PDF Download

Total Page：16

File Type：pdf, Size：1020Kb

S100A6 (ABT-S100A6) mouse mAb Ready to use Catalog No : YM6668R Reactivity : Human, Mouse Applications : IHC-p,IF(paraffin section) Gene Name : S100A6 CACY Protein Name : S100A6 Human Gene Id : 6277 Human Swiss Prot P06703 No : Immunogen : Synthesized peptide derived from human S100A6 Specificity : This antibody detects endogenous levels of human S100A6. Heat-induced epitope retrieval (HIER) TRIS-EDTA of pH8.0 was highly recommended as antigen repair method in paraffin section Formulation : Liquid in PBS containing, 0.5% BSA and 0.02% sodium azide. Source : Mouse/IgG1, Kappa Dilution : Ready to use for IHC-p Purification : The antibody was affinity-purified from mouse ascites by affinity- chromatography using specific immunogen. Storage Stability : 4°C/ 1 years Background : S100 calcium binding protein A6(S100A6) Homo sapiens The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in stimulation of Ca2+-dependent insulin release, stimulation of prolactin secretion, and exocytosis. Chromosomal rearrangements 1 / 2 and altered expression of this gene have been implicated in melanoma. [provided by RefSeq, Jul 2008], Function : induction:Preferentially expressed when quiescent fibroblasts are stimulated to proliferate. It is inducible by growth factors and overexpressed in acute myeloid leukemias.,miscellaneous:This protein co-purified with the prolactin receptor.,PTM:The N-terminus is blocked.,similarity:Belongs to the S-100 family.,similarity:Contains 2 EF-hand domains.,subunit:Homodimer, antiparallel. Interacts with SUGT1., Subcellular Nuclear, Cytoplasmic Location : Expression : Brain,Fibroblast,Placenta,Platelet, Products Images 2 / 2 Powered by TCPDF (www.tcpdf.org).

Copy Link

Recommended publications

Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino-Like Mouse Models: Tracking the Role of the Hairless Gene
University of Tennessee, Knoxville TRACE: Tennessee Research and Creative Exchange Doctoral Dissertations Graduate School 5-2006 Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino-like Mouse Models: Tracking the Role of the Hairless Gene Yutao Liu University of Tennessee - Knoxville Follow this and additional works at: https://trace.tennessee.edu/utk_graddiss Part of the Life Sciences Commons Recommended Citation Liu, Yutao, "Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino- like Mouse Models: Tracking the Role of the Hairless Gene. " PhD diss., University of Tennessee, 2006. https://trace.tennessee.edu/utk_graddiss/1824 This Dissertation is brought to you for free and open access by the Graduate School at TRACE: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of TRACE: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. To the Graduate Council: I am submitting herewith a dissertation written by Yutao Liu entitled "Molecular and Physiological Basis for Hair Loss in Near Naked Hairless and Oak Ridge Rhino-like Mouse Models: Tracking the Role of the Hairless Gene." I have examined the final electronic copy of this dissertation for form and content and recommend that it be accepted in partial fulfillment of the requirements for the degree of Doctor of Philosophy, with a major in Life Sciences. Brynn H. Voy, Major Professor We have read this dissertation and recommend its acceptance: Naima Moustaid-Moussa, Yisong Wang, Rogert Hettich Accepted for the Council: Carolyn R.
[Show full text]
Peripherally Generated Foxp3+ Regulatory T Cells Mediate the Immunomodulatory Effects of Ivig in Allergic Airways Disease
Peripherally Generated Foxp3+ Regulatory T Cells Mediate the Immunomodulatory Effects of IVIg in Allergic Airways Disease This information is current as Amir H. Massoud, Gabriel N. Kaufman, Di Xue, Marianne of September 26, 2021. Béland, Marieme Dembele, Ciriaco A. Piccirillo, Walid Mourad and Bruce D. Mazer J Immunol published online 20 February 2017 http://www.jimmunol.org/content/early/2017/02/18/jimmun ol.1502361 Downloaded from Supplementary http://www.jimmunol.org/content/suppl/2017/02/18/jimmunol.150236 Material 1.DCSupplemental http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on September 26, 2021 *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 © 2017 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. Published February 20, 2017, doi:10.4049/jimmunol.1502361 The Journal of Immunology Peripherally Generated Foxp3+ Regulatory T Cells Mediate the Immunomodulatory Effects of IVIg in Allergic Airways Disease Amir H. Massoud,*,†,1 Gabriel N. Kaufman,* Di Xue,* Marianne Be´land,* Marieme Dembele,* Ciriaco A.
[Show full text]
1 Supporting Information for a Microrna Network Regulates
Supporting Information for A microRNA Network Regulates Expression and Biosynthesis of CFTR and CFTR-ΔF508 Shyam Ramachandrana,b, Philip H. Karpc, Peng Jiangc, Lynda S. Ostedgaardc, Amy E. Walza, John T. Fishere, Shaf Keshavjeeh, Kim A. Lennoxi, Ashley M. Jacobii, Scott D. Rosei, Mark A. Behlkei, Michael J. Welshb,c,d,g, Yi Xingb,c,f, Paul B. McCray Jr.a,b,c Author Affiliations: Department of Pediatricsa, Interdisciplinary Program in Geneticsb, Departments of Internal Medicinec, Molecular Physiology and Biophysicsd, Anatomy and Cell Biologye, Biomedical Engineeringf, Howard Hughes Medical Instituteg, Carver College of Medicine, University of Iowa, Iowa City, IA-52242 Division of Thoracic Surgeryh, Toronto General Hospital, University Health Network, University of Toronto, Toronto, Canada-M5G 2C4 Integrated DNA Technologiesi, Coralville, IA-52241 To whom correspondence should be addressed: Email: [email protected] (M.J.W.); yi- [email protected] (Y.X.); Email: [email protected] (P.B.M.) This PDF file includes: Materials and Methods References Fig. S1. miR-138 regulates SIN3A in a dose-dependent and site-specific manner. Fig. S2. miR-138 regulates endogenous SIN3A protein expression. Fig. S3. miR-138 regulates endogenous CFTR protein expression in Calu-3 cells. Fig. S4. miR-138 regulates endogenous CFTR protein expression in primary human airway epithelia. Fig. S5. miR-138 regulates CFTR expression in HeLa cells. Fig. S6. miR-138 regulates CFTR expression in HEK293T cells. Fig. S7. HeLa cells exhibit CFTR channel activity. Fig. S8. miR-138 improves CFTR processing. Fig. S9. miR-138 improves CFTR-ΔF508 processing. Fig. S10. SIN3A inhibition yields partial rescue of Cl- transport in CF epithelia.
[Show full text]
2020 Program Book
PROGRAM BOOK Note that TAGC was cancelled and held online with a different schedule and program. This document serves as a record of the original program designed for the in-person meeting. April 22–26, 2020 Gaylord National Resort & Convention Center Metro Washington, DC TABLE OF CONTENTS About the GSA ........................................................................................................................................................ 3 Conference Organizers ...........................................................................................................................................4 General Information ...............................................................................................................................................7 Mobile App ....................................................................................................................................................7 Registration, Badges, and Pre-ordered T-shirts .............................................................................................7 Oral Presenters: Speaker Ready Room - Camellia 4.......................................................................................7 Poster Sessions and Exhibits - Prince George’s Exhibition Hall ......................................................................7 GSA Central - Booth 520 ................................................................................................................................8 Internet Access ..............................................................................................................................................8
[Show full text]
S41467-020-18249-3.Pdf
ARTICLE https://doi.org/10.1038/s41467-020-18249-3 OPEN Pharmacologically reversible zonation-dependent endothelial cell transcriptomic changes with neurodegenerative disease associations in the aged brain Lei Zhao1,2,17, Zhongqi Li 1,2,17, Joaquim S. L. Vong2,3,17, Xinyi Chen1,2, Hei-Ming Lai1,2,4,5,6, Leo Y. C. Yan1,2, Junzhe Huang1,2, Samuel K. H. Sy1,2,7, Xiaoyu Tian 8, Yu Huang 8, Ho Yin Edwin Chan5,9, Hon-Cheong So6,8, ✉ ✉ Wai-Lung Ng 10, Yamei Tang11, Wei-Jye Lin12,13, Vincent C. T. Mok1,5,6,14,15 &HoKo 1,2,4,5,6,8,14,16 1234567890():,; The molecular signatures of cells in the brain have been revealed in unprecedented detail, yet the ageing-associated genome-wide expression changes that may contribute to neurovas- cular dysfunction in neurodegenerative diseases remain elusive. Here, we report zonation- dependent transcriptomic changes in aged mouse brain endothelial cells (ECs), which pro- minently implicate altered immune/cytokine signaling in ECs of all vascular segments, and functional changes impacting the blood–brain barrier (BBB) and glucose/energy metabolism especially in capillary ECs (capECs). An overrepresentation of Alzheimer disease (AD) GWAS genes is evident among the human orthologs of the differentially expressed genes of aged capECs, while comparative analysis revealed a subset of concordantly downregulated, functionally important genes in human AD brains. Treatment with exenatide, a glucagon-like peptide-1 receptor agonist, strongly reverses aged mouse brain EC transcriptomic changes and BBB leakage, with associated attenuation of microglial priming. We thus revealed tran- scriptomic alterations underlying brain EC ageing that are complex yet pharmacologically reversible.
[Show full text]
The UVB-Induced Gene Expression Profile of Human Epidermis in Vivo Is Different from That of Cultured Keratinocytes
Oncogene (2006) 25, 2601–2614 & 2006 Nature Publishing Group All rights reserved 0950-9232/06 $30.00 www.nature.com/onc ORIGINAL ARTICLE The UVB-induced gene expression proﬁle of human epidermis in vivo is different from that of cultured keratinocytes CD Enk1, J Jacob-Hirsch2, H Gal3, I Verbovetski4, N Amariglio2, D Mevorach4, A Ingber1, D Givol3, G Rechavi2 and M Hochberg1 1Department of Dermatology, The Hadassah-Hebrew University Medical Center, Jerusalem, Israel; 2Department of Pediatric Hemato-Oncology and Functional Genomics, Safra Children’s Hospital, Sheba Medical Center and Sackler School of Medicine, Tel-Aviv University,Tel Aviv, Israel; 3Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot, Israel and 4The Laboratory for Cellular and Molecular Immunology, Department of Medicine, The Hadassah-Hebrew University Medical Center, Jerusalem, Israel In order to obtain a comprehensive picture of the radiation. UVB, with a wavelength range between 290 molecular events regulating cutaneous photodamage of and 320 nm, represents one of the most important intact human epidermis, suction blister roofs obtained environmental hazards affectinghuman skin (Hahn after a single dose of in vivo ultraviolet (UV)B exposure and Weinberg, 2002). To protect itself against the were used for microarray proﬁling. We found a changed DNA-damaging effects of sunlight, the skin disposes expression of 619 genes. Half of the UVB-regulated genes over highly complicated cellular programs, including had returned to pre-exposure baseline levels at 72 h, cell-cycle arrest, DNA repair and apoptosis (Brash et al., underscoring the transient character of the molecular 1996). Failure in selected elements of these defensive cutaneous UVB response.
[Show full text]
The Landscape of Human Mutually Exclusive Splicing
bioRxiv preprint doi: https://doi.org/10.1101/133215; this version posted May 2, 2017. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-ND 4.0 International license. The landscape of human mutually exclusive splicing Klas Hatje1,2,#,*, Ramon O. Vidal2,*, Raza-Ur Rahman2, Dominic Simm1,3, Björn Hammesfahr1,$, Orr Shomroni2, Stefan Bonn2§ & Martin Kollmar1§ 1 Group of Systems Biology of Motor Proteins, Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany 2 Group of Computational Systems Biology, German Center for Neurodegenerative Diseases, Göttingen, Germany 3 Theoretical Computer Science and Algorithmic Methods, Institute of Computer Science, Georg-August-University Göttingen, Germany § Corresponding authors # Current address: Roche Pharmaceutical Research and Early Development, Pharmaceutical Sciences, Roche Innovation Center Basel, F. Hoffmann-La Roche Ltd., Basel, Switzerland $ Current address: Research and Development - Data Management (RD-DM), KWS SAAT SE, Einbeck, Germany * These authors contributed equally E-mail addresses: KH: [email protected], RV: [email protected], RR: [email protected], DS: [email protected], BH: [email protected], OS: [email protected], SB: [email protected], MK: [email protected] - 1 - bioRxiv preprint doi: https://doi.org/10.1101/133215; this version posted May 2, 2017. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity.
[Show full text]
S100A6 and Its Brain Ligands in Neurodegenerative Disorders
International Journal of Molecular Sciences Review S100A6 and Its Brain Ligands in Neurodegenerative Disorders Anna Filipek * and Wiesława Le´sniak Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Street, 02-093 Warsaw, Poland; [email protected] * Correspondence: a.fi[email protected] Received: 13 May 2020; Accepted: 29 May 2020; Published: 1 June 2020 Abstract: The S100A6 protein is present in different mammalian cells and tissues including the brain. It binds Ca2+ and Zn2+ and interacts with many target proteins/ligands. The best characterized ligands of S100A6, expressed at high level in the brain, include CacyBP/SIP and Sgt1. Research concerning the functional role of S100A6 and these two ligands indicates that they are involved in various signaling pathways that regulate cell proliferation, differentiation, cytoskeletal organization, and others. In this review, we focused on the expression/localization of these proteins in the brain and on their possible role in neurodegenerative diseases. Published results demonstrate that S100A6, CacyBP/SIP, and Sgt1 are expressed in various brain structures and in the spinal cord and can be found in different cell types including neurons and astrocytes. When it comes to their possible involvement in nervous system pathology, it is evident that their expression/level and/or subcellular localization is changed when compared to normal conditions. Among diseases in which such changes have been observed are Alzheimer’s disease (AD), amyotrophic lateral sclerosis (ALS), epileptogenesis, Parkinson’s disease (PD), Huntington’s disease (HD), and others. Keywords: S100A6; CacyBP/SIP; Sgt1; neurodegeneration; β amyloid plaques; neurofibrillary tangles; Lewy bodies 1.
[Show full text]
Downloaded from the UCSC Genome of This Alu Exon Is Under Dynamic Regulation in Human Browser Database [53]
UCLA UCLA Previously Published Works Title The contribution of Alu exons to the human proteome. Permalink https://escholarship.org/uc/item/12m2d462 Journal Genome biology, 17(1) ISSN 1474-7596 Authors Lin, Lan Jiang, Peng Park, Juw Won et al. Publication Date 2016-01-28 DOI 10.1186/s13059-016-0876-5 Peer reviewed eScholarship.org Powered by the California Digital Library University of California Lin et al. Genome Biology (2016) 17:15 DOI 10.1186/s13059-016-0876-5 RESEARCH Open Access The contribution of Alu exons to the human proteome Lan Lin1*†, Peng Jiang2†, Juw Won Park1,3,4†, Jinkai Wang1†, Zhi-xiang Lu1, Maggie P. Y. Lam5, Peipei Ping5,6 and Yi Xing1* Abstract Background: Alu elements are major contributors to lineage-specific new exons in primate and human genomes. Recent studies indicate that some Alu exons have high transcript inclusion levels or tissue-specific splicing profiles, and may play important regulatory roles in modulating mRNA degradation or translational efficiency. However, the contribution of Alu exons to the human proteome remains unclear and controversial. The prevailing view is that exons derived from young repetitive elements, such as Alu elements, are restricted to regulatory functions and have not had adequate evolutionary time to be incorporated into stable, functional proteins. Results: We adopt a proteotranscriptomics approach to systematically assess the contribution of Alu exons to the human proteome. Using RNA sequencing, ribosome profiling, and proteomics data from human tissues and cell lines, we provide evidence for the translational activities of Alu exons and the presence of Alu exon derived peptides in human proteins.
[Show full text]
S100A6, a Calcium- and Zinc-Binding Protein, Is Overexpressed in SOD1 Mutant Mice, a Model for Amyotrophic Lateral Sclerosis
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Biochimica et Biophysica Acta 1498 (2000) 264^272 www.elsevier.com/locate/bba S100A6, a calcium- and zinc-binding protein, is overexpressed in SOD1 mutant mice, a model for amyotrophic lateral sclerosis Daphne¨ Hoyaux a, Jules Alao a, Julia Fuchs b, Robert Kiss a, Bernhard Keller b, Claus W. Heizmann c, Roland Pochet a;*, Detlev Frermann a; b a Laboratory of Histopathology, Faculty of Medicine, Universite¨ Libre de Bruxelles, CP 620, 808 route de Lennik, 1070 Brussels, Belgium b Center of Physiology, Department of Neuro- and Sense Physiology, University of Go«ttingen, Go«ttingen, Germany c Division of Clinical Chemistry and Biochemistry, Department of Pediatrics, University of Zu«rich, Zu«rich, Switzerland Received 11 September 2000; accepted 12 September 2000 Abstract Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterised by selective degeneration of motoneurones. Familial ALS is an age-dependent autosomal dominant disorder in which mutations in the homodimeric enzyme Cu/Zn superoxide dismutase 1 (SOD1) is linked to the disease. An animal model for this disease is a transgenic mouse expressing the mutated human SOD1G93A gene. Recent electrophysiological data emphasised that the striking selective vulnerability of motoneurones might be due to their differential calcium buffering capacities. Therefore we have investigated, using immunohistochemistry, the expression of different calcium binding proteins in brainstem and spinal cord from normal and SOD1 mutated mice. Among the 13 calcium-binding proteins screened, only one, S100A6, a homodimeric calcium- binding protein able to bind four Zn2, appeared to be highly expressed in the SOD1 mutated mice.
[Show full text]
Development of Novel Analysis and Data Integration Systems to Understand Human Gene Regulation
Development of novel analysis and data integration systems to understand human gene regulation Dissertation zur Erlangung des Doktorgrades Dr. rer. nat. der FakultätfürMathematik und Informatik der Georg-August-UniversitätGöttingen im PhD Programme in Computer Science (PCS) der Georg-August University School of Science (GAUSS) vorgelegt von Raza-Ur Rahman aus Pakistan Göttingen,April 2018 Prof. Dr. Stefan Bonn, Zentrum fürMolekulare Neurobiologie (ZMNH), Betreuungsausschuss: Institut fürMedizinische Systembiologie, Hamburg Prof. Dr. Tim Beißbarth, Institut fürMedizinische Statistik, Universitätsmedizin, Georg-August Universität,Göttingen Prof. Dr. Burkhard Morgenstern, Institut fürMikrobiologie und Genetik Abtl. Bioinformatik, Georg-August Universität,Göttingen Prüfungskommission: Prof. Dr. Stefan Bonn, Zentrum fürMolekulare Neurobiologie (ZMNH), Referent: Institut fürMedizinische Systembiologie, Hamburg Prof. Dr. Tim Beißbarth, Institut fürMedizinische Statistik, Universitätsmedizin, Korreferent: Georg-August Universität,Göttingen Prof. Dr. Burkhard Morgenstern, Weitere Mitglieder Institut fürMikrobiologie und Genetik Abtl. Bioinformatik, der Prüfungskommission: Georg-August Universität,Göttingen Prof. Dr. Carsten Damm, Institut fürInformatik, Georg-August Universität,Göttingen Prof. Dr. Florentin Wörgötter, Physikalisches Institut Biophysik, Georg-August-Universität,Göttingen Prof. Dr. Stephan Waack, Institut fürInformatik, Georg-August Universität,Göttingen Tag der mündlichen Prüfung: der 30. März2018
[Show full text]
Zimmer Cell Calcium 2013 Mammalian S100 Evolution.Pdf
Cell Calcium 53 (2013) 170–179 Contents lists available at SciVerse ScienceDirect Cell Calcium jo urnal homepage: www.elsevier.com/locate/ceca Evolution of the S100 family of calcium sensor proteins a,∗ b b,1 b Danna B. Zimmer , Jeannine O. Eubanks , Dhivya Ramakrishnan , Michael F. Criscitiello a Center for Biomolecular Therapeutics and Department of Biochemistry & Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, MD 20102, United States b Comparative Immunogenetics Laboratory, Department of Veterinary Pathobiology, College of Veterinary Medicine & Biomedical Sciences, Texas A&M University, College Station, TX 77843-4467, United States a r t i c l e i n f o a b s t r a c t 2+ Article history: The S100s are a large group of Ca sensors found exclusively in vertebrates. Transcriptomic and genomic Received 4 October 2012 data from the major radiations of mammals were used to derive the evolution of the mammalian Received in revised form 1 November 2012 S100s genes. In human and mouse, S100s and S100 fused-type proteins are in a separate clade from Accepted 3 November 2012 2+ other Ca sensor proteins, indicating that an ancient bifurcation between these two gene lineages Available online 14 December 2012 has occurred. Furthermore, the ﬁve genomic loci containing S100 genes have remained largely intact during the past 165 million years since the shared ancestor of egg-laying and placental mammals. Keywords: Nonetheless, interesting births and deaths of S100 genes have occurred during mammalian evolution. Mammals The S100A7 loci exhibited the most plasticity and phylogenetic analyses clariﬁed relationships between Phylogenetic analyses the S100A7 proteins encoded in the various mammalian genomes.
[Show full text]