Human Flow Cytometry Antibodies
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(CD147) Is Induced by C/Ebpβ and Is Differentially Expressed in ALK+
Laboratory Investigation (2017) 97, 1095–1102 © 2017 USCAP, Inc All rights reserved 0023-6837/17 EMMPRIN (CD147) is induced by C/EBPβ and is differentially expressed in ALK+ and ALK − anaplastic large-cell lymphoma Janine Schmidt1, Irina Bonzheim1, Julia Steinhilber1, Ivonne A Montes-Mojarro1, Carlos Ortiz-Hidalgo2, Wolfram Klapper3, Falko Fend1 and Leticia Quintanilla-Martínez1 Anaplastic lymphoma kinase-positive (ALK+) anaplastic large-cell lymphoma (ALCL) is characterized by expression of oncogenic ALK fusion proteins due to the translocation t(2;5)(p23;q35) or variants. Although genotypically a T-cell lymphoma, ALK+ ALCL cells frequently show loss of T-cell-specific surface antigens and expression of monocytic markers. C/EBPβ, a transcription factor constitutively overexpressed in ALK+ ALCL cells, has been shown to play an important role in the activation and differentiation of macrophages and is furthermore capable of transdifferentiating B-cell and T-cell progenitors to macrophages in vitro. To analyze the role of C/EBPβ for the unusual phenotype of ALK+ ALCL cells, C/EBPβ was knocked down by RNA interference in two ALK+ ALCL cell lines, and surface antigen expression profiles of these cell lines were generated using a Human Cell Surface Marker Screening Panel (BD Biosciences). Interesting candidate antigens were further analyzed by immunohistochemistry in primary ALCL ALK+ and ALK − cases. Antigen expression profiling revealed marked changes in the expression of the activation markers CD25, CD30, CD98, CD147, and CD227 after C/EBPβ knockdown. Immunohistochemical analysis confirmed a strong, membranous CD147 (EMMPRIN) expression in ALK+ ALCL cases. In contrast, ALK − ALCL cases showed a weaker CD147 expression. -
Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse
Welcome to More Choice CD Marker Handbook For more information, please visit: Human bdbiosciences.com/eu/go/humancdmarkers Mouse bdbiosciences.com/eu/go/mousecdmarkers Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse CD3 CD3 CD (cluster of differentiation) molecules are cell surface markers T Cell CD4 CD4 useful for the identification and characterization of leukocytes. The CD CD8 CD8 nomenclature was developed and is maintained through the HLDA (Human Leukocyte Differentiation Antigens) workshop started in 1982. CD45R/B220 CD19 CD19 The goal is to provide standardization of monoclonal antibodies to B Cell CD20 CD22 (B cell activation marker) human antigens across laboratories. To characterize or “workshop” the antibodies, multiple laboratories carry out blind analyses of antibodies. These results independently validate antibody specificity. CD11c CD11c Dendritic Cell CD123 CD123 While the CD nomenclature has been developed for use with human antigens, it is applied to corresponding mouse antigens as well as antigens from other species. However, the mouse and other species NK Cell CD56 CD335 (NKp46) antibodies are not tested by HLDA. Human CD markers were reviewed by the HLDA. New CD markers Stem Cell/ CD34 CD34 were established at the HLDA9 meeting held in Barcelona in 2010. For Precursor hematopoetic stem cell only hematopoetic stem cell only additional information and CD markers please visit www.hcdm.org. Macrophage/ CD14 CD11b/ Mac-1 Monocyte CD33 Ly-71 (F4/80) CD66b Granulocyte CD66b Gr-1/Ly6G Ly6C CD41 CD41 CD61 (Integrin b3) CD61 Platelet CD9 CD62 CD62P (activated platelets) CD235a CD235a Erythrocyte Ter-119 CD146 MECA-32 CD106 CD146 Endothelial Cell CD31 CD62E (activated endothelial cells) Epithelial Cell CD236 CD326 (EPCAM1) For Research Use Only. -
Mast Cells Promote Seasonal White Adipose Beiging in Humans
Diabetes Volume 66, May 2017 1237 Mast Cells Promote Seasonal White Adipose Beiging in Humans Brian S. Finlin,1 Beibei Zhu,1 Amy L. Confides,2 Philip M. Westgate,3 Brianna D. Harfmann,1 Esther E. Dupont-Versteegden,2 and Philip A. Kern1 Diabetes 2017;66:1237–1246 | DOI: 10.2337/db16-1057 Human subcutaneous (SC) white adipose tissue (WAT) localized to the neck and thorax of humans (4–8), and in a increases the expression of beige adipocyte genes in the process known as beiging (9), UCP1-positive adipocytes winter. Studies in rodents suggest that a number of form in subcutaneous (SC) white adipose tissue (WAT) immune mediators are important in the beiging response. (10). Beige adipocytes have unique developmental origins, We studied the seasonal beiging response in SC WAT gene signatures, and functional properties, including being from lean humans. We measured the gene expression of highly inducible to increase UCP1 in response to catechol- various immune cell markers and performed multivariate amines (9,11–13). Although questions exist about whether analysis of the gene expression data to identify genes beige fat can make a meaningful contribution to energy OBESITY STUDIES that predict UCP1. Interleukin (IL)-4 and, unexpectedly, expenditure in humans (reviewed in Porter et al. [14]), the mast cell marker CPA3 predicted UCP1 gene expres- the induction of beige fat in rodent models is associated sion. Therefore, we investigated the effects of mast with increased energy expenditure and improved glucose cells on UCP1 induction by adipocytes. TIB64 mast cells homeostasis (13). responded to cold by releasing histamine and IL-4, and this medium stimulated UCP1 expression and lipolysis by Activation of the sympathetic nervous system by cold 3T3-L1 adipocytes. -
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated. -
Supplementary Table 1: Adhesion Genes Data Set
Supplementary Table 1: Adhesion genes data set PROBE Entrez Gene ID Celera Gene ID Gene_Symbol Gene_Name 160832 1 hCG201364.3 A1BG alpha-1-B glycoprotein 223658 1 hCG201364.3 A1BG alpha-1-B glycoprotein 212988 102 hCG40040.3 ADAM10 ADAM metallopeptidase domain 10 133411 4185 hCG28232.2 ADAM11 ADAM metallopeptidase domain 11 110695 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 195222 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 165344 8751 hCG20021.3 ADAM15 ADAM metallopeptidase domain 15 (metargidin) 189065 6868 null ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme) 108119 8728 hCG15398.4 ADAM19 ADAM metallopeptidase domain 19 (meltrin beta) 117763 8748 hCG20675.3 ADAM20 ADAM metallopeptidase domain 20 126448 8747 hCG1785634.2 ADAM21 ADAM metallopeptidase domain 21 208981 8747 hCG1785634.2|hCG2042897 ADAM21 ADAM metallopeptidase domain 21 180903 53616 hCG17212.4 ADAM22 ADAM metallopeptidase domain 22 177272 8745 hCG1811623.1 ADAM23 ADAM metallopeptidase domain 23 102384 10863 hCG1818505.1 ADAM28 ADAM metallopeptidase domain 28 119968 11086 hCG1786734.2 ADAM29 ADAM metallopeptidase domain 29 205542 11085 hCG1997196.1 ADAM30 ADAM metallopeptidase domain 30 148417 80332 hCG39255.4 ADAM33 ADAM metallopeptidase domain 33 140492 8756 hCG1789002.2 ADAM7 ADAM metallopeptidase domain 7 122603 101 hCG1816947.1 ADAM8 ADAM metallopeptidase domain 8 183965 8754 hCG1996391 ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma) 129974 27299 hCG15447.3 ADAMDEC1 ADAM-like, -
Flow Reagents Single Color Antibodies CD Chart
CD CHART CD N° Alternative Name CD N° Alternative Name CD N° Alternative Name Beckman Coulter Clone Beckman Coulter Clone Beckman Coulter Clone T Cells B Cells Granulocytes NK Cells Macrophages/Monocytes Platelets Erythrocytes Stem Cells Dendritic Cells Endothelial Cells Epithelial Cells T Cells B Cells Granulocytes NK Cells Macrophages/Monocytes Platelets Erythrocytes Stem Cells Dendritic Cells Endothelial Cells Epithelial Cells T Cells B Cells Granulocytes NK Cells Macrophages/Monocytes Platelets Erythrocytes Stem Cells Dendritic Cells Endothelial Cells Epithelial Cells CD1a T6, R4, HTA1 Act p n n p n n S l CD99 MIC2 gene product, E2 p p p CD223 LAG-3 (Lymphocyte activation gene 3) Act n Act p n CD1b R1 Act p n n p n n S CD99R restricted CD99 p p CD224 GGT (γ-glutamyl transferase) p p p p p p CD1c R7, M241 Act S n n p n n S l CD100 SEMA4D (semaphorin 4D) p Low p p p n n CD225 Leu13, interferon induced transmembrane protein 1 (IFITM1). p p p p p CD1d R3 Act S n n Low n n S Intest CD101 V7, P126 Act n p n p n n p CD226 DNAM-1, PTA-1 Act n Act Act Act n p n CD1e R2 n n n n S CD102 ICAM-2 (intercellular adhesion molecule-2) p p n p Folli p CD227 MUC1, mucin 1, episialin, PUM, PEM, EMA, DF3, H23 Act p CD2 T11; Tp50; sheep red blood cell (SRBC) receptor; LFA-2 p S n p n n l CD103 HML-1 (human mucosal lymphocytes antigen 1), integrin aE chain S n n n n n n n l CD228 Melanotransferrin (MT), p97 p p CD3 T3, CD3 complex p n n n n n n n n n l CD104 integrin b4 chain; TSP-1180 n n n n n n n p p CD229 Ly9, T-lymphocyte surface antigen p p n p n -
No Evidence for Basigin/CD147 As a Direct SARS-Cov-2 Spike
www.nature.com/scientificreports OPEN No evidence for basigin/CD147 as a direct SARS‑CoV‑2 spike binding receptor Jarrod Shilts 1*, Thomas W. M. Crozier 2, Edward J. D. Greenwood2, Paul J. Lehner 2 & Gavin J. Wright 1,3* The spike protein of SARS‑CoV‑2 is known to enable viral invasion into human cells through direct binding to host receptors including ACE2. An alternate entry receptor for the virus was recently proposed to be basigin/CD147. These early studies have already prompted a clinical trial and multiple published hypotheses speculating on the role of this host receptor in viral infection and pathogenesis. Here, we report that we are unable to fnd evidence supporting the role of basigin as a putative spike binding receptor. Recombinant forms of the SARS‑CoV‑2 spike do not interact with basigin expressed on the surface of human cells, and by using specialized assays tailored to detect receptor interactions as weak or weaker than the proposed basigin‑spike binding, we report no evidence for a direct interaction between the viral spike protein to either of the two common isoforms of basigin. Finally, removing basigin from the surface of human lung epithelial cells by CRISPR/Cas9 results in no change in their susceptibility to SARS‑CoV‑2 infection. Given the pressing need for clarity on which viral targets may lead to promising therapeutics, we present these fndings to allow more informed decisions about the translational relevance of this putative mechanism in the race to understand and treat COVID‑19. Te sudden emergence of SARS-CoV-2 in late 2019 has demanded extensive research be directed to resolve the many uncharted aspects of this previously-unknown virus. -
Human Lectins, Their Carbohydrate Affinities and Where to Find Them
biomolecules Review Human Lectins, Their Carbohydrate Affinities and Where to Review HumanFind Them Lectins, Their Carbohydrate Affinities and Where to FindCláudia ThemD. Raposo 1,*, André B. Canelas 2 and M. Teresa Barros 1 1, 2 1 Cláudia D. Raposo * , Andr1 é LAQVB. Canelas‐Requimte,and Department M. Teresa of Chemistry, Barros NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829‐516 Caparica, Portugal; [email protected] 12 GlanbiaLAQV-Requimte,‐AgriChemWhey, Department Lisheen of Chemistry, Mine, Killoran, NOVA Moyne, School E41 of ScienceR622 Co. and Tipperary, Technology, Ireland; canelas‐ [email protected] NOVA de Lisboa, 2829-516 Caparica, Portugal; [email protected] 2* Correspondence:Glanbia-AgriChemWhey, [email protected]; Lisheen Mine, Tel.: Killoran, +351‐212948550 Moyne, E41 R622 Tipperary, Ireland; [email protected] * Correspondence: [email protected]; Tel.: +351-212948550 Abstract: Lectins are a class of proteins responsible for several biological roles such as cell‐cell in‐ Abstract:teractions,Lectins signaling are pathways, a class of and proteins several responsible innate immune for several responses biological against roles pathogens. such as Since cell-cell lec‐ interactions,tins are able signalingto bind to pathways, carbohydrates, and several they can innate be a immuneviable target responses for targeted against drug pathogens. delivery Since sys‐ lectinstems. In are fact, able several to bind lectins to carbohydrates, were approved they by canFood be and a viable Drug targetAdministration for targeted for drugthat purpose. delivery systems.Information In fact, about several specific lectins carbohydrate were approved recognition by Food by andlectin Drug receptors Administration was gathered for that herein, purpose. plus Informationthe specific organs about specific where those carbohydrate lectins can recognition be found by within lectin the receptors human was body. -
Pancancer IO360 Human Vapril2018
Gene Name Official Full Gene name Alias/Prev Symbols Previous Name(s) Alias Symbol(s) Alias Name(s) A2M alpha-2-macroglobulin FWP007,S863-7,CPAMD5 ABCF1 ATP binding cassette subfamily F member 1 ABC50 ATP-binding cassette, sub-family F (GCN20),EST123147 member 1 ACVR1C activin A receptor type 1C activin A receptor, type IC ALK7,ACVRLK7 ADAM12 ADAM metallopeptidase domain 12 a disintegrin and metalloproteinase domainMCMPMltna,MLTN 12 (meltrin alpha) meltrin alpha ADGRE1 adhesion G protein-coupled receptor E1 TM7LN3,EMR1 egf-like module containing, mucin-like, hormone receptor-like sequence 1,egf-like module containing, mucin-like, hormone receptor-like 1 ADM adrenomedullin AM ADORA2A adenosine A2a receptor ADORA2 RDC8 AKT1 AKT serine/threonine kinase 1 v-akt murine thymoma viral oncogene homologRAC,PKB,PRKBA,AKT 1 ALDOA aldolase, fructose-bisphosphate A aldolase A, fructose-bisphosphate ALDOC aldolase, fructose-bisphosphate C aldolase C, fructose-bisphosphate ANGPT1 angiopoietin 1 KIAA0003,Ang1 ANGPT2 angiopoietin 2 Ang2 ANGPTL4 angiopoietin like 4 angiopoietin-like 4 pp1158,PGAR,ARP4,HFARP,FIAF,NL2fasting-induced adipose factor,hepatic angiopoietin-related protein,PPARG angiopoietin related protein,hepatic fibrinogen/angiopoietin-related protein,peroxisome proliferator-activated receptor (PPAR) gamma induced angiopoietin-related protein,angiopoietin-related protein 4 ANLN anillin actin binding protein anillin (Drosophila Scraps homolog), actin bindingANILLIN,Scraps,scra protein,anillin, actin binding protein (scraps homolog, Drosophila) -
Development and Validation of a Protein-Based Risk Score for Cardiovascular Outcomes Among Patients with Stable Coronary Heart Disease
Supplementary Online Content Ganz P, Heidecker B, Hveem K, et al. Development and validation of a protein-based risk score for cardiovascular outcomes among patients with stable coronary heart disease. JAMA. doi: 10.1001/jama.2016.5951 eTable 1. List of 1130 Proteins Measured by Somalogic’s Modified Aptamer-Based Proteomic Assay eTable 2. Coefficients for Weibull Recalibration Model Applied to 9-Protein Model eFigure 1. Median Protein Levels in Derivation and Validation Cohort eTable 3. Coefficients for the Recalibration Model Applied to Refit Framingham eFigure 2. Calibration Plots for the Refit Framingham Model eTable 4. List of 200 Proteins Associated With the Risk of MI, Stroke, Heart Failure, and Death eFigure 3. Hazard Ratios of Lasso Selected Proteins for Primary End Point of MI, Stroke, Heart Failure, and Death eFigure 4. 9-Protein Prognostic Model Hazard Ratios Adjusted for Framingham Variables eFigure 5. 9-Protein Risk Scores by Event Type This supplementary material has been provided by the authors to give readers additional information about their work. Downloaded From: https://jamanetwork.com/ on 10/02/2021 Supplemental Material Table of Contents 1 Study Design and Data Processing ......................................................................................................... 3 2 Table of 1130 Proteins Measured .......................................................................................................... 4 3 Variable Selection and Statistical Modeling ........................................................................................ -
Suppressive Myeloid Cells Are a Hallmark of Severe COVID-19
medRxiv preprint doi: https://doi.org/10.1101/2020.06.03.20119818; this version posted June 5, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted medRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license . 1 Suppressive myeloid cells are a hallmark of 2 severe COVID-19 3 Jonas Schulte-Schrepping1*, Nico Reusch1*, Daniela Paclik2*, Kevin Baßler1*, Stephan 4 Schlickeiser3*, Bowen Zhang4*, Benjamin Krämer5*, Tobias Krammer6*, Sophia Brumhard7*, 5 Lorenzo Bonaguro1*, Elena De Domenico8*, Daniel Wendisch7*, Martin Grasshoff4, Theodore S. 6 Kapellos1, Michael Beckstette4, Tal Pecht1, Adem Saglam8, Oliver Dietrich6, Henrik E. Mei9, Axel 7 R. Schulz9, Claudia Conrad7, Désirée Kunkel10, Ehsan Vafadarnejad6, Cheng-Jian Xu4,11, Arik 8 Horne1, Miriam Herbert1, Anna Drews8, Charlotte Thibeault7, Moritz Pfeiffer7, Stefan 9 Hippenstiel7,12, Andreas Hocke7,12, Holger Müller-Redetzky7, Katrin-Moira Heim7, Felix Machleidt7, 10 Alexander Uhrig7, Laure Bousquillon de Jarcy7, Linda Jürgens7, Miriam Stegemann7, Christoph 11 R. Glösenkamp7, Hans-Dieter Volk2,3,13, Christine Goffinet14,15, Jan Raabe5, Kim Melanie Kaiser5, 12 Michael To Vinh5, Gereon Rieke5, Christian Meisel14, Thomas Ulas8, Matthias Becker8, Robert 13 Geffers16, Martin Witzenrath7,12, Christian Drosten14,19, Norbert Suttorp7,12, Christof von Kalle17, 14 Florian Kurth7,18, Kristian Händler8, Joachim L. Schultze1,8,#,$, Anna C Aschenbrenner20,#, Yang 15 Li4,#, -
Targets to Watch for SARS-Cov-2 and COVID-19
Drugs of the Future 2020, 45(4): 1-6 (Advanced Publication) Copyright © 2020 Clarivate Analytics CCC: 0377-8282/2020 DOI: 10.1358/dof.2020.45.4.3150676 Targets to Watch Taking aim at a fast-moving target: targets to watch for SARS-CoV-2 and COVID-19 L.A. Sorbera, A.I. Graul and C. Dulsat Clarivate Analytics, Barcelona, Spain Contents six coronaviruses had been known to cause disease in humans: HCoV-229E, HCoV-OC43, HCoV-NL63, HCoV-HKU1, Summary ........................................... 1 severe acute respiratory syndrome coronavirus (SARS-CoV) Introduction ........................................ 1 and Middle East respiratory virus coronavirus (MERS-CoV). SARS-CoV-2 and COVID-19 ............................ 1 The first four are endemic locally; they have been associ- Targets ............................................. 2 ated mainly with mild, self-limiting disease, whereas the latter two—both betacoronaviruses—can cause severe References .......................................... 5 illness (1-3). Given the high prevalence and wide distribution of coro- naviruses, their large genetic diversity as well as the fre- Summary quent recombination of their genomes, and increasing Severe acute respiratory syndrome coronavirus 2 (SARS- activity at the human–animal interface, these viruses CoV-2) is characterized as a betacoronavirus and recog- represent an ongoing threat to human health (4). This fact nized as the seventh discrete coronavirus species capable of recently became starkly evident, with the emergence and causing human disease. This new coronavirus causes febrile rapid spread of a novel coronavirus, first in mainland China respiratory illness and on March 11, 2020, was character- and now globally. The virus—provisionally designated ized as a global pandemic. Investigators have accelerated 2019-nCoV and later given the official name SARS-CoV-2, the search for a vaccine to prevent infection and for agents due to its similarity to SARS-CoV—was quickly isolated to treat it.