RFC5 Antibody Cat

Total Page：16

File Type：pdf, Size：1020Kb

RFC5 Antibody Cat. No.: 23-370 RFC5 Antibody Immunohistochemistry of paraffin-embedded human lung cancer using RFC5 antibody (23-370) at dilution of 1:100 (40x lens). Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human, Mouse, Rat Recombinant fusion protein containing a sequence corresponding to amino acids 181-340 IMMUNOGEN: of human RFC5 (NP_031396.1). TESTED APPLICATIONS: IHC, WB WB: ,1:500 - 1:2000 APPLICATIONS: IHC: ,1:50 - 1:200 POSITIVE CONTROL: 1) HeLa 2) U-251MG September 26, 2021 1 https://www.prosci-inc.com/rfc5-antibody-23-370.html 3) SKOV3 4) MCF-7 5) Mouse liver 6) Mouse spleen PREDICTED MOLECULAR Observed: 38kDa WEIGHT: Properties PURIFICATION: Affinity purification CLONALITY: Polyclonal ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: PBS with 0.02% sodium azide, 50% glycerol, pH7.3. STORAGE CONDITIONS: Store at -20˚C. Avoid freeze / thaw cycles. Additional Info OFFICIAL SYMBOL: RFC5 ALTERNATE NAMES: RFC5, MGC1155, RFC36 GENE ID: 5985 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References The elongation of primed DNA templates by DNA polymerase delta and DNA polymerase epsilon requires the accessory proteins proliferating cell nuclear antigen (PCNA) and replication factor C (RFC). RFC, also named activator 1, is a protein complex consisting of five distinct subunits of 140, 40, 38, 37, and 36 kD. This gene encodes the 36 kD subunit. BACKGROUND: This subunit can interact with the C-terminal region of PCNA. It forms a core complex with the 38 and 40 kDa subunits. The core complex possesses DNA-dependent ATPase activity, which was found to be stimulated by PCNA in an in vitro system. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome 9. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 26, 2021 2 https://www.prosci-inc.com/rfc5-antibody-23-370.html.

Copy Link

Recommended publications

Deregulated Gene Expression Pathways in Myelodysplastic Syndrome Hematopoietic Stem Cells
Leukemia (2010) 24, 756–764 & 2010 Macmillan Publishers Limited All rights reserved 0887-6924/10 $32.00 www.nature.com/leu ORIGINAL ARTICLE Deregulated gene expression pathways in myelodysplastic syndrome hematopoietic stem cells A Pellagatti1, M Cazzola2, A Giagounidis3, J Perry1, L Malcovati2, MG Della Porta2,MJa¨dersten4, S Killick5, A Verma6, CJ Norbury7, E Hellstro¨m-Lindberg4, JS Wainscoat1 and J Boultwood1 1LRF Molecular Haematology Unit, NDCLS, John Radcliffe Hospital, Oxford, UK; 2Department of Hematology Oncology, University of Pavia Medical School, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy; 3Medizinische Klinik II, St Johannes Hospital, Duisburg, Germany; 4Division of Hematology, Department of Medicine, Karolinska Institutet, Stockholm, Sweden; 5Department of Haematology, Royal Bournemouth Hospital, Bournemouth, UK; 6Albert Einstein College of Medicine, Bronx, NY, USA and 7Sir William Dunn School of Pathology, University of Oxford, Oxford, UK To gain insight into the molecular pathogenesis of the the World Health Organization.6,7 Patients with refractory myelodysplastic syndromes (MDS), we performed global gene anemia (RA) with or without ringed sideroblasts, according to expression profiling and pathway analysis on the hemato- poietic stem cells (HSC) of 183 MDS patients as compared with the the French–American–British classification, were subdivided HSC of 17 healthy controls. The most significantly deregulated based on the presence or absence of multilineage dysplasia. In pathways in MDS include interferon signaling, thrombopoietin addition, patients with RA with excess blasts (RAEB) were signaling and the Wnt pathways. Among the most signifi- subdivided into two categories, RAEB1 and RAEB2, based on the cantly deregulated gene pathways in early MDS are immuno- percentage of bone marrow blasts.
[Show full text]
Supplementary Table S1. Correlation Between the Mutant P53-Interacting Partners and PTTG3P, PTTG1 and PTTG2, Based on Data from Starbase V3.0 Database
Supplementary Table S1. Correlation between the mutant p53-interacting partners and PTTG3P, PTTG1 and PTTG2, based on data from StarBase v3.0 database. PTTG3P PTTG1 PTTG2 Gene ID Coefficient-R p-value Coefficient-R p-value Coefficient-R p-value NF-YA ENSG00000001167 −0.077 8.59e-2 −0.210 2.09e-6 −0.122 6.23e-3 NF-YB ENSG00000120837 0.176 7.12e-5 0.227 2.82e-7 0.094 3.59e-2 NF-YC ENSG00000066136 0.124 5.45e-3 0.124 5.40e-3 0.051 2.51e-1 Sp1 ENSG00000185591 −0.014 7.50e-1 −0.201 5.82e-6 −0.072 1.07e-1 Ets-1 ENSG00000134954 −0.096 3.14e-2 −0.257 4.83e-9 0.034 4.46e-1 VDR ENSG00000111424 −0.091 4.10e-2 −0.216 1.03e-6 0.014 7.48e-1 SREBP-2 ENSG00000198911 −0.064 1.53e-1 −0.147 9.27e-4 −0.073 1.01e-1 TopBP1 ENSG00000163781 0.067 1.36e-1 0.051 2.57e-1 −0.020 6.57e-1 Pin1 ENSG00000127445 0.250 1.40e-8 0.571 9.56e-45 0.187 2.52e-5 MRE11 ENSG00000020922 0.063 1.56e-1 −0.007 8.81e-1 −0.024 5.93e-1 PML ENSG00000140464 0.072 1.05e-1 0.217 9.36e-7 0.166 1.85e-4 p63 ENSG00000073282 −0.120 7.04e-3 −0.283 1.08e-10 −0.198 7.71e-6 p73 ENSG00000078900 0.104 2.03e-2 0.258 4.67e-9 0.097 3.02e-2 Supplementary Table S2.
[Show full text]
Early Growth Response 1 Regulates Hematopoietic Support and Proliferation in Human Primary Bone Marrow Stromal Cells
Hematopoiesis SUPPLEMENTARY APPENDIX Early growth response 1 regulates hematopoietic support and proliferation in human primary bone marrow stromal cells Hongzhe Li, 1,2 Hooi-Ching Lim, 1,2 Dimitra Zacharaki, 1,2 Xiaojie Xian, 2,3 Keane J.G. Kenswil, 4 Sandro Bräunig, 1,2 Marc H.G.P. Raaijmakers, 4 Niels-Bjarne Woods, 2,3 Jenny Hansson, 1,2 and Stefan Scheding 1,2,5 1Division of Molecular Hematology, Department of Laboratory Medicine, Lund University, Lund, Sweden; 2Lund Stem Cell Center, Depart - ment of Laboratory Medicine, Lund University, Lund, Sweden; 3Division of Molecular Medicine and Gene Therapy, Department of Labora - tory Medicine, Lund University, Lund, Sweden; 4Department of Hematology, Erasmus MC Cancer Institute, Rotterdam, the Netherlands and 5Department of Hematology, Skåne University Hospital Lund, Skåne, Sweden ©2020 Ferrata Storti Foundation. This is an open-access paper. doi:10.3324/haematol. 2019.216648 Received: January 14, 2019. Accepted: July 19, 2019. Pre-published: August 1, 2019. Correspondence: STEFAN SCHEDING - [email protected] Li et al.: Supplemental data 1. Supplemental Materials and Methods BM-MNC isolation Bone marrow mononuclear cells (BM-MNC) from BM aspiration samples were isolated by density gradient centrifugation (LSM 1077 Lymphocyte, PAA, Pasching, Austria) either with or without prior incubation with RosetteSep Human Mesenchymal Stem Cell Enrichment Cocktail (STEMCELL Technologies, Vancouver, Canada) for lineage depletion (CD3, CD14, CD19, CD38, CD66b, glycophorin A). BM-MNCs from fetal long bones and adult hip bones were isolated as reported previously 1 by gently crushing bones (femora, tibiae, fibulae, humeri, radii and ulna) in PBS+0.5% FCS subsequent passing of the cell suspension through a 40-µm filter.
[Show full text]
RFC5 Antibody (F54778)
RFC5 Antibody (F54778) Catalog No. Formulation Size F54778-0.4ML In 1X PBS, pH 7.4, with 0.09% sodium azide 0.4 ml F54778-0.08ML 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 Format Purified Clonality Polyclonal (rabbit origin) Isotype Rabbit Ig Purity Purified UniProt P40937 Applications Flow cytometry : 1:25 (1x10e6 cells) Western blot : 1:500-1:2000 Limitations This RFC5 antibody is available for research use only. Western blot testing of 1) non-transfected and 2) transfected 293 cell lysate with RFC5 antibody. Western blot testing of human HeLa cell lysate with RFC5 antibody. Predicted molecular weight ~38 kDa. Flow cytometry testing of human HeLa cells with RFC5 antibody; Blue=isotype control, Green= RFC5 antibody. Description The elongation of primed DNA templates by DNA polymerase delta and DNA polymerase epsilon requires the accessory proteins proliferating cell nuclear antigen (PCNA) and replication factor C (RFC). RFC, also named activator 1, is a protein complex consisting of five distinct subunits of 140, 40, 38, 37, and 36 kD. RFC5 is the 36 kD subunit. This subunit can interact with the C-terminal region of PCNA. It forms a core complex with the 38 and 40 kDa subunits. The core complex possesses DNA-dependent ATPase activity, which was found to be stimulated by PCNA in an in vitro system. Application Notes The stated application concentrations are suggested starting points. Titration of the RFC5 antibody may be required due to differences in protocols and secondary/substrate sensitivity.
[Show full text]
The Synthetic Genetic Interaction Spectrum of Essential Genes
LETTERS The synthetic genetic interaction spectrum of essential genes Armaity P Davierwala1, Jennifer Haynes2, Zhijian Li1,2, Reneé L Brost1, Mark D Robinson1, Lisa Yu3, Sanie Mnaimneh1, Huiming Ding1, Hongwei Zhu1, Yiqun Chen1, Xin Cheng1, Grant W Brown3, Charles Boone1,2,4, Brenda J Andrews1,2,4 & Timothy R Hughes1,2,4 The nature of synthetic genetic interactions involving essential mapping these genetic interactions2,3. Essential gene function is also genes (those required for viability) has not been previously buffered by both nonessential and other essential genes because hypomorphic (partially functional) alleles of essential genes often http://www.nature.com/naturegenetics examined in a broad and unbiased manner. We crossed yeast strains carrying promoter-replacement alleles for more than have synthetic lethal interactions with deletion alleles of nonessential half of all essential yeast genes1 to a panel of 30 different genes and hypomorphic alleles of other essential genes2,3,7.Genetic mutants with defects in diverse cellular processes. The resulting interactions among essential genes have not been examined system- genetic network is biased toward interactions between atically and objectively because of the inherent difficulty in creating functionally related genes, enabling identification of a and working with hypomorphic alleles. previously uncharacterized essential gene (PGA1) required for specific functions of the endoplasmic reticulum. But there are also many interactions between genes with dissimilar functions, Query gene (crossed to array) Gene Ontology labels (array strains) suggesting that individual essential genes are required for buffering many cellular processes. The most notable feature of the essential synthetic genetic network is that it has an interaction density five times that of nonessential synthetic 2005 Nature Publishing Group Group 2005 Nature Publishing genetic networks2,3, indicating that most yeast genetic © -linked glycosylation -linked interactions involve at least one essential gene.
[Show full text]
Coordinated Regulation of Heterochromatin Inheritance by Dpb3–Dpb4 Complex
Coordinated regulation of heterochromatin inheritance by Dpb3–Dpb4 complex Haijin Hea,1, Yang Lib,c,1, Qianhua Donga,1, An-Yun Changd,e, Feng Gaob, Zhongxuan Chia, Min Sub, Faben Zhangb,c, Hyoju Bana, Rob Martienssend, Yu-hang Chenb,c,2, and Fei Lia,2 aDepartment of Biology, New York University, New York, NY 10003-6688; bState Key Laboratory of Molecular Developmental Biology, Chinese Academy of Sciences Center for Excellence in Biomacromolecules, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China; cCollege of Life Sciences, University of Chinese Academy of Sciences, Beijing 100049, China; dHoward Hughes Medical Institute, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724; and eMolecular and Cellular Biology Program, Stony Brook University, Stony Brook, NY 11794 Edited by Jasper Rine, University of California, Berkeley, CA, and approved October 6, 2017 (received for review July 25, 2017) During DNA replication, chromatin is disrupted ahead of the replica- H3K9 methylation in fission yeast is mediated by the CLCR com- tion fork, and epigenetic information must be restored behind the plex, which contains the H3K9 methyltransferase Clr4/Suv39 and the fork. How epigenetic marks are inherited through DNA replication silencing proteins Rik1, Dos1/Raf1, Dos2/Raf2, and Cul4 (8–12). remains poorly understood. Histone H3 lysine 9 (H3K9) methylation RNA interference (RNAi) plays an important role in H3K9 meth- and histone hypoacetylation are conserved hallmarks of heterochro- ylation and heterochromatin silencing (13). During replication, matin. We previously showed that the inheritance of H3K9 methyl- Cdc20/Pol2, the DNA polymerase (Pol) epsilon catalytic subunit, ation during DNA replication depends on the catalytic subunit of DNA interacts with the CLRC complex.
[Show full text]
Investigation of Crucial Genes and Micrornas in Conventional Osteosarcoma Using Gene Expression Profiling Analysis
MOLECULAR MEDICINE REPORTS 16: 7617-7624, 2017 Investigation of crucial genes and microRNAs in conventional osteosarcoma using gene expression profiling analysis CHUANGANG PENG1, QI YANG2, BO WEI3, BAOMING YUAN1, YONG LIU4, YUXIANG LI4, DAWER GU4, GUOCHAO YIN4, BO WANG4, DEHUI XU4, XUEBING ZHANG4 and DALIANG KONG5 1Orthopaedic Medical Center, The 2nd Hospital of Jilin University, Changchun, Jilin 130041; Departments of 2Gynecology and Obstetrics and 3Neurosurgery, China-Japan Union Hospital of Jilin University, Changchun, Jilin 130033; 4Department of Orthopaedics, Jilin Oilfield General Hospital, Songyuan, Jilin 131200;5 Department of Orthopaedics, China-Japan Union Hospital of Jilin University, Changchun, Jilin 130033, P.R. China Received November 23, 2016; Accepted July 3, 2017 DOI: 10.3892/mmr.2017.7506 Abstract. The present study aimed to screen potential genes targeted by miRNA (miR)-802, miR-224-3p and miR-522-3p. associated with conventional osteosarcoma (OS) and obtain The DEGs encoding RFC may be important for the develop- further information on the pathogenesis of this disease. The ment of conventional OS, and their expression may be regulated microarray dataset GSE14359 was downloaded from the Gene by a number of miRNAs, including miR-802, miR-224-3p and Expression Omnibus. A total of 10 conventional OS samples miR-522-3p. and two non-neoplastic primary osteoblast samples in the dataset were selected to identify the differentially expressed Introduction genes (DEGs) using the Linear Models for Microarray Data package. The potential functions of the DEGs were predicted Osteosarcoma (OS) is the most common malignancy of bone in using Gene Ontology (GO) and pathway enrichment analyses. early adolescence (1).
[Show full text]
Control of Genome Integrity by RFC Complexes; Conductors of PCNA Loading Onto and Unloading from Chromatin During DNA Replication
Review Control of Genome Integrity by RFC Complexes; Conductors of PCNA Loading onto and Unloading from Chromatin during DNA Replication Yasushi Shiomi *and Hideo Nishitani * Graduate School of Life Science, University of Hyogo, Kamigori, Ako‐gun, Hyogo 678‐1297, Japan Correspondence: [email protected]‐hyogo.ac.jp (Y.S.); [email protected]‐hyogo.ac.jp (H.N.) Academic Editor: Eishi Noguchi Received: 28 November 2016; Accepted: 21 January 2017; Published: 26 January 2017 Abstract: During cell division, genome integrity is maintained by faithful DNA replication during S phase, followed by accurate segregation in mitosis. Many DNA metabolic events linked with DNA replication are also regulated throughout the cell cycle. In eukaryotes, the DNA sliding clamp, proliferating cell nuclear antigen (PCNA), acts on chromatin as a processivity factor for DNA polymerases. Since its discovery, many other PCNA binding partners have been identified that function during DNA replication, repair, recombination, chromatin remodeling, cohesion, and proteolysis in cell‐cycle progression. PCNA not only recruits the proteins involved in such events, but it also actively controls their function as chromatin assembles. Therefore, control of PCNA‐loading onto chromatin is fundamental for various replication‐coupled reactions. PCNA is loaded onto chromatin by PCNA‐loading replication factor C (RFC) complexes. Both RFC1‐RFC and Ctf18‐RFC fundamentally function as PCNA loaders. On the other hand, after DNA synthesis, PCNA must be removed from chromatin by Elg1‐RFC. Functional defects in RFC complexes lead to chromosomal abnormalities. In this review, we summarize the structural and functional relationships among RFC complexes, and describe how the regulation of PCNA loading/unloading by RFC complexes contributes to maintaining genome integrity.
[Show full text]
Transcriptome Analysis of Differentially Expressed Mrna Related to Pigeon Muscle Development
animals Article Transcriptome Analysis of Differentially Expressed mRNA Related to Pigeon Muscle Development Hao Ding 1,2,† , Yueyue Lin 1,2,†, Tao Zhang 1,2,* , Lan Chen 1,2, Genxi Zhang 1,2, Jinyu Wang 1,2, Kaizhou Xie 1,2 and Guojun Dai 1,2 1 College of Animal Science and Technology, Yangzhou University, Yangzhou 225000, China; [email protected] (H.D.); [email protected] (Y.L.); [email protected] (L.C.); [email protected] (G.Z.); [email protected] (J.W.); [email protected] (K.X.); [email protected] (G.D.) 2 Joint International Research Laboratory of Agriculture and Agri−Product Safety, Ministry of Education, Yangzhou University, Yangzhou 225000, China * Correspondence: [email protected] † These authors are contributed equally to this study. Simple Summary: The growth and development of skeletal muscle determine the meat production performance of pigeons and are regulated by complex gene networks. To explore the genes involved in regulating the growth and development of pigeon skeletal muscle, RNA sequencing (RNA−seq) was used to characterise gene expression proﬁles during the development and growth of pigeon breast muscle and identify differentially expressed genes (DEGs) among different stages. This study expanded the diversity of pigeon mRNA, and it was helpful to understand the role of mRNA in pigeon muscle development and growth. Abstract: The mechanisms behind the gene expression and regulation that modulate the development and growth of pigeon skeletal muscle remain largely unknown. In this study, we performed gene Citation: Ding, H.; Lin, Y.; Zhang, T.; expression analysis on skeletal muscle samples at different developmental and growth stages using Chen, L.; Zhang, G.; Wang, J.; Xie, K.; RNA sequencing (RNA−Seq).
[Show full text]
Identification of the Fifth Subunit of Saccharomyces Cerevisiae Replication Factor C Sonja L
4986-4991 Nucleic Acids Research, 1995, Vol. 23, No. 24 Q--::;/l 1995 Oxford University Press Identification of the fifth subunit of Saccharomyces cerevisiae Replication Factor C Sonja L. Gary and Peter M. J. Burgers* Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid, St Louis, MO 63110, USA Received October 3, 1995; Revised and Accepted October 26, 1995 ABSTRACT cloned using a combination of peptide sequence analysis and homology-based PCR (16-19). However, it is not yet known Yeast replication factor C (RF-C) is a multipolypeptide whether these five polypeptides are sufficient to reconstitute the complex required for chromosomal DNA replication. human RF-C complex. Previously the complex from yeast Previously this complex was known to consist of at (yRF-C) was known to contain at least four subunits of 100, 41, least four subunits. We here report the identification of 40 and 37 kDa (6,13,20). The small subunits of yeast and human a fifth RF-C subunit from Saccharomyces cerevisiae, RF-C show high sequence similarity, both among themselves and encoded by the RFC5 (YBRO810) gene. This subunit between species. With the exception of the 38 kDa subunit, each exhibits highest homology to the 38 kDa subunit (38%) human RF-C subunit appears to have a yeast homolog with which of human RF-C (activator 1). Like the other four RFC it shares particular homology. genes, the RFC5 gene Is essential for yeast viability, In this paper we describe the identification of a fifth RF-C indicating an essential function for each subunit.
[Show full text]
RFC5 (F-9): Sc-376528
SAN TA C RUZ BI OTEC HNOL OG Y, INC . RFC5 (F-9): sc-376528 BACKGROUND APPLICATIONS Replication factor C (RFC) is an essential DNA polymerase accessory protein RFC5 (F-9) is recommended for detection of RFC5 of mouse, rat and human that is required for numerous aspects of DNA metabolism including DNA origin by Western Blotting (starting dilution 1:100, dilution range 1:100- replication, DNA repair, and telomere metabolism. RFC is a heteropentameric 1:1000), immunoprecipitation [1-2 µg per 100-500 µg of total protein (1 ml complex that recognizes a primer on a template DNA, binds to a primer termi - of cell lysate)], immunofluorescence (starting dilution 1:50, dilution range nus, and loads proliferating cell nuclear antigen (PCNA) onto DNA at primer- 1:50-1:500) and solid phase ELISA (starting dilution 1:30, dilution range template junctions in an ATP-dependent reaction. All five of the RFC subunits 1:30- 1:3000). share a set of related sequences (RFC boxes) that include nucleotide-binding Suitable for use as control antibody for RFC5 siRNA (h): sc-37637, RFC5 consensus sequences. Four of the five RFC genes (RFC1, RFC2, RFC3, and siRNA (m): sc-37638, RFC5 shRNA Plasmid (h): sc-37637-SH, RFC5 shRNA RFC4) have consensus ATP-binding motifs. The small RFC proteins, RFC2, Plasmid (m): sc-37638-SH, RFC5 shRNA (h) Lentiviral Particles: sc-37637-V RFC3, RFC4 and RFC5, interact with Rad24, whereas the RFC1 subunit does and RFC5 shRNA (m) Lentiviral Particles: sc-37638-V. not. The human RFC5 gene maps to chromosome 12q24.23 and encodes the RFC5 subunit.
[Show full text]
Renoprotective Effect of Combined Inhibition of Angiotensin-Converting Enzyme and Histone Deacetylase
BASIC RESEARCH www.jasn.org Renoprotective Effect of Combined Inhibition of Angiotensin-Converting Enzyme and Histone Deacetylase † ‡ Yifei Zhong,* Edward Y. Chen, § Ruijie Liu,*¶ Peter Y. Chuang,* Sandeep K. Mallipattu,* ‡ ‡ † | ‡ Christopher M. Tan, § Neil R. Clark, § Yueyi Deng, Paul E. Klotman, Avi Ma’ayan, § and ‡ John Cijiang He* ¶ *Department of Medicine, Mount Sinai School of Medicine, New York, New York; †Department of Nephrology, Longhua Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, China; ‡Department of Pharmacology and Systems Therapeutics and §Systems Biology Center New York, Mount Sinai School of Medicine, New York, New York; |Baylor College of Medicine, Houston, Texas; and ¶Renal Section, James J. Peters Veterans Affairs Medical Center, New York, New York ABSTRACT The Connectivity Map database contains microarray signatures of gene expression derived from approximately 6000 experiments that examined the effects of approximately 1300 single drugs on several human cancer cell lines. We used these data to prioritize pairs of drugs expected to reverse the changes in gene expression observed in the kidneys of a mouse model of HIV-associated nephropathy (Tg26 mice). We predicted that the combination of an angiotensin-converting enzyme (ACE) inhibitor and a histone deacetylase inhibitor would maximally reverse the disease-associated expression of genes in the kidneys of these mice. Testing the combination of these inhibitors in Tg26 mice revealed an additive renoprotective effect, as suggested by reduction of proteinuria, improvement of renal function, and attenuation of kidney injury. Furthermore, we observed the predicted treatment-associated changes in the expression of selected genes and pathway components. In summary, these data suggest that the combination of an ACE inhibitor and a histone deacetylase inhibitor could have therapeutic potential for various kidney diseases.
[Show full text]