Mouse Mol.Wt.: 48 Kda Panx1 Antibody

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#M040570 Panx1 Antibody Order 021-34695924 [email protected] Support 400-6123-828 50ul [email protected] 100 uL Web www.abmart.cn Description: The pannexin gene family encodes a second class of putative gap junction proteins and are highly conserved in invertebrates and mammals. Pannexins (Panx) are four-pass transmembrane proteins that oligomerize to form large pore ion and metabolite-permeable channels. Pannexin-1 (PANX1) and Pannexin-3 are closely related, while Pannexin-2 is a more distant relation. PANX1 is a transmembrane protein that forms a mechanosensitive ATP-permeable channel between adjacent cells and in the endoplasmic reticulum. PANX1 may play a role as a Ca2+ -leak channel to regulate ER Ca2+ homeostasis and regulates neural stem and progenitor cell proliferation. Uniprot: Q96RD7 Alternative Names： innexin; MRS1; Pannexin 1; Panx1; PX1; Specificity: Antibody detects endogenous levels of total PANX1. Reactivity: Human, Mouse, Rat Source: Mouse Mol.Wt.: 48 kDa Storage Condition: Store at -20 °C. Stable for 12 months from date of receipt. 1 For in vitro research use only and not intended for use in humans or animals. Application: WB 1:1000-1:2000；IHC/IF 1:100-1:1000 Western blot analysis of PANX1 expression in SH-SY5Y whole cell lysates, 其他推荐产品 #M20001 His-Tag (2A8) Mouse mAb #M20002 Myc-Tag (19C2) Mouse mAb #M20003 HA-Tag (26D11) Mouse mAb #M20004 GFP-Tag (7G9) Mouse mAb #M20007 GST-Tag (12G8) Mouse mAb #M20008 DYDDDDDK-Tag (3B9) Mouse mAb (Binds to same epitope as Sigma’s Anti- FLAG M2 Antibody) #M20012 Anti-Myc-Tag Mouse mAb (Agarose Conjugated) #M20013 Anti-HA-Tag Mouse mAb (Agarose Conjugated) #M20018 Anti-DYKDDDDK-Tag Mouse Antibody (Agarose Conjugated) (Same as Sigma’s Anti-FLAG M2) #M20118 Anti-DYKDDDDK-Tag Mouse Antibody (Magnetic Beads) (Same as Sigma’s Anti-FLAG M2) 2 For in vitro research use only and not intended for use in humans or animals. .

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Biochemical and Functional Analyses of PANX1 Variants
Western University Scholarship@Western Electronic Thesis and Dissertation Repository June 2019 Biochemical and Functional Analyses of PANX1 Variants Daniel Nouri Nejad The University of Western Ontario Supervisor Penuela, Silvia The University of Western Ontario Graduate Program in Anatomy and Cell Biology A thesis submitted in partial fulfillment of the equirr ements for the degree in Master of Science © Daniel Nouri Nejad 2019 Follow this and additional works at: https://ir.lib.uwo.ca/etd Part of the Molecular Biology Commons Recommended Citation Nouri Nejad, Daniel, "Biochemical and Functional Analyses of PANX1 Variants" (2019). Electronic Thesis and Dissertation Repository. 6230. https://ir.lib.uwo.ca/etd/6230 This Dissertation/Thesis is brought to you for free and open access by Scholarship@Western. It has been accepted for inclusion in Electronic Thesis and Dissertation Repository by an authorized administrator of Scholarship@Western. For more information, please contact [email protected]. Abstract Pannexin 1 (PANX1) is a glycoprotein capable of forming large-pore single- membrane channels permeable to signaling molecules such as ATP. In this study, we interrogated different domains by introducing naturally occurring variants reported in melanoma and assessed their impact on the channel function of PANX1 at the cell surface. From this, we discovered a novel tyrosine phosphorylation site at Tyr150, that when disrupted via a missense mutation resulted in hypo-glycosylation and a greater capacity to traffic to the cell-surface and enhanced dye uptake. We have also uncovered a highly conserved ancestral allele, Gln5His, that has a greater allele frequency than the derived allele Gln5 in global and cancer cohorts but was not associated with cancer aggressiveness.
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A High-Throughput Approach to Uncover Novel Roles of APOBEC2, a Functional Orphan of the AID/APOBEC Family
Rockefeller University Digital Commons @ RU Student Theses and Dissertations 2018 A High-Throughput Approach to Uncover Novel Roles of APOBEC2, a Functional Orphan of the AID/APOBEC Family Linda Molla Follow this and additional works at: https://digitalcommons.rockefeller.edu/ student_theses_and_dissertations Part of the Life Sciences Commons A HIGH-THROUGHPUT APPROACH TO UNCOVER NOVEL ROLES OF APOBEC2, A FUNCTIONAL ORPHAN OF THE AID/APOBEC FAMILY A Thesis Presented to the Faculty of The Rockefeller University in Partial Fulfillment of the Requirements for the degree of Doctor of Philosophy by Linda Molla June 2018 © Copyright by Linda Molla 2018 A HIGH-THROUGHPUT APPROACH TO UNCOVER NOVEL ROLES OF APOBEC2, A FUNCTIONAL ORPHAN OF THE AID/APOBEC FAMILY Linda Molla, Ph.D. The Rockefeller University 2018 APOBEC2 is a member of the AID/APOBEC cytidine deaminase family of proteins. Unlike most of AID/APOBEC, however, APOBEC2’s function remains elusive. Previous research has implicated APOBEC2 in diverse organisms and cellular processes such as muscle biology (in Mus musculus), regeneration (in Danio rerio), and development (in Xenopus laevis). APOBEC2 has also been implicated in cancer. However the enzymatic activity, substrate or physiological target(s) of APOBEC2 are unknown. For this thesis, I have combined Next Generation Sequencing (NGS) techniques with state-of-the-art molecular biology to determine the physiological targets of APOBEC2. Using a cell culture muscle differentiation system, and RNA sequencing (RNA-Seq) by polyA capture, I demonstrated that unlike the AID/APOBEC family member APOBEC1, APOBEC2 is not an RNA editor. Using the same system combined with enhanced Reduced Representation Bisulfite Sequencing (eRRBS) analyses I showed that, unlike the AID/APOBEC family member AID, APOBEC2 does not act as a 5-methyl-C deaminase.
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Single-Cell Dynamics of Pannexin-1- Facilitated Programmed ATP Loss
RESEARCH ARTICLE Single-cell dynamics of pannexin-1- facilitated programmed ATP loss during apoptosis Hiromi Imamura1†*, Shuichiro Sakamoto1†, Tomoki Yoshida1, Yusuke Matsui2, Silvia Penuela3, Dale W Laird3, Shin Mizukami4, Kazuya Kikuchi2, Akira Kakizuka1 1Graduate School of Biostudies, Kyoto University, Kyoto, Japan; 2Graduate School of Engineering, Osaka University, Suita, Japan; 3Department of Anatomy and Cell Biology, Schulich School of Medicine and Dentistry, University of Western Ontario, London, Canada; 4Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Sendai, Japan Abstract ATP is essential for all living cells. However, how dead cells lose ATP has not been well investigated. In this study, we developed new FRET biosensors for dual imaging of intracellular ATP level and caspase-3 activity in single apoptotic cultured human cells. We show that the cytosolic ATP level starts to decrease immediately after the activation of caspase-3, and this process is completed typically within 2 hr. The ATP decrease was facilitated by caspase-dependent cleavage of the plasma membrane channel pannexin-1, indicating that the intracellular decrease of the apoptotic cell is a ‘programmed’ process. Apoptotic cells deficient of pannexin-1 sustained the ability to produce ATP through glycolysis and to consume ATP, and did not stop wasting glucose much longer period than normal apoptotic cells. Thus, the pannexin-1 plays a role in arresting the metabolic activity of dead apoptotic cells, most likely through facilitating the loss of intracellular ATP. *For correspondence: [email protected] †These authors contributed equally to this work Introduction Competing interests: The Living cells require energy that is provided by the principal intracellular energy carrier, adenosine-tri- authors declare that no phosphate (ATP).
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Pannexins and Connexins: Their Relevance for Oocyte Developmental Competence
International Journal of Molecular Sciences Review Pannexins and Connexins: Their Relevance for Oocyte Developmental Competence Paweł Kordowitzki 1,2, Gabriela Sokołowska 3, Marta Wasielak-Politowska 4, Agnieszka Skowronska 5 and Mariusz T. Skowronski 2,* 1 Institute of Animal Reproduction and Food Research of Polish Academy of Sciences, Bydgoska Street 7, 10-243 Olsztyn, Poland; [email protected] 2 Department of Basic and Preclinical Sciences, Faculty of Biological and Veterinary Sciences, Nicolaus Copernicus University, Gagarina Street 7, 87-100 Torun, Poland 3 Department of Reproduction and Gynecological Endocrinology, Medical University of Bialystok, Jana KilińskiegoStreet 1, 15-089 Białystok, Poland; [email protected] 4 Center of Gynecology, Endocrinology and Reproductive Medicine—Artemida, JagiellońskaStreet 78, 10-357 Olsztyn, Poland; [email protected] 5 Department of Human Physiology and Pathophysiology, School of Medicine, Collegium Medicum, University of Warmia and Mazury, Warszawska Street 30, 10-357 Olsztyn, Poland; [email protected] * Correspondence: [email protected]; Tel.: +48-566-112-231 Abstract: The oocyte is the major determinant of embryo developmental competence in all mam- malian species. Although fundamental advances have been generated in the field of reproductive medicine and assisted reproductive technologies in the past three decades, researchers and clinicians are still trying to elucidate molecular factors and pathways, which could be pivotal for the oocyte’s developmental competence. The cell-to-cell and cell-to-matrix communications are crucial not only Citation: Kordowitzki, P.; for oocytes but also for multicellular organisms in general. This latter mentioned communication is Sokołowska, G.; Wasielak-Politowska, among others possibly due to the Connexin and Pannexin families of large-pore forming channels.
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Regulation of Neuroblastoma Malignant Properties by Pannexin 1 Channels: Role of Post-Translational Modifications and Mutations
Regulation of Neuroblastoma Malignant Properties by Pannexin 1 Channels: Role of Post-Translational Modifications and Mutations Stephen Henry Holland A thesis submitted in partial fulfillment of the requirements for the Master’s degree in Science specializing in Cellular Molecular Medicine Department of Cellular Molecular Medicine Faculty of Medicine University of Ottawa © Stephen Henry Holland, Ottawa, Canada, 2020 Abstract Neuroblastoma (NB) is the most common extracranial solid tumour in childhood. NB is thought to arise from the failed differentiation of neural crest progenitor cells that would normally form tissues of the adrenal gland and sympathetic nervous system. These neural crest progenitors then uncontrollably proliferate forming a tumour. Despite aggressive surgery and chemotherapy, the cure rate of high-risk NB patients remains below 30%. Our laboratory has shown that human NB tumour specimens and high-risk patient derived cell lines express pannexin 1 (PANX1), and that treatment with the PANX1 channel blockers carbenoxolone or probenecid constitute reduce NB progression in vitro and in vivo. PANX1 is a glycoprotein that forms single membrane channels best known to serve as conduits for ATP release. Interestingly, while PANX1 was also detected in control neurons by western blotting, its banding pattern was strikingly different as a band at around 50 kDa was found in all NB cell lines, but not in neurons. Using shRNA targeting PANX1 and deglycosylation enzymes, I have shown that this band corresponds to a PANX1 glycosylated species. PANX1 has been reported to be phosphorylated in NB at amino acid Y10. PANX1 is also predicted to be glycosylated at N255. In order to study the role of these post-translational modifications, myc-tagged Y10F and N255A PANX1 mutants were engineered by site-directed mutagenesis.
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Signatures of Adaptive Evolution in Platyrrhine Primate Genomes 5 6 Hazel Byrne*, Timothy H
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GLIA 55:46–56 (2007) Pannexin1 is Expressed by Neurons and Glia but Does Not Form Functional Gap Junctions 1 2 3 1 YAN HUANG, * JUDITH B. GRINSPAN, CHARLES K. ABRAMS, AND STEVEN S. SCHERER 1Department of Neurology, The University of Pennsylvania Medical Center, Philadelphia, Pennsylvania 2Research Neurology, Children’s Hospital of Philadelphia, Philadelphia, Pennsylvania 3Department of Neuroscience and Neurology, Albert Einstein College of Medicine, Bronx, New York KEY WORDS with Panx2, forms functional channels, but Panx2 itself connexin; astrocytes; oligodendrocytes does not form functional channels (Bruzzone et al., 2003, 2005). Panx1 hemichannels are not gated by external Ca21, are remarkably sensitive to carbenoxolone, have ABSTRACT large unitary conductance, are permeant for ATP, are Pannexins are a newly described family of proteins that mechanosensitive, and can be activated by extracellular may form gap junctions. We made antisera against mouse pannexin1 (Panx1). HeLa cells expressing Panx1 have cell ATP acting through P2Y purinergic receptors (Bao et al., surface labeling, but not gap junction plaques, and do not 2004a; Bruzzone et al., 2005; Locovei et al., 2006a). transfer small ﬂuorescent dyes or neurobiotin in a scrape- Here we describe our analysis of mouse Panx1 (mPanx1), loading assay. Neuro2a cells expressing Panx1 are not elec- using antisera raised against sequences in the C-termi- trophysiologically coupled. Intracellular Panx1-immuno- nus. mPanx1 is expressed in the cell membrane of trans- reactivity, but not gap junction plaques, is seen in cultured fected HeLa cells, but does not form gap junction plaques oligodendrocytes, astrocytes, and hippocampal neurons. or functional channels in scrape-loading assays. Further, Thus, at least in these mammalian cells lines, Panx1 does Neuro2a cells that express mPanx1 are not electrophy- not form morphological or functional gap junctions, and it siologically coupled.
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Panx1 Channels Promote Both Anti- and Pro-Seizure-Like Activities in The
bioRxiv preprint doi: https://doi.org/10.1101/2021.06.03.446992; this version posted June 4, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. PWF et al. 2021 1 2 3 4 5 6 7 8 Panx1 channels promote both anti- and pro-seizure-like 9 activities in the zebrafish via p2rx7 receptors and ATP signaling 10 11 12 13 14 15 16 1,2,4* 1,2 1,2 1,2 17 Paige Whyte-Fagundes , Daria Taskina , Nickie Safarian , Christiane Zoidl , Peter L 18 Carlen3,4, Logan W Donaldson1, Georg R Zoidl1,2,4* 19 20 21 22 1 Department of Biology, York University; Toronto, Ontario, M3J1P3; Canada 23 2 Center of Vision Research (CVR), York University; Toronto, Ontario, M3J1P3; Canada 24 3 Department of Medicine, Physiology and BME, University of Toronto, 399 Bathurst St., 5w442, 25 Toronto, ON M5T 2S8, Canada 26 4 Department, Krembil Research Institute, University Health Network, 135 Nassau Street, 27 Toronto, ON M5T 1M8, Canada 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 *Corresponding authors: [email protected], [email protected] 45 46 Keywords: Pannexin1, seizures, epilepsy, electrophysiology, behavior, TALENs, Zebrafish, ATP 47 bioRxiv preprint doi: https://doi.org/10.1101/2021.06.03.446992; this version posted June 4, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission.
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PANX1 Antibody Catalog # ASC11574
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 PANX1 Antibody Catalog # ASC11574 Specification PANX1 Antibody - Product Information Application WB, IF Primary Accession Q96RD7 Other Accession NP_056183, 39995064 Reactivity Human, Mouse, Rat Host Rabbit Clonality Polyclonal Isotype IgG Calculated MW 47 kDa KDa Application Notes PANX1 antibody can be used for detection of PANX1 by Western blot at 1 - 2 µg/mL. For im munofluorescence Western blot analysis of PANX1 in human start at 20 µg/mL. ovary tissue lysate with PANX1 antibody at 1 µg/mL. PANX1 Antibody - Additional Information Gene ID 24145 Target/Specificity PANX1; Two transcript variants encoding different isoforms have been found for this gene. Reconstitution & Storage PANX1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. Immunofluorescence of PANX1 in human ovary tissue with PANX1 antibody at 20 Precautions µg/mL. PANX1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. PANX1 Antibody - Background PANX1 Antibody: The pannexin gene family PANX1 Antibody - Protein Information encodes a second class of putative gap junction proteins and are highly conserved in invertebrates and mammals. Pannexins (Panx) Name PANX1 (HGNC:8599) are four-pass transmembrane proteins that oligomerize to form large pore ion and Page 1/2 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 Synonyms MRS1 metabolite-permeable channels.
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