Anti-IL1RL2 Antibody

Total Page:16

File Type:pdf, Size:1020Kb

Anti-IL1RL2 Antibody D127219 Anti-IL1RL2 antibody Cat. No. D127219 Package 25 μl/100 μl/200 μl Storage -20°C, pH7.4 PBS, 0.05% NaN3, 40% Glycerol Product overview Description A n ti-IL1RL2 rabbit polyclonal antibody Applications ELISA, WB, IHC Immunogen Fusion protein of human IL1RL2 Reactivity Human Content 1 mg/ml Host species Rabbit Ig class Immunogen-specific rabbit IgG Purification Antigen affinity purification Target information Symbol IL1RL2 Full name interleukin 1 receptor like 2 Synonyms IL-36R; IL1RRP2; IL-1Rrp2; IL1R-rp2 Swissprot Q9HB29 Target Background The protein encoded by this gene is a member of the interleukin 1 receptor family. An experiment with transient gene expression demonstrated that this receptor was incapable of binding to interleukin 1 alpha and interleukin 1 beta with high affinity. This gene and four other interleukin 1 receptor family genes, including interleukin 1 receptor, type I (IL1R1), interleukin 1 receptor, type II (IL1R2), interleukin 1 receptor-like 1 (IL1RL1), and interleukin 18 receptor 1 (IL18R1), form a cytokine receptor gene cluster in a region mapped to chromosome 2q12. [provided by RefSeq, Jul 2008] Sangon Biotech Applications Immunohistochemistry Predicted cell location: Cytoplasm Predicted cell location: Cytoplasm Positive control: Human prostate cancer Positive control: Human ovarian cancer Recommended dilution: 100-300 Recommended dilution: 100-300 The image on the left is immunohistochemistry of paraffin-embedded The image on the left is immunohistochemistry of paraffin-embedded Human prostate cancer tissue using D127219(IL1RL2 Antibody) at Human ovarian cancer tissue using D127219(IL1RL2 Antibody) at dilution 1/130, on the right is treated with fusion protein. (Original dilution 1/130, on the right is treated with fusion protein. (Original magnification: ×200) magnification: ×200) Western blotting Predicted band size:65 kDa Positive control:K562 cell lysate Recommended dilution: 500-2000 Gel: 8%SDS-PAGE Lysate: 40 μg Lane: K562 cell lysate Primary antibody: D127219(IL1RL2 Antibody) at dilution 1/1000 Secondary antibody: Goat anti rabbit IgG at 1/5000 dilution Exposure time: 20 seconds ELISA Sangon Biotech Recommended dilution: 5000-10000 .
Recommended publications
  • Genetics of Interleukin 1 Receptor-Like 1 in Immune and Inflammatory Diseases
    Current Genomics, 2010, 11, 591-606 591 Genetics of Interleukin 1 Receptor-Like 1 in Immune and Inflammatory Diseases Loubna Akhabir and Andrew Sandford* Department of Medicine, University of British Columbia, UBC James Hogg Research Centre, Providence Heart + Lung Institute, Room 166, St. Paul's Hospital, 1081 Burrard Street, Vancouver, BC V6Z 1Y6, Canada Abstract: Interleukin 1 receptor-like 1 (IL1RL1) is gaining in recognition due to its involvement in immune/inflamma- tory disorders. Well-designed animal studies have shown its critical role in experimental allergic inflammation and human in vitro studies have consistently demonstrated its up-regulation in several conditions such as asthma and rheumatoid ar- thritis. The ligand for IL1RL1 is IL33 which emerged as playing an important role in initiating eosinophilic inflammation and activating other immune cells resulting in an allergic phenotype. An IL1RL1 single nucleotide polymorphism (SNP) was among the most significant results of a genome-wide scan inves- tigating eosinophil counts; in the same study, this SNP associated with asthma in 10 populations. The IL1RL1 gene resides in a region of high linkage disequilibrium containing interleukin 1 receptor genes as well as in- terleukin 18 receptor and accessory genes. This poses a challenge to researchers interested in deciphering genetic associa- tion signals in the region as all of the genes represent interesting candidates for asthma and allergic disease. The IL1RL1 gene and its resulting soluble and receptor proteins have emerged as key regulators of the inflammatory proc- ess implicated in a large variety of human pathologies We review the function and expression of the IL1RL1 gene.
    [Show full text]
  • Evolutionary Divergence and Functions of the Human Interleukin (IL) Gene Family Chad Brocker,1 David Thompson,2 Akiko Matsumoto,1 Daniel W
    UPDATE ON GENE COMPLETIONS AND ANNOTATIONS Evolutionary divergence and functions of the human interleukin (IL) gene family Chad Brocker,1 David Thompson,2 Akiko Matsumoto,1 Daniel W. Nebert3* and Vasilis Vasiliou1 1Molecular Toxicology and Environmental Health Sciences Program, Department of Pharmaceutical Sciences, University of Colorado Denver, Aurora, CO 80045, USA 2Department of Clinical Pharmacy, University of Colorado Denver, Aurora, CO 80045, USA 3Department of Environmental Health and Center for Environmental Genetics (CEG), University of Cincinnati Medical Center, Cincinnati, OH 45267–0056, USA *Correspondence to: Tel: þ1 513 821 4664; Fax: þ1 513 558 0925; E-mail: [email protected]; [email protected] Date received (in revised form): 22nd September 2010 Abstract Cytokines play a very important role in nearly all aspects of inflammation and immunity. The term ‘interleukin’ (IL) has been used to describe a group of cytokines with complex immunomodulatory functions — including cell proliferation, maturation, migration and adhesion. These cytokines also play an important role in immune cell differentiation and activation. Determining the exact function of a particular cytokine is complicated by the influence of the producing cell type, the responding cell type and the phase of the immune response. ILs can also have pro- and anti-inflammatory effects, further complicating their characterisation. These molecules are under constant pressure to evolve due to continual competition between the host’s immune system and infecting organisms; as such, ILs have undergone significant evolution. This has resulted in little amino acid conservation between orthologous proteins, which further complicates the gene family organisation. Within the literature there are a number of overlapping nomenclature and classification systems derived from biological function, receptor-binding properties and originating cell type.
    [Show full text]
  • 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 ........................................................................................
    [Show full text]
  • Science Journals
    SCIENCE IMMUNOLOGY | RESEARCH RESOURCE T CELL MEMORY Copyright © 2020 The Authors, some rights reserved; Early precursors and molecular determinants of tissue- exclusive licensee + American Association resident memory CD8 T lymphocytes revealed by for the Advancement of Science. No claim single-cell RNA sequencing to original U.S. Nadia S. Kurd1*†, Zhaoren He2,3*, Tiani L. Louis1, J. Justin Milner3, Kyla D. Omilusik3, Government Works Wenhao Jin2, Matthew S. Tsai1, Christella E. Widjaja1, Jad N. Kanbar1, Jocelyn G. Olvera1, Tiffani Tysl1, Lauren K. Quezada1, Brigid S. Boland1, Wendy J. Huang2, Cornelis Murre3, Ananda W. Goldrath3, Gene W. Yeo2,4‡, John T. Chang1,5‡§ + During an immune response to microbial infection, CD8 T cells give rise to distinct classes of cellular progeny that coordinately mediate clearance of the pathogen and provide long-lasting protection against reinfection, including Downloaded from a subset of noncirculating tissue-resident memory (TRM) cells that mediate potent protection within nonlymphoid + tissues. Here, we used single-cell RNA sequencing to examine the gene expression patterns of individual CD8 T cells in the spleen and small intestine intraepithelial lymphocyte (siIEL) compartment throughout the course of their differentiation in response to viral infection. These analyses revealed previously unknown transcriptional + heterogeneity within the siIEL CD8 T cell population at several stages of differentiation, representing functionally distinct TRM cell subsets and a subset of TRM cell precursors within the tissue early in infection. Together, these http://immunology.sciencemag.org/ + findings may inform strategies to optimize CD8 T cell responses to protect against microbial infection and cancer. INTRODUCTION composed of distinct subsets that play unique roles in mediating CD8+ T cells responding to microbial challenge differentiate into protective immunity.
    [Show full text]
  • A Cytokine Network Involving IL-36Γ, IL-23, and IL-22 Promotes Antimicrobial Defense and Recovery from Intestinal Barrier Damage
    A cytokine network involving IL-36γ, IL-23, and IL-22 promotes antimicrobial defense and recovery from intestinal barrier damage Vu L. Ngoa, Hirohito Aboa, Estera Maxima, Akihito Harusatoa, Duke Geema, Oscar Medina-Contrerasa, Didier Merlinb,c, Andrew T. Gewirtza, Asma Nusratd, and Timothy L. Denninga,1 aCenter for Inflammation, Immunity & Infection, Institute for Biomedical Sciences, Georgia State University, Atlanta, GA 30303; bCenter for Diagnostics and Therapeutics, Institute for Biomedical Sciences, Georgia State University, Atlanta, GA 30303; cAtlanta Veterans Affairs Medical Center, Decatur, GA 30033; and dDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109 Edited by Fabio Cominelli, Case Western Reserve University School of Medicine, Cleveland, OH, and accepted by Editorial Board Member Tadatsugu Taniguchi April 23, 2018 (received for review November 10, 2017) The gut epithelium acts to separate host immune cells from unre- and antiapoptotic pathways that collectively aid in limiting bac- stricted interactions with the microbiota and other environmen- terial encroachment while promoting epithelial proliferation, tal stimuli. In response to epithelial damage or dysfunction, wound healing, and repair (7). Mice that lack the ability to immune cells are activated to produce interleukin (IL)-22, which is produce IL-22 following administration of dextran sodium sul- involved in repair and protection of barrier surfaces. However, the fate (DSS) or Citrobacter rodentium are grossly unable to repair specific pathways leading to IL-22 and associated antimicrobial barrier damage or control pathogenic bacterial expansion (8–10). peptide (AMP) production in response to intestinal tissue damage These data suggest that IL-22 plays a nonredundant function in remain incompletely understood.
    [Show full text]
  • Human Colon Cancer Primer Library
    Human Colon Cancer Primer Library Catalog No: HCCR-1 Supplier: RealTimePrimers Lot No: XXXXX Supplied as: solid Stability: store at -20°C Description Contains 88 primer sets directed against cytokine and chemokine receptor genes and 8 housekeeping gene primer sets. Provided in a 96-well microplate (20 ul - 10 uM). Perform up to 100 PCR arrays (based on 20 ul assay volume per reaction). Just add cDNA template and SYBR green master mix. Gene List: • CCR1 chemokine (C-C motif) receptor 1 • IL11RA interleukin 11 receptor, alpha • CCR2 chemokine (C-C motif) receptor 2 • IL11RB interleukin 11 receptor, beta • CCR3 chemokine (C-C motif) receptor 3 • IL12RB1 interleukin 12 receptor, beta 1 • CCR4 chemokine (C-C motif) receptor 4 • IL12RB2 interleukin 12 receptor, beta 2 • CCR5 chemokine (C-C motif) receptor 5 • IL13RA1 interleukin 13 receptor, alpha 1 • CCR6 chemokine (C-C motif) receptor 6 • IL13RA2 interleukin 13 receptor, alpha 2 • CCR7 chemokine (C-C motif) receptor 7 • IL15RA interleukin 15 receptor, alpha • CCR8 chemokine (C-C motif) receptor 8 • IL15RB interleukin 15 receptor, beta • CCR9 chemokine (C-C motif) receptor 9 • IL17RA interleukin 17 receptor A • CCR10 chemokine (C-C motif) receptor 10 • IL17RB interleukin 17 receptor B • CX3CR1 chemokine (C-X3-C motif) receptor 1 • IL17RC interleukin 17 receptor C • CXCR1 chemokine (C-X-C motif) receptor 1 • IL17RD interleukin 17 receptor D • CXCR2 chemokine (C-X-C motif) receptor 2 • IL17RE interleukin 17 receptor E • CXCR3 chemokine (C-X-C motif) receptor 3 • IL18R1 interleukin 18 receptor
    [Show full text]
  • Engineered Type 1 Regulatory T Cells Designed for Clinical Use Kill Primary
    ARTICLE Acute Myeloid Leukemia Engineered type 1 regulatory T cells designed Ferrata Storti Foundation for clinical use kill primary pediatric acute myeloid leukemia cells Brandon Cieniewicz,1* Molly Javier Uyeda,1,2* Ping (Pauline) Chen,1 Ece Canan Sayitoglu,1 Jeffrey Mao-Hwa Liu,1 Grazia Andolfi,3 Katharine Greenthal,1 Alice Bertaina,1,4 Silvia Gregori,3 Rosa Bacchetta,1,4 Norman James Lacayo,1 Alma-Martina Cepika1,4# and Maria Grazia Roncarolo1,2,4# Haematologica 2021 Volume 106(10):2588-2597 1Department of Pediatrics, Division of Stem Cell Transplantation and Regenerative Medicine, Stanford School of Medicine, Stanford, CA, USA; 2Stanford Institute for Stem Cell Biology and Regenerative Medicine, Stanford School of Medicine, Stanford, CA, USA; 3San Raffaele Telethon Institute for Gene Therapy, Milan, Italy and 4Center for Definitive and Curative Medicine, Stanford School of Medicine, Stanford, CA, USA *BC and MJU contributed equally as co-first authors #AMC and MGR contributed equally as co-senior authors ABSTRACT ype 1 regulatory (Tr1) T cells induced by enforced expression of interleukin-10 (LV-10) are being developed as a novel treatment for Tchemotherapy-resistant myeloid leukemias. In vivo, LV-10 cells do not cause graft-versus-host disease while mediating graft-versus-leukemia effect against adult acute myeloid leukemia (AML). Since pediatric AML (pAML) and adult AML are different on a genetic and epigenetic level, we investigate herein whether LV-10 cells also efficiently kill pAML cells. We show that the majority of primary pAML are killed by LV-10 cells, with different levels of sensitivity to killing. Transcriptionally, pAML sensitive to LV-10 killing expressed a myeloid maturation signature.
    [Show full text]
  • The Relationship of Indoxyl Sulfate and P-Cresyl Sulfate with Target
    www.nature.com/scientificreports OPEN The relationship of indoxyl sulfate and p‑cresyl sulfate with target cardiovascular proteins in hemodialysis patients Ping‑Hsun Wu1,2,6,9, Yi‑Ting Lin1,2,8,9, Yi‑Wen Chiu2,3,6, Gabriel Baldanzi9, Jiun‑Chi Huang1,2,6,7, Shih‑Shin Liang4, Su‑Chu Lee6, Szu‑Chia Chen1,2,6,7, Ya‑Ling Hsu5, Mei‑Chuan Kuo2,3,6* & Shang‑Jyh Hwang2,3,6 Protein‑bound uremic toxins (Indoxyl sulfate [IS] and p‑cresyl sulfate [PCS]) are both associated with cardiovascular (CV) and all‑cause mortality in subjects with chronic kidney disease (CKD). Possible mechanisms have not been elucidated. In hemodialysis patients, we investigated the relationship between the free form of IS and PCS and 181 CV‑related proteins. First, IS or PCS concentrations were checked, and high levels were associated with an increased risk of acute coronary syndrome (ACS) in 333 stable HD patients. CV proteins were further quantifed by a proximity extension assay. We examined associations between the free form protein‑bound uremic toxins and the quantifed proteins with correction for multiple testing in the discovery process. In the second step, the independent association was evaluated by multivariable‑adjusted models. We rank the CV proteins related to protein‑bound uremic toxins by bootstrapped confdence intervals and ascending p‑value. Six proteins (signaling lymphocytic activation molecule family member 5, complement component C1q receptor, C–C motif chemokine 15 [CCL15], bleomycin hydrolase, perlecan, and cluster of diferentiation 166 antigen) were negatively associated with IS. Fibroblast growth factor 23 [FGF23] was the only CV protein positively associated with IS.
    [Show full text]
  • Primary Chicken and Duck Endothelial Cells Display a Differential Response to Infection with Highly Pathogenic Avian Influenza Virus
    G C A T T A C G G C A T genes Article Primary Chicken and Duck Endothelial Cells Display a Differential Response to Infection with Highly Pathogenic Avian Influenza Virus Zhen Wei Marcus Tong 1,†, Anjana C. Karawita 1,2,† , Colin Kern 3, Huaijun Zhou 3 , Jane E. Sinclair 1 , Limin Yan 1, Keng Yih Chew 1, Sue Lowther 2, Lee Trinidad 2, Arjun Challagulla 2 , Karel A. Schat 4 , Michelle L. Baker 2 and Kirsty R. Short 1,5,* 1 School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane 4072, Australia; [email protected] (Z.W.M.T.); [email protected] (A.C.K.); [email protected] (J.E.S.); [email protected] (L.Y.); [email protected] (K.Y.C.) 2 CSIRO, Australian Centre for Disease Preparedness, Health, and Biosecurity Business Unit, Geelong 3219, Australia; [email protected] (S.L.); [email protected] (L.T.); [email protected] (A.C.); [email protected] (M.L.B.) 3 Department of Animal Science, University of California, Davis, CA 95616, USA; [email protected] (C.K.); [email protected] (H.Z.) 4 Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA; [email protected] 5 Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane 4072, Australia * Correspondence: [email protected] † These authors contributed equally to this work. Citation: Tong, Z.W.M.; Karawita, A.C.; Kern, C.; Zhou, H.; Sinclair, J.E.; Abstract: Highly pathogenic avian influenza viruses (HPAIVs) in gallinaceous poultry are associated Yan, L.; Chew, K.Y.; Lowther, S.; Trinidad, L.; Challagulla, A.; et al.
    [Show full text]
  • IL-1 Receptor-Related Protein 2 B Activation Through the Orphan Κ of NF
    Two Novel IL-1 Family Members, IL-1δ and IL-1 ε, Function as an Antagonist and Agonist of NF- κB Activation Through the Orphan IL-1 Receptor-Related Protein 2 This information is current as of September 27, 2021. Reno Debets, Jackie C. Timans, Bernhard Homey, Sandra Zurawski, Theodore R. Sana, Sylvia Lo, Janet Wagner, Gina Edwards, Teresa Clifford, Satish Menon, J. Fernando Bazan and Robert A. Kastelein J Immunol 2001; 167:1440-1446; ; Downloaded from doi: 10.4049/jimmunol.167.3.1440 http://www.jimmunol.org/content/167/3/1440 http://www.jimmunol.org/ References This article cites 52 articles, 22 of which you can access for free at: http://www.jimmunol.org/content/167/3/1440.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists by guest on September 27, 2021 • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2001 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. Two Novel IL-1 Family Members, IL-1␦ and IL-1⑀, Function as an Antagonist and Agonist of NF-␬B Activation Through the Orphan IL-1 Receptor-Related Protein 21 Reno Debets, Jackie C.
    [Show full text]
  • Common Genetic Variation at the IL1RL1 Locus Regulates IL- 33/ST2 Signaling
    Common genetic variation at the IL1RL1 locus regulates IL- 33/ST2 signaling Jennifer E. Ho, … , Richard T. Lee, Thomas J. Wang J Clin Invest. 2013;123(10):4208-4218. https://doi.org/10.1172/JCI67119. Research Article Immunology The suppression of tumorigenicity 2/IL-33 (ST2/IL-33) pathway has been implicated in several immune and inflammatory diseases. ST2 is produced as 2 isoforms. The membrane-bound isoform (ST2L) induces an immune response when bound to its ligand, IL-33. The other isoform is a soluble protein (sST2) that is thought to be a decoy receptor for IL-33 signaling. Elevated sST2 levels in serum are associated with an increased risk for cardiovascular disease. We investigated the determinants of sST2 plasma concentrations in 2,991 Framingham Offspring Cohort participants. While clinical and environmental factors explained some variation in sST2 levels, much of the variation in sST2 production was driven by genetic factors. In a genome-wide association study (GWAS), multiple SNPs within IL1RL1 (the gene encoding ST2) demonstrated associations with sST2 concentrations. Five missense variants of IL1RL1 correlated with higher sST2 levels in the GWAS and mapped to the intracellular domain of ST2, which is absent in sST2. In a cell culture model, IL1RL1 missense variants increased sST2 expression by inducing IL-33 expression and enhancing IL-33 responsiveness (via ST2L). Our data suggest that genetic variation in IL1RL1 can result in increased levels of sST2 and alter immune and inflammatory signaling through the ST2/IL-33 pathway. Find the latest version: https://jci.me/67119/pdf Research article Common genetic variation at the IL1RL1 locus regulates IL-33/ST2 signaling Jennifer E.
    [Show full text]
  • Peripheral Nerve Single-Cell Analysis Identifies Mesenchymal Ligands That Promote Axonal Growth
    Research Article: New Research Development Peripheral Nerve Single-Cell Analysis Identifies Mesenchymal Ligands that Promote Axonal Growth Jeremy S. Toma,1 Konstantina Karamboulas,1,ª Matthew J. Carr,1,2,ª Adelaida Kolaj,1,3 Scott A. Yuzwa,1 Neemat Mahmud,1,3 Mekayla A. Storer,1 David R. Kaplan,1,2,4 and Freda D. Miller1,2,3,4 https://doi.org/10.1523/ENEURO.0066-20.2020 1Program in Neurosciences and Mental Health, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada, 2Institute of Medical Sciences University of Toronto, Toronto, Ontario M5G 1A8, Canada, 3Department of Physiology, University of Toronto, Toronto, Ontario M5G 1A8, Canada, and 4Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5G 1A8, Canada Abstract Peripheral nerves provide a supportive growth environment for developing and regenerating axons and are es- sential for maintenance and repair of many non-neural tissues. This capacity has largely been ascribed to paracrine factors secreted by nerve-resident Schwann cells. Here, we used single-cell transcriptional profiling to identify ligands made by different injured rodent nerve cell types and have combined this with cell-surface mass spectrometry to computationally model potential paracrine interactions with peripheral neurons. These analyses show that peripheral nerves make many ligands predicted to act on peripheral and CNS neurons, in- cluding known and previously uncharacterized ligands. While Schwann cells are an important ligand source within injured nerves, more than half of the predicted ligands are made by nerve-resident mesenchymal cells, including the endoneurial cells most closely associated with peripheral axons. At least three of these mesen- chymal ligands, ANGPT1, CCL11, and VEGFC, promote growth when locally applied on sympathetic axons.
    [Show full text]