Paula Marttinen8, Robert McFarland1 , Alberto Sanz2, Brendan J Battersby8 , Penelope E Bonnen9, Michael T Ryan3, Zofia MA Chrzanowska-Lightowlers1, Robert N Lightowlers1 & Robert W Taylor1,* Abstract Introduction OXA1, the mitochondrial member of the YidC/Alb3/Oxa1 membrane Mitochondrial disorders encompass a wide range of clinical pheno- protein insertase family, is required for the assembly of oxidative types and are genetically heterogeneous. Mitochondrial dysfunction phosphorylation complexes IV and V in yeast. However, depletion can arise from mutations in either the maternally inherited mito- of human OXA1 (OXA1L) was previously reported to impair assem- chondrial genome (mtDNA) or in nuclear genes that encode mito- bly of complexes I and V only. We report a patient presenting with chondrial proteins. The 13 mtDNA-encoded polypeptides are severe encephalopathy, hypotonia and developmental delay who essential components of the oxidative phosphorylation (OXPHOS) died at 5 years showing complex IV deficiency in skeletal muscle. system. Many nuclear genetic defects causing mitochondrial disease Whole exome sequencing identified biallelic OXA1L variants are in gene products required for maintaining correct expression of (c.500_507dup, p.(Ser170Glnfs*18) and c.620G>T, p.(Cys207Phe)) mtDNA. These include proteins involved in replication, mtDNA that segregated with disease. Patient muscle and fibroblasts maintenance, transcription, mtRNA processing, maturation and showed decreased OXA1L and subunits of complexes IV and V.
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A Meta-Analysis of the Effects of High-LET Ionizing Radiations in Human Gene Expression
Supplementary Materials A Meta-Analysis of the Effects of High-LET Ionizing Radiations in Human Gene Expression Table S1. Statistically significant DEGs (Adj. p-value < 0.01) derived from meta-analysis for samples irradiated with high doses of HZE particles, collected 6-24 h post-IR not common with any other meta- analysis group. This meta-analysis group consists of 3 DEG lists obtained from DGEA, using a total of 11 control and 11 irradiated samples [Data Series: E-MTAB-5761 and E-MTAB-5754]. Ensembl ID Gene Symbol Gene Description Up-Regulated Genes ↑ (2425) ENSG00000000938 FGR FGR proto-oncogene, Src family tyrosine kinase ENSG00000001036 FUCA2 alpha-L-fucosidase 2 ENSG00000001084 GCLC glutamate-cysteine ligase catalytic subunit ENSG00000001631 KRIT1 KRIT1 ankyrin repeat containing ENSG00000002079 MYH16 myosin heavy chain 16 pseudogene ENSG00000002587 HS3ST1 heparan sulfate-glucosamine 3-sulfotransferase 1 ENSG00000003056 M6PR mannose-6-phosphate receptor, cation dependent ENSG00000004059 ARF5 ADP ribosylation factor 5 ENSG00000004777 ARHGAP33 Rho GTPase activating protein 33 ENSG00000004799 PDK4 pyruvate dehydrogenase kinase 4 ENSG00000004848 ARX aristaless related homeobox ENSG00000005022 SLC25A5 solute carrier family 25 member 5 ENSG00000005108 THSD7A thrombospondin type 1 domain containing 7A ENSG00000005194 CIAPIN1 cytokine induced apoptosis inhibitor 1 ENSG00000005381 MPO myeloperoxidase ENSG00000005486 RHBDD2 rhomboid domain containing 2 ENSG00000005884 ITGA3 integrin subunit alpha 3 ENSG00000006016 CRLF1 cytokine receptor like
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Mitochondrial Ribosomal Proteins: Candidate Genes for Mitochondrial Disease James E
March/April 2004 ⅐ Vol. 6 ⅐ No. 2 review Mitochondrial ribosomal proteins: Candidate genes for mitochondrial disease James E. Sylvester, PhD1, Nathan Fischel-Ghodsian, MD2, Edward B. Mougey, PhD1, and Thomas W. O’Brien, PhD3 Most of the energy requirement for cell growth, differentiation, and development is met by the mitochondria in the form of ATP produced by the process of oxidative phosphorylation. Human mitochondrial DNA encodes a total of 13 proteins, all of which are essential for oxidative phosphorylation. The mRNAs for these proteins are translated on mitochondrial ribosomes. Recently, the genes for human mitochondrial ribosomal proteins (MRPs) have been identified. In this review, we summarize their refined chromosomal location. It is well known that mutations in the mitochondrial translation system, i.e., ribosomal RNA and transfer RNA cause various pathologies. In this review, we suggest possible associations between clinical conditions and MRPs based on coincidence of genetic map data and chromosomal location. These MRPs may be candidate genes for the clinical condition or may act as modifiers of existing known gene mutations (mt-tRNA, mt-rRNA, etc.). Genet Med 2004:6(2):73–80. Key Words: mitochondrial, ribosomal proteins, oxidative phosphorylation, candidate genes, translation Most of the energy requirements for cell growth, differenti- THE MITORIBOSOME ation, and development are met by the mitochondrial ATP Human cells contain two genomes and two protein synthe- produced by the process of oxidative phosphorylation. Mito- sizing (translation) systems. The first is the nuclear genome of chondrial DNA encodes 13 essential proteins of this oxidative 3 ϫ 109 bp that has 30,000 to 40,000 genes coding a much phosphorylation system.
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Effect of Hyperoside on Cervical Cancer Cells and Transcriptome Analysis Of
Guo et al. Cancer Cell Int (2019) 19:235 https://doi.org/10.1186/s12935-019-0953-4 Cancer Cell International PRIMARY RESEARCH Open Access Efect of hyperoside on cervical cancer cells and transcriptome analysis of diferentially expressed genes Weikang Guo1†, Hui Yu2†, Lu Zhang1, Xiuwei Chen1, Yunduo Liu1, Yaoxian Wang1* and Yunyan Zhang1* Abstract Background: Hyperoside (Hy) is a plant-derived quercetin 3-D-galactoside that exhibits inhibitory activities on vari- ous tumor types. The objective of the current study was to explore Hy efects on cervical cancer cell proliferation, and to perform a transcriptome analysis of diferentially expressed genes. Methods: Cervical cancer HeLa and C-33A cells were cultured and the efect of Hy treatment was determined using the Cell Counting Kit-8 (CCK-8) assay. After calculating the IC50 of Hy in HeLa and C-33A cells, the more sensitive to Hy treatment cell type was selected for RNA-Seq. Diferentially expressed genes (DEGs) were identifed by comparing gene expression between the Hy and control groups. Candidate genes were determined through DEG analysis, pro- tein interaction network (PPI) construction, PPI module analysis, transcription factor (TF) prediction, TF-target network construction, and survival analysis. Finally, the key candidate genes were verifed by RT-qPCR and western blot. Results: Hy inhibited HeLa and C33A cell proliferation in a dose- and time-dependent manner, as determined by the CCK-8 assay. Treatment of C-33A cells with 2 mM Hy was selected for the subsequent experiments. Compared with the control group, 754 upregulated and 509 downregulated genes were identifed after RNA-Seq.
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Mitochondrial Nucleoid Interacting Proteins Support Mitochondrial Protein Synthesis J
Published online 26 March 2012 Nucleic Acids Research, 2012, Vol. 40, No. 13 6109–6121 doi:10.1093/nar/gks266 Mitochondrial nucleoid interacting proteins support mitochondrial protein synthesis J. He1, H. M. Cooper1, A. Reyes1,M.DiRe1, H. Sembongi1, T. R. Litwin2, J. Gao1, K. C. Neuman2, I. M. Fearnley1, A. Spinazzola1, J. E. Walker1 and I. J. Holt1,* 1MRC-Mitochondrial Biology Unit, Wellcome Trust-MRC Building, Hills Road Cambridge, CB2 0XY, UK and 2Laboratory of Molecular Biophysics, NHLBI, National Institutes of Health, Bethesda, MD 20892, USA Received October 31, 2011; Revised March 6, 2012; Accepted March 10, 2012 ABSTRACT mitochondrial transcription factor A (3); ATAD3, a protein with displacement loop binding properties, which Mitochondrial ribosomes and translation factors has also been implicated in processes in mitochondria co-purify with mitochondrial nucleoids of human other than DNA metabolism (4); hydroxyacyl dehydro- cells, based on affinity protein purification of genase A; NIPSNAP1, a mitochondrial protein linked to tagged mitochondrial DNA binding proteins. amino acid metabolism, (5) and TUFM, the mitochon- Among the most frequently identified proteins drial translation elongation factor (6). More recently, we were ATAD3 and prohibitin, which have been identiﬁed proteins that are more tightly associated with identified previously as nucleoid components, mtDNA than TFAM, they included two cytoskeletal using a variety of methods. Both proteins are proteins, b-actin and non-muscle myosin IIA that contrib- demonstrated to be required for mitochondrial ute to mtDNA maintenance (7). Enriched mitochondrial protein synthesis in human cultured cells, and nucleoprotein preparations have been isolated independ- ently by immunocapture with antibodies to two known the major binding partner of ATAD3 is the mitochon- mtDNA binding proteins, SSBP1 or mitochondrial drial ribosome.
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Open Min-Joon-Upload-Final.Pdf
The Pennsylvania State University The Graduate School Eberly College of Science MAMMALIAN MITOCHONDRIAL RIBOSOMAL PROTEINS : A MATTER OF LIFE AND DEATH A Dissertation in Biochemistry, Microbiology and Molecular Biology by Min-Joon Han © 2010 Min-Joon Han Submitted in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy August 2010 The dissertation of Min-Joon Han was reviewed and approved* by the following: Emine C. Koc Assistant Professor of Biochemistry and Molecular Biology Dissertation Co-Advisor Co-Chair of Committee Hasan Koc Research Assistant Professor of Biochemistry and Molecular Biology Dissertation Co-Advisor Co-Chair of Committee Craig E. Cameron Paul Berg Professor of Biochemistry and Molecular Biology Wendy Hanna-Rose Associate Professor of Biochemistry and Molecular Biology Teh-hui Kao Professor of Biochemistry and Molecular Biology Seogchan Kang Professor of Plant pathology Scott B. Selleck Professor of Biochemistry and Molecular Biology Head of the Department of Biochemistry and Molecular Biology *Signatures are on file in the Graduate School ii ABSTRACT Human mitochondria are essential for cell survival while playing key roles in programmed cell death also called apoptosis. First of all, mitochondria are the main source of energy for the eukaryotic cell. Mitochondria produce more than 90% of the energy used by mammalian cells in a process referred to as oxidative phosphorylation. This demanding mechanism requires a lot of proteins, which are nucleus-encoded, synthesized in cytoplasm, and imported into mitochondria. However, it also requires 13 mitochondrial-encoded proteins. Mitochondria have their own 16.5 kb circular genome (mtDNA) and ribosome to translate these 13 proteins.
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OXA1L Mutations Cause Mitochondrial Encephalopathy and a Combined Oxidative Phosphorylation Defect
Research Article OXA1L mutations cause mitochondrial encephalopathy and a combined oxidative phosphorylation defect Kyle Thompson1, Nicole Mai1, Monika Oláhová1, Filippo Scialó2, Luke E Formosa3, David A Stroud4, Madeleine Garrett3, Nichola Z Lax1, Fiona M Robertson1, Cristina Jou5, Andres Nascimento6, Carlos Ortez6, Cecilia Jimenez-Mallebrera6, Steven A Hardy1, Langping He1, Garry K Brown7, Paula Marttinen8, Robert McFarland1 , Alberto Sanz2, Brendan J Battersby8 , Penelope E Bonnen9, Michael T Ryan3, Zofia MA Chrzanowska-Lightowlers1, Robert N Lightowlers1 & Robert W Taylor1,* Abstract Introduction OXA1, the mitochondrial member of the YidC/Alb3/Oxa1 membrane Mitochondrial disorders encompass a wide range of clinical pheno- protein insertase family, is required for the assembly of oxidative types and are genetically heterogeneous. Mitochondrial dysfunction phosphorylation complexes IV and V in yeast. However, depletion can arise from mutations in either the maternally inherited mito- of human OXA1 (OXA1L) was previously reported to impair assem- chondrial genome (mtDNA) or in nuclear genes that encode mito- bly of complexes I and V only. We report a patient presenting with chondrial proteins. The 13 mtDNA-encoded polypeptides are severe encephalopathy, hypotonia and developmental delay who essential components of the oxidative phosphorylation (OXPHOS) died at 5 years showing complex IV deficiency in skeletal muscle. system. Many nuclear genetic defects causing mitochondrial disease Whole exome sequencing identified biallelic OXA1L variants are in gene products required for maintaining correct expression of (c.500_507dup, p.(Ser170Glnfs*18) and c.620G>T, p.(Cys207Phe)) mtDNA. These include proteins involved in replication, mtDNA that segregated with disease. Patient muscle and fibroblasts maintenance, transcription, mtRNA processing, maturation and showed decreased OXA1L and subunits of complexes IV and V.
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Anti-MRPS26 Antibody (ARG59921)
Product datasheet [email protected] ARG59921 Package: 100 μl anti-MRPS26 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes MRPS26 Tested Reactivity Hu Tested Application WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name MRPS26 Antigen Species Human Immunogen Recombinant fusion protein corresponding to aa. 1-205 of Human MRPS26 (NP_110438.1). Conjugation Un-conjugated Alternate Names C20orf193; RPMS13; GI008; NY-BR-87; MRP-S13; MRP-S26; 28S ribosomal protein S26, mitochondrial; MRPS13; S13mt; S26mt; dJ534B8.3; 28S ribosomal protein S13, mitochondrial Application Instructions Application table Application Dilution WB 1:500 - 1:2000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control HeLa Calculated Mw 24 kDa Observed Size 24 kDa Properties Form Liquid Purification Affinity purified. Buffer PBS (pH 7.3), 0.02% Sodium azide and 50% Glycerol. Preservative 0.02% Sodium azide Stabilizer 50% Glycerol Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Gene Symbol MRPS26 Gene Full Name mitochondrial ribosomal protein S26 Background 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.
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