TRIM55 Antibody Cat

Total Page：16

File Type：pdf, Size：1020Kb

TRIM55 Antibody Cat. No.: 25-867 TRIM55 Antibody Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human, Mouse, Rat Antibody produced in rabbits immunized with a synthetic peptide corresponding a region IMMUNOGEN: of human TRIM55. TESTED APPLICATIONS: ELISA, WB TRIM55 antibody can be used for detection of TRIM55 by ELISA at 1:62500. TRIM55 APPLICATIONS: antibody can be used for detection of TRIM55 by western blot at 1 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 - 100,000. POSITIVE CONTROL: 1) Cat. No. 1201 - HeLa Cell Lysate PREDICTED MOLECULAR 27 kDa WEIGHT: Properties PURIFICATION: Antibody is purified by peptide affinity chromatography method. CLONALITY: Polyclonal CONJUGATE: Unconjugated PHYSICAL STATE: Liquid September 28, 2021 1 https://www.prosci-inc.com/trim55-antibody-25-867.html Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% BUFFER: sucrose. CONCENTRATION: batch dependent For short periods of storage (days) store at 4˚C. For longer periods of storage, store STORAGE CONDITIONS: TRIM55 antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles. Additional Info OFFICIAL SYMBOL: TRIM55 ALTERNATE NAMES: TRIM55, MURF-2, RNF29, muRF2 ACCESSION NO.: NP_908975 PROTEIN GI NO.: 34878852 GENE ID: 84675 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References TRIM55 contains a RING zinc finger, a motif known to be involved in protein-protein interactions. This protein associates transiently with microtubules, myosin, and titin during muscle sarcomere assembly. It may act as a transient adaptor and plays a regulatory role in the assembly of sarcomeres.The protein encoded by this gene contains BACKGROUND: a RING zinc finger, a motif known to be involved in protein-protein interactions. This protein associates transiently with microtubules, myosin, and titin during muscle sarcomere assembly. It may act as a transient adaptor and plays a regulatory role in the assembly of sarcomeres. Four alternatively spliced transcript variants encoding distinct isoforms have been described. REFERENCES: 1) Lange, S., (2005) Science 308 (5728), 1599-1603. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 28, 2021 2 https://www.prosci-inc.com/trim55-antibody-25-867.html.

Copy Link

Recommended publications

Integrating Single-Step GWAS and Bipartite Networks Reconstruction Provides Novel Insights Into Yearling Weight and Carcass Traits in Hanwoo Beef Cattle
animals Article Integrating Single-Step GWAS and Bipartite Networks Reconstruction Provides Novel Insights into Yearling Weight and Carcass Traits in Hanwoo Beef Cattle Masoumeh Naserkheil 1 , Abolfazl Bahrami 1 , Deukhwan Lee 2,* and Hossein Mehrban 3 1 Department of Animal Science, University College of Agriculture and Natural Resources, University of Tehran, Karaj 77871-31587, Iran; [email protected] (M.N.); [email protected] (A.B.) 2 Department of Animal Life and Environment Sciences, Hankyong National University, Jungang-ro 327, Anseong-si, Gyeonggi-do 17579, Korea 3 Department of Animal Science, Shahrekord University, Shahrekord 88186-34141, Iran; [email protected] * Correspondence: [email protected]; Tel.: +82-31-670-5091 Received: 25 August 2020; Accepted: 6 October 2020; Published: 9 October 2020 Simple Summary: Hanwoo is an indigenous cattle breed in Korea and popular for meat production owing to its rapid growth and high-quality meat. Its yearling weight and carcass traits (backfat thickness, carcass weight, eye muscle area, and marbling score) are economically important for the selection of young and proven bulls. In recent decades, the advent of high throughput genotyping technologies has made it possible to perform genome-wide association studies (GWAS) for the detection of genomic regions associated with traits of economic interest in diﬀerent species. In this study, we conducted a weighted single-step genome-wide association study which combines all genotypes, phenotypes and pedigree data in one step (ssGBLUP). It allows for the use of all SNPs simultaneously along with all phenotypes from genotyped and ungenotyped animals. Our results revealed 33 relevant genomic regions related to the traits of interest.
[Show full text]
Genetically Modified Mouse Models to Help Fight COVID-19
PERSPECTIVE https://doi.org/10.1038/s41596-020-00403-2 Genetically modified mouse models to help fight COVID-19 1,2✉ 2 3 Channabasavaiah B. Gurumurthy , Rolen M. Quadros , Guy P. Richardson✉ , Larisa Y. Poluektova 1, Suzanne L. Mansour4 and Masato Ohtsuka 5,6 The research community is in a race to understand the molecular mechanisms of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection, to repurpose currently available antiviral drugs and to develop new therapies and vaccines against coronavirus disease 2019 (COVID-19). One major challenge in achieving these goals is the paucity of suitable preclinical animal models. Mice constitute ~70% of all the laboratory animal species used in biomedical research. Unfortunately, SARS-CoV-2 infects mice only if they have been genetically modified to express human ACE2. The inherent resistance of wild-type mice to SARS-CoV-2, combined with a wealth of genetic tools that are available only for modifying mice, offers a unique opportunity to create a versatile set of genetically engineered mouse models useful for COVID-19 research. We propose three broad categories of these models and more than two dozen designs that may be useful for SARS-CoV-2 research and for fighting COVID-19. 1234567890():,; 1234567890():,; – he research community is in desperate need of animal in SARS virus studies4 7. Like SARS-CoV, SARS-CoV-2 uses Tmodels for testing therapeutics and vaccines against the hACE2 receptor for entry into cells. Therefore some of coronavirus disease 2019 (COVID-19), and for studies these transgenic models have been investigated for their suit- aimed at understanding the molecular mechanisms of severe ability for SARS-CoV-2 studies8,9.
[Show full text]
The Role of Transcriptional Factor D-Site-Binding Protein in Circadian CCL2 Gene Expression in Anti-Thy1 Nephritis
Cellular & Molecular Immunology www.nature.com/cmi ARTICLE The role of transcriptional factor D-site-binding protein in circadian CCL2 gene expression in anti-Thy1 nephritis Yang Lu1, Yan Mei1, Lei Chen1, Lingling Wu1, Xu Wang1, Yingjie Zhang1,BoFu1, Xizhao Chen1, Yuansheng Xie1, Guangyan Cai1, Xueyuan Bai1, Qinggang Li1 and Xiangmei Chen1 Mesangial proliferative glomerulonephritis (MsPGN) is an inflammatory disease, but both the nature of disease progression and its regulation remain unclear. In the present study, we monitored the course of anti-Thy1 nephritis from days 1 to 5 and established gene expression profiles at each time point using microarrays to explore the development of inflammation. According to the gene expression profiles, macrophage infiltration (triggered by CCL2 activation) was evident on day 1 and enhanced inflammation over the next few days. We screened for genes with expression levels similar to CCL2 and found that the upregulation of the circadian gene albumin D-site-binding protein (DBP) was involved in CCL2 activation in mesangial cells. More importantly, CCL2 expression showed oscillatory changes similar to DBP, and DBP induced peak CCL2 expression at 16:00 a clock on day 1 in the anti-Thy1 nephritis model. We knocked down DBP through transfection with a small interfering RNA (siRNA) and used RNA sequencing to identify the DBP-regulated TNF-α-CCL2 pathway. We performed chromatin immunoprecipitation sequencing (ChIP-Seq) and the dual luciferase assay to show that DBP bound to the TRIM55 promoter, regulating gene expression and in turn controlling the TNF-α-CCL2 pathway. In conclusion, DBP-regulated circadian CCL2 expression by the TRIM55-TNF pathway in injured mesangial cells at an early stage, which promoted macrophage recruitment and in turn triggered infiltration and inflammation in a model of anti-Thy1 nephritis.
[Show full text]
Gene Expression Profiles of Ductal Versus Acinar Adenocarcinoma of the Prostate
Modern Pathology (2009) 22, 1273–1279 & 2009 USCAP, Inc. All rights reserved 0893-3952/09 $32.00 1273 Gene expression profiles of ductal versus acinar adenocarcinoma of the prostate Souzan Sanati1, Mark A Watson2, Andrea L Salavaggione2 and Peter A Humphrey1 1Department of Pathology and Immunology, Division of Anatomic and Molecular Pathology, Washington University School of Medicine, St Louis, MO, USA and 2Department of Pathology and Immunology, Division of Laboratory and Genomic Medicine, Washington University School of Medicine, St Louis, MO, USA Ductal adenocarcinoma is an uncommon variant of prostatic adenocarcinoma with a generally more aggressive clinical course than usual acinar adenocarcinoma. However, the molecular distinction between ductal and acinar adenocarcinomas is not well characterized. The aim of this investigation was to evaluate the relatedness of ductal versus acinar prostatic adenocarcinoma by comparative gene expression profiling. Archived, de- identified, snap frozen tumor tissue from 5 ductal adenocarcinomas, 3 mixed ductal–acinar adenocarcinomas, and 11 acinar adenocarcinomas cases were analyzed. All cases of acinar and ductal adenocarcinomas were matched by Gleason grade. RNA from whole tissue sections of the 5 ductal and 11 acinar adenocarcinomas cases were subjected to gene expression profiling on Affymetrix U133Plus2 microarrays. Independently, laser- capture microdissection was also performed on the three mixed ductal–acinar cases and five pure acinar cases to isolate homogeneous populations of ductal and acinar carcinoma cells from the same tumor. Seven of these laser-capture microdissected samples (three ductal and four acinar cell populations) were similarly analyzed on U133Plus2 arrays. Analysis of data from whole sections of ductal and acinar carcinomas identified only 25 gene transcripts whose expression was significantly and at least two-fold different between ductal and acinar adenocarcinomas.
[Show full text]
Investigating Host Genes Involved In. HIY Control by a Novel Computational Method to Combine GWAS with Eqtl
Investigating Host Genes Involved in. HIY Control by a Novel Computational Method to Combine GWAS with eQTL by Yi Song THESIS Submitted In partial satisfaction of me teqoitements for the degree of MASTER OF SCIENCE In Biological and Medical Informatics In the GRADUATE DIVISION Copyright (2012) by Yi Song ii Acknowledgement First and foremost, I would like to thank my advisor Professor Hao Li, without whom this thesis would not have been possible. I am very grateful that Professor Li lead me into the field of human genomics and gave me the opportunity to pursue this interesting study in his laboratory. Besides the wealth of knowledge and invaluable insights that he offered in every meeting we had, Professor Li is one of the most approachable faculties I have met. I truly appreciate his patient guidance and his enthusiastic supervision throughout my master’s career. I am sincerely thankful to Professor Patricia Babbitt, the Associate Director of the Biomedical Informatics program at UCSF. Over my two years at UCSF, she has always been there to offer her help when I was faced with difficulties. I would also like to thank both Professor Babbitt and Professor Nevan Krogan for investing their valuable time in evaluating my work. I take immense pleasure in thanking my co-workers Dr. Xin He and Christopher Fuller. It has been a true enjoyment to discuss science with Dr. He, whose enthusiasm is a great inspiration to me. I also appreciate his careful editing of my thesis. Christopher Fuller, a PhD candidate in the Biomedical Informatics program, has provided great help for me on technical problems.
[Show full text]
TRIM55 Purified Maxpab Rabbit Polyclonal Antibody (D01P)
TRIM55 purified MaxPab rabbit polyclonal antibody (D01P) Catalog # : H00084675-D01P 規格 : [ 100 ug ] List All Specification Application Image Product Rabbit polyclonal antibody raised against a full-length human TRIM55 Western Blot (Tissue lysate) Description: protein. Immunogen: TRIM55 (NP_908974.1, 1 a.a. ~ 452 a.a) full-length human protein. Sequence: MSASLNYKSFSKEQQTMDNLEKQLICPICLEMFTKPVVILPCQHNLCRKC ASDIFQASNPYLPTRGGTTMASGGRFRCPSCRHEVVLDRHGVYGLQRN enlarge LLVENIIDIYKQESTRPEKKSDQPMCEEHEEERINIYCLNCEVPTCSLCKVF GAHKDCQVAPLTHVFQRQKSELSDGIAILVGSNDRVQGVISQLEDTCKTI Western Blot (Transfected EECCRKQKQELCEKFDYLYGILEERKNEMTQVITRTQEEKLEHVRALIKK lysate) YSDHLENVSKLVESGIQFMDEPEMAVFLQNAKTLLKKISEASKAFQMEKIE HGYENMNHFTVNLNREEKIIREIDFYREDEDEEEEEGGEGEKEGEGEVG GEAVEVEEVENVQTEFPGEDENPEKASELSQVELQAAPGALPVSSPEPP PALPPAADAPVTQIGFEAPPLQGQAAAPASGSGADSEPARHIFSFSWLN SLNE Host: Rabbit enlarge Reactivity: Human, Mouse Quality Control Antibody reactive against mammalian transfected lysate. Testing: Storage Buffer: In 1x PBS, pH 7.4 Storage Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. Instruction: MSDS: Download Datasheet: Download Applications Western Blot (Tissue lysate) TRIM55 MaxPab rabbit polyclonal antibody. Western Blot analysis of TRIM55 expression in mouse kidney. Protocol Download Western Blot (Transfected lysate) Page 1 of 2 2020/7/15 Western Blot analysis of TRIM55 expression in transfected 293T cell line (H00084675-T02) by TRIM55 MaxPab polyclonal antibody. Lane 1: TRIM55 transfected lysate(50.80 KDa). Lane 2: Non-transfected
[Show full text]
Barkbase: Epigenomic Annotation of Canine Genomes
G C A T T A C G G C A T genes Article BarkBase: Epigenomic Annotation of Canine Genomes Kate Megquier 1, Diane P. Genereux 1 , Jessica Hekman 1 , Ross Swofford 1, Jason Turner-Maier 1, Jeremy Johnson 1, Jacob Alonso 1, Xue Li 1,2, Kathleen Morrill 1,2, Lynne J. Anguish 3, Michele Koltookian 1, Brittney Logan 2, Claire R. Sharp 4 , Lluis Ferrer 5, Kerstin Lindblad-Toh 1,6, Vicki N. Meyers-Wallen 7, Andrew Hoffman 8,9 and Elinor K. Karlsson 1,2,10,* 1 Vertebrate Genomics, Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA; [email protected] (K.M.); [email protected] (D.P.G.); [email protected] (J.H.); swoff[email protected] (R.S.); [email protected] (J.T.-M.); [email protected] (J.J.); [email protected] (J.A.); [email protected] (X.L.); [email protected] (K.M.); [email protected] (M.K.); [email protected] (K.L.-T.) 2 Bioinformatics and Integrative Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA; [email protected] 3 Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA; [email protected] 4 School of Veterinary and Life Sciences, College of Veterinary Medicine, Murdoch University, Perth, Murdoch, WA 6150, Australia; [email protected] 5 Departament de Medicina i Cirurgia Animals Veterinary School, Universitat Autonoma de Barcelona, 08193 Barcelona, Spain; [email protected] 6 Science for Life Laboratory, Department of Medical Biochemistry &
[Show full text]
Anti-TRIM55 / MURF2 Antibody (ARG40365)
Product datasheet [email protected] ARG40365 Package: 100 μl anti-TRIM55 / MURF2 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes TRIM55 / MURF2 Tested Reactivity Hu Tested Application WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name TRIM55 / MURF2 Antigen Species Human Immunogen KLH-conjugated synthetic peptide between aa. 295-329 of Human TRIM55. Conjugation Un-conjugated Alternate Names Muscle-specific RING finger protein 2; muRF2; MuRF-2; MURF-2; RNF29; MuRF2; RING finger protein 29; Tripartite motif-containing protein 55 Application Instructions Application table Application Dilution WB 1:2000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control Human liver Calculated Mw 60 kDa Observed Size ~ 65 kDa Properties Form Liquid Purification Purification with Protein A and immunogen peptide. Buffer PBS and 0.09% (W/V) Sodium azide. Preservative 0.09% (W/V) Sodium azide. 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 or below. 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 TRIM55 Gene Full Name tripartite motif containing 55 Background The protein encoded by this gene contains a RING zinc finger, a motif known to be involved in protein- protein interactions.
[Show full text]
Novel and Highly Recurrent Chromosomal Alterations in Se´Zary Syndrome
Research Article Novel and Highly Recurrent Chromosomal Alterations in Se´zary Syndrome Maarten H. Vermeer,1 Remco van Doorn,1 Remco Dijkman,1 Xin Mao,3 Sean Whittaker,3 Pieter C. van Voorst Vader,4 Marie-Jeanne P. Gerritsen,5 Marie-Louise Geerts,6 Sylke Gellrich,7 Ola So¨derberg,8 Karl-Johan Leuchowius,8 Ulf Landegren,8 Jacoba J. Out-Luiting,1 Jeroen Knijnenburg,2 Marije IJszenga,2 Karoly Szuhai,2 Rein Willemze,1 and Cornelis P. Tensen1 Departments of 1Dermatology and 2Molecular Cell Biology, Leiden University Medical Center, Leiden, the Netherlands; 3Department of Dermatology, St Thomas’ Hospital, King’s College, London, United Kingdom; 4Department of Dermatology, University Medical Center Groningen, Groningen, the Netherlands; 5Department of Dermatology, Radboud University Nijmegen Medical Center, Nijmegen, the Netherlands; 6Department of Dermatology, Gent University Hospital, Gent, Belgium; 7Department of Dermatology, Charite, Berlin, Germany; and 8Department of Genetics and Pathology, Rudbeck Laboratory, University of Uppsala, Uppsala, Sweden Abstract Introduction This study was designed to identify highly recurrent genetic Se´zary syndrome (Sz) is an aggressive type of cutaneous T-cell alterations typical of Se´zary syndrome (Sz), an aggressive lymphoma/leukemia of skin-homing, CD4+ memory T cells and is cutaneous T-cell lymphoma/leukemia, possibly revealing characterized by erythroderma, generalized lymphadenopathy, and pathogenetic mechanisms and novel therapeutic targets. the presence of neoplastic T cells (Se´zary cells) in the skin, lymph High-resolution array-based comparative genomic hybridiza- nodes, and peripheral blood (1). Sz has a poor prognosis, with a tion was done on malignant T cells from 20 patients. disease-specific 5-year survival of f24% (1).
[Show full text]
Muscle Ring Finger-3 Protects Against Diabetic Cardiomyopathy Induced by a High Fat Diet Megan T
Quintana et al. BMC Endocrine Disorders (2015) 15:36 DOI 10.1186/s12902-015-0028-z RESEARCH ARTICLE Open Access Muscle ring finger-3 protects against diabetic cardiomyopathy induced by a high fat diet Megan T. Quintana1†, Jun He2,3†, Jenyth Sullivan5, Trisha Grevengoed6, Jonathan Schisler4,7, Yipin Han8, Joseph A. Hill9, Cecelia C. Yates10, William E. Stansfield1, Rudo F. Mapanga11, M. Faadiel Essop11, Michael J. Muehlbauer12, Christopher B. Newgard12,13, James R. Bain12,13 and Monte S. Willis2,4* Abstract Background: The pathogenesis of diabetic cardiomyopathy (DCM) involves the enhanced activation of peroxisome proliferator activating receptor (PPAR) transcription factors, including the most prominent isoform in the heart, PPARα. In cancer cells and adipocytes, post-translational modification of PPARs have been identified, including ligand-dependent degradation of PPARs by specific ubiquitin ligases. However, the regulation of PPARs in cardiomyocytes and heart have not previously been identified. We recently identified that muscle ring finger-1 (MuRF1) and MuRF2 differentially inhibit PPAR activities by mono-ubiquitination, leading to the hypothesis that MuRF3 may regulate PPAR activity in vivo to regulate DCM. Methods: MuRF3−/− mice were challenged with 26 weeks 60 % high fat diet to induce insulin resistance and DCM. Conscious echocardiography, blood glucose, tissue triglyceride, glycogen levels, immunoblot analysis of intracellular signaling, heart and skeletal muscle morphometrics, and PPARα,PPARβ,andPPARγ1 activities were assayed. Results: MuRF3−/− mice exhibited a premature systolic heart failure by 6 weeks high fat diet (vs. 12 weeks in MuRF3+/+). MuRF3−/− mice weighed significantly less than sibling-matched wildtype mice after 26 weeks HFD. These differences may be largely due to resistance to fat accumulation, as MRI analysis revealed MuRF3−/− mice had significantly less fat mass, but not lean body mass.
[Show full text]
Characterization of Porcine Tripartite Motif Genes As Host Restriction
Virus Research 270 (2019) 197647 Contents lists available at ScienceDirect Virus Research journal homepage: www.elsevier.com/locate/virusres Characterization of porcine tripartite motif genes as host restriction factors against PRRSV and PEDV infection T ⁎ ⁎ Ying Wei, Chuangchao Zou, Siying Zeng, Chunyi Xue , Yongchang Cao State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou 510006, China ARTICLE INFO ABSTRACT Keywords: Members of the tripartite motif (TRIM) family are the important effectors of the innate immune response against Porcine tripartite motif family viral infections. However, it is still unknown whether porcine TRIM (pTRIM) genes may restrict the infection of Positive selection porcine reproductive and respiratory syndrome virus (PRRSV) and porcine epidemic diarrhea virus (PEDV). In β IFN- this study, we firstly defined the entire pTRIM family. Fifty-seven pTRIMs were classified into 12 sub-families (C- Porcine reproductive and respiratory syndrome I to C-XII) based on variable C-terminus, and 17 out of them were identified as positively selected genes. Nine virus pTRIMs were identified as the IFN-stimulated genes in IFN-β treated porcine alveolar macrophages (PAMs). Porcine epidemic diarrhea virus Twelve pTRIMs were regulated in PRRSV or PEDV-infected PAMs, respectively. The mRNA expression of the implicated restriction factors (pTRIM5, 14, 21, 25 and 38) was detectable in all swine tissues studied, with the high expression in the spleen and lung tissues. These results firstly present the comprehensive characterization of pTRIM genes, and suggest the pTRIM5, 14, 21, 25, and 38 genes as the implicated host restriction factors against PRRSV and PEDV infection, which provide a basis to further study the functions of pTRIMs and the mechanism by which pTRIMs may act during viral infection.
[Show full text]
Supplementary Data Supplemental Fig. 1
Supplementary data Supplemental Fig. 1: Histological Comparison of tumor-of-origin to patient-derived-xenograft (PDX). immunoreactivity for H&E, Col4A, S100, and Ki67 in patient tumors of origin and corresponding PDX tumors with schematic depicting the site of the original tumor in the patient. Scale bar = 20um. Supplemental Fig. 2: Scatter plots displaying the correlation between tumor of origin and PDX DNA. Left: Tumor of origin v. patient derived xenograft (PDX) variant allele frequency (VAF) plots. Variance is in relation to the identity line, therefore, points along axis reflect evidence of heterogeneity. Right: Simple X/Y scatterplots showing raw counts gene expression levels of each tumor compared to its respective xenograft. The correlation coefficients (on a scale of 0 to 1) are included underneath. Supplemental Fig. 3: A) Heatmap of eight parental tumor samples with list of all genes. B) Heatmap of eight PDX samples with list of all genes. Both rows and columns of heatmaps are clustered using Euclidean distance and average linkage B A JH 2-002 JH 2-023 1 3 5 7 9 11 13 15 17 19 21 Chromosome 1 3 5 7 9 11 13 15 17 19 21 Chromosome 2 4 6 8 10 12 14 16 18 20 22 2 4 6 8 10 12 14 16 18 20 22 D C JH 2-031 WU-225 1 3 5 7 9 11 13 15 17 19 21 Chromosome Chromosome 1 3 5 7 9 11 13 15 17 19 21 2 4 6 8 10 12 14 16 18 20 22 2 4 6 8 10 12 14 16 18 20 22 E F WU-368 WU-386 Chromosome 1 3 5 7 9 11 13 15 17 19 21 Chromosome 1 3 5 7 9 11 13 15 17 19 21 2 4 6 8 10 12 14 16 18 20 22 2 4 6 8 10 12 14 16 18 20 22 G WU-436 Chromosome 1 3 5 7 9 11 13 15 17 19 21 2 4 6 8 10 12 14 16 18 20 22 Supplemental Figure 4: Gain of chromosome 8 is common in MPNST PDX.
[Show full text]