Anti-AID Antibody [EK2-5G9] (ARG23560)

Total Page:16

File Type:pdf, Size:1020Kb

Anti-AID Antibody [EK2-5G9] (ARG23560) Product datasheet [email protected] ARG23560 Package: 25 μg anti-AID antibody [EK2-5G9] Store at: -20°C Summary Product Description Rat Monoclonal antibody [EK2-5G9] recognizes AID. Rat anti Human AID antibody, clone EK2-5G9 recognizes human Single-stranded DNA cytosine deaminase, also known as Activation-induced cytidine deaminase or Cytidine aminohydrolase. AID is a 198 amino acid ~24 kDa RNA-editing enzyme essential for the initiation of immunoglobulin class switch recombination, somatic hypermutation and gene conversion.AID is selectively expressed by germinal centre B cells and B cell-derived lymphomas (Basso et al. 2012). Mutation in the AICDA gene is responsible for the autosomal recessive condition Immunodeficiency with hyper-IgM 2 (HIGM2) A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE resulting in extreme susceptibility to bacterial infection. Tested Reactivity Hu Tested Application ELISA, FACS, IHC-P, WB Host Rat Clonality Monoclonal Clone EK2-5G9 Isotype IgG2b Target Name AID Antigen Species Human Immunogen Synthetic peptide around aa. 185-198 of Human AID. Conjugation Un-conjugated Alternate Names Cytidine aminohydrolase; CDA2; HIGM2; Activation-induced cytidine deaminase; AID; EC 3.5.4.38; ARP2; Single-stranded DNA cytosine deaminase; HEL-S-284 Application Instructions Application table Application Dilution ELISA Assay-dependent FACS Assay-dependent IHC-P Assay-dependent WB Assay-dependent Application Note IHC-P: Antigen Retrieval: Boil tissue section in EDTA (pH 8.0). FACS: Membrane permeabilisation is required for this application. Use 10 µl of the suggested working dilution to label 10^6 cells in 100 µl. * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Calculated Mw 24 kDa Properties www.arigobio.com 1/2 Form Liquid Purification Purification with Protein G. Buffer PBS and 0.09% Sodium azide. Preservative 0.09% Sodium azide Concentration 1 mg/ml 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. Bioinformation Gene Symbol AICDA Gene Full Name activation-induced cytidine deaminase Background This gene encodes a RNA-editing deaminase that is a member of the cytidine deaminase family. The protein is involved in somatic hypermutation, gene conversion, and class-switch recombination of immunoglobulin genes. Defects in this gene are the cause of autosomal recessive hyper-IgM immunodeficiency syndrome type 2 (HIGM2). [provided by RefSeq, Feb 2009] Function Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation, gene conversion, and class-switch recombination in B-lymphocytes. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. [UniProt] www.arigobio.com 2/2 Powered by TCPDF (www.tcpdf.org).
Recommended publications
  • Gentaur Products List
    Chapter 2 : Gentaur Products List • Rabbit Anti LAMR1 Polyclonal Antibody Cy5 Conjugated Conjugated • Rabbit Anti Podoplanin gp36 Polyclonal Antibody Cy5 • Rabbit Anti LAMR1 CT Polyclonal Antibody Cy5 • Rabbit Anti phospho NFKB p65 Ser536 Polyclonal Conjugated Conjugated Antibody Cy5 Conjugated • Rabbit Anti CHRNA7 Polyclonal Antibody Cy5 Conjugated • Rat Anti IAA Monoclonal Antibody Cy5 Conjugated • Rabbit Anti EV71 VP1 CT Polyclonal Antibody Cy5 • Rabbit Anti Connexin 40 Polyclonal Antibody Cy5 • Rabbit Anti IAA Indole 3 Acetic Acid Polyclonal Antibody Conjugated Conjugated Cy5 Conjugated • Rabbit Anti LHR CGR Polyclonal Antibody Cy5 Conjugated • Rabbit Anti Integrin beta 7 Polyclonal Antibody Cy5 • Rabbit Anti Natrexone Polyclonal Antibody Cy5 Conjugated • Rabbit Anti MMP 20 Polyclonal Antibody Cy5 Conjugated Conjugated • Rabbit Anti Melamine Polyclonal Antibody Cy5 Conjugated • Rabbit Anti BCHE NT Polyclonal Antibody Cy5 Conjugated • Rabbit Anti NAP1 NAP1L1 Polyclonal Antibody Cy5 • Rabbit Anti Acetyl p53 K382 Polyclonal Antibody Cy5 • Rabbit Anti BCHE CT Polyclonal Antibody Cy5 Conjugated Conjugated Conjugated • Rabbit Anti HPV16 E6 Polyclonal Antibody Cy5 Conjugated • Rabbit Anti CCP Polyclonal Antibody Cy5 Conjugated • Rabbit Anti JAK2 Polyclonal Antibody Cy5 Conjugated • Rabbit Anti HPV18 E6 Polyclonal Antibody Cy5 Conjugated • Rabbit Anti HDC Polyclonal Antibody Cy5 Conjugated • Rabbit Anti Microsporidia protien Polyclonal Antibody Cy5 • Rabbit Anti HPV16 E7 Polyclonal Antibody Cy5 Conjugated • Rabbit Anti Neurocan Polyclonal
    [Show full text]
  • Phylogenetic Analysis, Subcellular Localization, and Expression
    BMC Plant Biology BioMed Central Research article Open Access Phylogenetic analysis, subcellular localization, and expression patterns of RPD3/HDA1 family histone deacetylases in plants Malona V Alinsug, Chun-Wei Yu and Keqiang Wu* Address: Institute of Plant Biology, College of Life Science, National Taiwan University, Taipei, Taiwan Email: Malona V Alinsug - [email protected]; Chun-Wei Yu - [email protected]; Keqiang Wu* - [email protected] * Corresponding author Published: 28 March 2009 Received: 26 November 2008 Accepted: 28 March 2009 BMC Plant Biology 2009, 9:37 doi:10.1186/1471-2229-9-37 This article is available from: http://www.biomedcentral.com/1471-2229/9/37 © 2009 Alinsug et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract Background: Although histone deacetylases from model organisms have been previously identified, there is no clear basis for the classification of histone deacetylases under the RPD3/ HDA1 superfamily, particularly on plants. Thus, this study aims to reconstruct a phylogenetic tree to determine evolutionary relationships between RPD3/HDA1 histone deacetylases from six different plants representing dicots with Arabidopsis thaliana, Populus trichocarpa, and Pinus taeda, monocots with Oryza sativa and Zea mays, and the lower plants with Physcomitrella patens. Results: Sixty two histone deacetylases of RPD3/HDA1 family from the six plant species were phylogenetically analyzed to determine corresponding orthologues. Three clusters were formed separating Class I, Class II, and Class IV.
    [Show full text]
  • Lysine Acetylation: Elucidating the Components of an Emerging Global Signaling Pathway in Trypanosomes
    Hindawi Publishing Corporation Journal of Biomedicine and Biotechnology Volume 2012, Article ID 452934, 16 pages doi:10.1155/2012/452934 Review Article Lysine Acetylation: Elucidating the Components of an Emerging Global Signaling Pathway in Trypanosomes Victoria Lucia Alonso1, 2 and Esteban Carlos Serra1, 2 1 Departamento de Microbiolog´ıa, Facultad de Ciencias Bioqu´ımicas y Farmac´euticas, Universidad Nacional de Rosario, Suipacha 531, Rosario 2000, Argentina 2 Instituto de Biolog´ıa Molecular y Celular de Rosario, CONICET-UNR, Suipacha 590, Rosario 2000, Argentina Correspondence should be addressed to Esteban Carlos Serra, [email protected] Received 17 April 2012; Revised 20 July 2012; Accepted 30 July 2012 Academic Editor: Andrea Silvana Ropolo´ Copyright © 2012 V. L. Alonso and E. C. Serra. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. In the past ten years the number of acetylated proteins reported in literature grew exponentially. Several authors have proposed that acetylation might be a key component in most eukaryotic signaling pathways, as important as phosphorylation. The enzymes involved in this process are starting to emerge; acetyltransferases and deacetylases are found inside and outside the nuclear compartment and have different regulatory functions. In trypanosomatids several of these enzymes have been described and are postulated to be novel antiparasitic targets for the rational design of drugs. In this paper we overview the most important known acetylated proteins and the advances made in the identification of new acetylated proteins using high-resolution mass spectrometry.
    [Show full text]
  • Data-Driven Insights Into Ligands, Proteins, and Genetic Mutations
    Data-Driven Insights into Ligands, Proteins, and Genetic Mutations by Jing Lu A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy (Bioinformatics) in the University of Michigan 2016 Doctoral Committee: Professor Heather A. Carlson, Chair Professor Charles L. Brooks III Assistant Professor Barry Grant Professor David S. Sept Professor Kerby A. Shedden © Jing Lu, 2016 Acknowledgements I would like to thank my advisor, Dr. Heather Carlson, for years of patient guidance, teaching, and support through the course of my PhD. I have learnt how to think critically and be rigorous in every step of research. I also want to express gratitude to my committee: Professor Charles L. Brooks III, Assistant Professor Barry Grant, Professor David S. Sept, Professor Kerby A. Shedden. Their advising is insightful and deepens my understanding of my research projects. I would like to thank Dr. Richard Smith for timely support for both my writing and research. For many Saturdays and Sundays, he promptly responds my requests for proofreading. Much of my work is built on his code in protein and ligand analysis. I would like to thank other members in Dr. Carlson’s lab for helping me with my work. Through the discussion with Dr. Jim Dunbar, I have learnt many critical ideas in Cheminformatics. Also, thank you to Sarah Graham and Jordan Clark for their tremendous friendship and willing to help with my writing. I would also thank previous members in Dr. Carlson’s lab. I would thank Dr. Phani Ghanakota for many late-night discussions and Dr.
    [Show full text]
  • Chemistry of Acetyl Transfer by Histone Modifying Enzymes: Structure, Mechanism and Implications for Effector Design
    Oncogene (2007) 26, 5528–5540 & 2007 Nature Publishing Group All rights reserved 0950-9232/07 $30.00 www.nature.com/onc REVIEW Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design SC Hodawadekar and R Marmorstein The Wistar Institute and The Department of Chemistry, University of Pennsylvania, Philadelphia, PA, USA The post-translational modification of histones plays an remodeling proteins that mobilize the histone proteins important role in chromatin regulation, a process that within chromatin (Varga-Weisz and Becker, 2006); insures the fidelity of gene expression and other DNA histone chaperone proteins that assemble, disassemble transactions. Of the enzymes that mediate post-transla- or replace variant histones within chromatin (Loyola tion modification, the histone acetyltransferase (HAT) and Almouzni, 2004); and post-translational modifica- and histone deacetylase (HDAC) proteins that add and tion enzymes that add or remove functional groups to or remove acetyl groups to and from target lysine residues from the histone proteins (Nightingale et al., 2006). within histones, respectively, have been the most exten- The post-translational modifications of histones sively studied at both the functional and structural levels. involve the addition or removal of acetyl, methyl or Not surprisingly, the aberrant activity of several of these phosphate groups as well as the reversible transfer of the enzymes have been implicated in human diseases such as ubiquitin and sumo proteins.
    [Show full text]
  • European Patent Office U.S. Patent and Trademark Office
    EUROPEAN PATENT OFFICE U.S. PATENT AND TRADEMARK OFFICE CPC NOTICE OF CHANGES 89 DATE: JULY 1, 2015 PROJECT RP0098 The following classification changes will be effected by this Notice of Changes: Action Subclass Group(s) Symbols deleted: C12Y 101/01063 C12Y 101/01128 C12Y 101/01161 C12Y 102/0104 C12Y 102/03011 C12Y 103/01004 C12Y 103/0103 C12Y 103/01052 C12Y 103/99007 C12Y 103/9901 C12Y 103/99013 C12Y 103/99021 C12Y 105/99001 C12Y 105/99002 C12Y 113/11013 C12Y 113/12012 C12Y 114/15002 C12Y 114/99028 C12Y 204/01119 C12Y 402/01052 C12Y 402/01058 C12Y 402/0106 C12Y 402/01061 C12Y 601/01025 C12Y 603/02027 Symbols newly created: C12Y 101/01318 C12Y 101/01319 C12Y 101/0132 C12Y 101/01321 C12Y 101/01322 C12Y 101/01323 C12Y 101/01324 C12Y 101/01325 C12Y 101/01326 C12Y 101/01327 C12Y 101/01328 C12Y 101/01329 C12Y 101/0133 C12Y 101/01331 C12Y 101/01332 C12Y 101/01333 CPC Form – v.4 CPC NOTICE OF CHANGES 89 DATE: JULY 1, 2015 PROJECT RP0098 Action Subclass Group(s) C12Y 101/01334 C12Y 101/01335 C12Y 101/01336 C12Y 101/01337 C12Y 101/01338 C12Y 101/01339 C12Y 101/0134 C12Y 101/01341 C12Y 101/01342 C12Y 101/03043 C12Y 101/03044 C12Y 101/98003 C12Y 101/99038 C12Y 102/01083 C12Y 102/01084 C12Y 102/01085 C12Y 102/01086 C12Y 103/01092 C12Y 103/01093 C12Y 103/01094 C12Y 103/01095 C12Y 103/01096 C12Y 103/01097 C12Y 103/0701 C12Y 103/08003 C12Y 103/08004 C12Y 103/08005 C12Y 103/08006 C12Y 103/08007 C12Y 103/08008 C12Y 103/08009 C12Y 103/99032 C12Y 104/01023 C12Y 104/01024 C12Y 104/03024 C12Y 105/01043 C12Y 105/01044 C12Y 105/01045 C12Y 105/03019 C12Y 105/0302
    [Show full text]
  • Source: the Arabidopsis Information Resource (TAIR);
    Table S1 List of targeted loci and information about their function in Arabidopsis thaliana (source: The Arabidopsis Information Resource (TAIR); https://www.arabidopsis.org/tools/bulk/genes/index.jsp). Locus Gene Model Gene Model Description Gene Model Primary Gene Symbol All Gene Symbols Identifier Name Type AT1G78800 AT1G78800.1 UDP-Glycosyltransferase superfamily protein_coding protein;(source:Araport11) AT5G06830 AT5G06830.1 hypothetical protein;(source:Araport11) protein_coding AT2G31740 AT2G31740.1 S-adenosyl-L-methionine-dependent methyltransferases protein_coding superfamily protein;(source:Araport11) AT5G11960 AT5G11960.1 magnesium transporter, putative protein_coding (DUF803);(source:Araport11) AT4G00560 AT4G00560.4 NAD(P)-binding Rossmann-fold superfamily protein_coding protein;(source:Araport11) AT1G80510 AT1G80510.1 Encodes a close relative of the amino acid transporter ANT1 protein_coding (AT3G11900). AT2G21250 AT2G21250.1 NAD(P)-linked oxidoreductase superfamily protein_coding protein;(source:Araport11) AT5G04420 AT5G04420.1 Galactose oxidase/kelch repeat superfamily protein_coding protein;(source:Araport11) AT4G34910 AT4G34910.1 P-loop containing nucleoside triphosphate hydrolases protein_coding superfamily protein;(source:Araport11) AT5G66120 AT5G66120.2 3-dehydroquinate synthase;(source:Araport11) protein_coding AT1G45110 AT1G45110.1 Tetrapyrrole (Corrin/Porphyrin) protein_coding Methylase;(source:Araport11) AT1G67420 AT1G67420.2 Zn-dependent exopeptidases superfamily protein_coding protein;(source:Araport11) AT3G62370
    [Show full text]
  • The Ubiquitin-Proteasome System in Spongiform Degenerative Disorders Brandi R
    The ubiquitin-proteasome system in spongiform degenerative disorders Brandi R. Whatley, Lian Li, Lih-Shen Chin To cite this version: Brandi R. Whatley, Lian Li, Lih-Shen Chin. The ubiquitin-proteasome system in spongiform degen- erative disorders. Biochimica et Biophysica Acta - Molecular Basis of Disease, Elsevier, 2008, 1782 (12), pp.700. 10.1016/j.bbadis.2008.08.006. hal-00562851 HAL Id: hal-00562851 https://hal.archives-ouvertes.fr/hal-00562851 Submitted on 4 Feb 2011 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. ÔØ ÅÒÙ×Ö ÔØ The ubiquitin-proteasome system in spongiform degenerative disorders Brandi R. Whatley, Lian Li, Lih-Shen Chin PII: S0925-4439(08)00159-2 DOI: doi: 10.1016/j.bbadis.2008.08.006 Reference: BBADIS 62842 To appear in: BBA - Molecular Basis of Disease Received date: 1 April 2008 Revised date: 13 August 2008 Accepted date: 15 August 2008 Please cite this article as: Brandi R. Whatley, Lian Li, Lih-Shen Chin, The ubiquitin- proteasome system in spongiform degenerative disorders, BBA - Molecular Basis of Disease (2008), doi: 10.1016/j.bbadis.2008.08.006 This is a PDF file of an unedited manuscript that has been accepted for publication.
    [Show full text]
  • Adenine Aminohydrolase: Occurrence and Possible Significance in Trypanosomid Flagellates (Crithidia/Leishmania/ Coformycin/Deoxycoformycin) G
    Proc. Natl. Acad. Sci. USA Vol. 76, No. 8, pp. 3670-3672, August 1979 Biochemistry Adenine aminohydrolase: Occurrence and possible significance in trypanosomid flagellates (Crithidia/Leishmania/ coformycin/deoxycoformycin) G. W. KIDDER AND LINDA L. NOLAN Biological Laboratory, Amherst College, Amherst, Massachusetts 01002 Communicated by William Trager, May 7, 1979 ABSTRACT Adenine aminohydrolase (EC 3.5.4.2) from four -C. fasciculata was grown in the defined medium of Kidder species of Leishmania and from Crithidia fasciculata was ex- and Dutta (5), in low profile flasks when large amounts of tissue amined for specific activities, affinity for substrate (adenine), were needed or in side-arm Nephelo flasks (Bellco, Vineland, and stability to heat. All were found to be strongly and non- competitively inhibited by both coformycin and deoxyco- NJ) or 25 X 125 mm optically clear tubes for the growth studies. formycin, two tight-binding inhibitors-of adenosine deaminase Growth was followed by reading optical densities at 650 nm, (adenosine aminohydrolase, EC 3.5.4.4). Deoxycoformycin is with uninoculated medium as the standard. In all cases hemin, the more potent inhibitor of the two. Neither inhibitor was ac- glucose, and inhibitors (if any) were filter sterilized and added tive against the purine phosphoribosyltransferases. When de- to the bulk of the heat-sterilized medium. oxycoformycin was added to the defined growth medium con- L. tarentolae was grown in low profile flasks in heat-sterilized taining hypoxanthine as the purine source, the. growth of C. Beef-Heart Infusion (Difco) to which fasciculata was unaffected, but when adenine was the purine filter-sterilized hemin (6 source for the organism, severe inhibition resulted.
    [Show full text]
  • Protein T1 C1 Accession No. Description
    Protein T1 C1 Accession No. Description SW:143B_HUMAN + + P31946 14-3-3 protein beta/alpha (protein kinase c inhibitor protein-1) (kcip-1) (protein 1054). 14-3-3 protein epsilon (mitochondrial import stimulation factor l subunit) (protein SW:143E_HUMAN + + P42655 P29360 Q63631 kinase c inhibitor protein-1) (kcip-1) (14-3-3e). SW:143S_HUMAN + - P31947 14-3-3 protein sigma (stratifin) (epithelial cell marker protein 1). SW:143T_HUMAN + - P27348 14-3-3 protein tau (14-3-3 protein theta) (14-3-3 protein t-cell) (hs1 protein). 14-3-3 protein zeta/delta (protein kinase c inhibitor protein-1) (kcip-1) (factor SW:143Z_HUMAN + + P29312 P29213 activating exoenzyme s) (fas). P01889 Q29638 Q29681 Q29854 Q29861 Q31613 hla class i histocompatibility antigen, b-7 alpha chain precursor (mhc class i antigen SW:1B07_HUMAN + - Q9GIX1 Q9TP95 b*7). hla class i histocompatibility antigen, b-14 alpha chain precursor (mhc class i antigen SW:1B14_HUMAN + - P30462 O02862 P30463 b*14). P30479 O19595 Q29848 hla class i histocompatibility antigen, b-41 alpha chain precursor (mhc class i antigen SW:1B41_HUMAN + - Q9MY79 Q9MY94 b*41) (bw-41). hla class i histocompatibility antigen, b-42 alpha chain precursor (mhc class i antigen SW:1B42_HUMAN + - P30480 P79555 b*42). P30488 O19615 O19624 O19641 O19783 O46702 hla class i histocompatibility antigen, b-50 alpha chain precursor (mhc class i antigen SW:1B50_HUMAN + - O78172 Q9TQG1 b*50) (bw-50) (b-21). hla class i histocompatibility antigen, b-54 alpha chain precursor (mhc class i antigen SW:1B54_HUMAN + - P30492 Q9TPQ9 b*54) (bw-54) (bw-22). P30495 O19758 P30496 hla class i histocompatibility antigen, b-56 alpha chain precursor (mhc class i antigen SW:1B56_HUMAN - + P79490 Q9GIM3 Q9GJ17 b*56) (bw-56) (bw-22).
    [Show full text]
  • Genome Wide Analysis Identifies Sphingolipid Metabolism As a New Target of Valproic Acid" (2016)
    Wayne State University Wayne State University Dissertations 1-1-2016 Genome Wide Analysis Identifies phinS golipid Metabolism As A New Target Of Valproic Acid Shyamalagauri Jadhav Jadhav Wayne State University, Follow this and additional works at: https://digitalcommons.wayne.edu/oa_dissertations Part of the Biology Commons, and the Molecular Biology Commons Recommended Citation Jadhav, Shyamalagauri Jadhav, "Genome Wide Analysis Identifies Sphingolipid Metabolism As A New Target Of Valproic Acid" (2016). Wayne State University Dissertations. 1545. https://digitalcommons.wayne.edu/oa_dissertations/1545 This Open Access Dissertation is brought to you for free and open access by DigitalCommons@WayneState. It has been accepted for inclusion in Wayne State University Dissertations by an authorized administrator of DigitalCommons@WayneState. GENOME WIDE ANALYSIS IDENTIFIES SPHINGOLIPID METABOLISM AS A NEW TARGET OF VALPROIC ACID by SHYAMALAGAURI JADHAV DISSERTATION Submitted to the Graduate School of Wayne State University, Detroit, Michigan In partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY 2016 MAJOR: BIOLOGICAL SCIENCES Approved By: _____________________________ Advisor Date _____________________________ _____________________________ _____________________________ ©COPYRIGHT BY SHYAMALAGAURI JADHAV 2016 All Rights Reserved DEDICATION I would like to dedicate my dissertation to my late mother Chandrakala Jadhav who was a constant support and inspiration through the years. ii ACKNOWLEDGEMENTS First and foremost I would like to thank my advisor, Dr. Miriam L. Greenberg for her intellectual, moral, financial, and emotional support throughout my graduate journey. The realization of this thesis would have been impossible without her constant encouragement and strong support. I would like to thank her for the confidence she had in my ability to think and design the project through; and for her guidance when needed.
    [Show full text]
  • The Role of Endocannabinoid System Based on Mrna Expression During the Late Luteal Phase and Estrus in the Bovine Endometrium
    Ann. Anim. Sci., Vol. 19, No. 4 (2019) 979–989 DOI: 10.2478/aoas-2019-0044 THE ROLE OF ENDOCANNABINOID SYSTEM BASED ON mRNA EXPRESSION DURING THE LATE LUTEAL PHASE AND ESTRUS IN THE BOVINE ENDOMETRIUM Essa Dirandeh♦, Zarbakht Ansari-Pirsaraei, Hamid Deldar Department of Animal Science, Sari Agricultural Sciences and Natural Resources University, P.O. Box 578, Sari, Mazandaran, Iran ♦Corresponding author: [email protected] Abstract There are several findings indicating that the endocannabinoid system (ECS) is an important fac- tor, acting in multiple ways in regulating reproductive function but changes of this system in the bovine endometrium have rarely been investigated; therefore, this study was designed to consider an association between endometrial ECS expression and different stages of the estrous cycles. MRNA expressions of the ECS were investigated during the late luteal phase and estrus using real-time PCR. Following estrous synchronization of sixteen Holstein dairy cows (34±1.3 kg/day of milk production), using two PGF2α injections given 14 days apart, at 30 and 44 days in milk (DIM), blood samples and ultrasonography (US) were performed every other day from the day of second PGF2α injection (44 DIM) until the start of the next estrous cycle (67±2 DIM) to verify CL development and ovulation. Based on blood and US results endometrial tissue was collected on days 16 (late luteal phase) and 21 (estrus) of the synchronized estrous cycle (ovulation = d 0). Real-time PCR analysis of ECS mRNA expression revealed endocannabinoid receptor (CNR2), diacylglycerol lipase (DAGL), cyclooxygenase-2 (COX-2), fatty acid amide hydrolase (FAAH) and monoglyceride lipase (MGLL) had significant fold differences when comparing two different stages of the estrous cycle (late luteal phase vs.
    [Show full text]