GUCY1A3 (C-Term) Blocking Peptide Synthetic Peptide Catalog # Bp7134b

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GUCY1A3 (C-Term) Blocking Peptide Synthetic Peptide Catalog # Bp7134b

10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 GUCY1A3 (C-term) Blocking peptide Synthetic peptide Catalog # BP7134b Specification GUCY1A3 (C-term) Blocking peptide - GUCY1A3 (C-term) Blocking peptide - Product Background Information Soluble guanylate cyclase (sGC), a Primary Accession Q02108 heterodimeric protein consisting of an alpha and a beta subunit, catalyzes the conversion of GTP to the second messenger cGMP and GUCY1A3 (C-term) Blocking peptide - Additional Information functions as the main receptor for nitric oxide and nitrovasodilator drugs. Gene ID 2982 GUCY1A3 (C-term) Blocking peptide - References Other Names Guanylate cyclase soluble subunit alpha-3, Saino, M., et al., Oncol. Rep. 12(1):47-52 GCS-alpha-3, GCS-alpha-1, Soluble (2004).Zhou, Y., et al., Gene 245(2):319-328 guanylate cyclase large subunit, GUCY1A3, (2000).Papapetropoulos, A., et al., J. Cell. GUC1A3, GUCSA3, GUCY1A1 Physiol. 167(2):213-221 (1996).Giuili, G., et al., Target/Specificity Hum. Genet. 91(3):257-260 (1993).Giuili, G., et The synthetic peptide sequence used to al., FEBS Lett. 304(1):83-88 (1992). generate the antibody <a href=/product/pr oducts/AP7134b>AP7134b</a> was selected from the C-term region of human GUCY1A3. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. Precautions This product is for research use only. Not for use in diagnostic or therapeutic procedures. GUCY1A3 (C-term) Blocking peptide - Protein Information Name GUCY1A1 (HGNC:4685) Page 1/2 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 Cellular Location Cytoplasm. Tissue Location Detected in brain cortex and lung (at protein level). GUCY1A3 (C-term) Blocking peptide - Protocols Provided below are standard protocols that you may find useful for product applications. • Blocking Peptides Page 2/2 Powered by TCPDF (www.tcpdf.org).

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Table 2. Significant
Table 2. Significant (Q < 0.05 and |d | > 0.5) transcripts from the meta-analysis Gene Chr Mb Gene Name Affy ProbeSet cDNA_IDs d HAP/LAP d HAP/LAP d d IS Average d Ztest P values Q-value Symbol ID (study #5) 1 2 STS B2m 2 122 beta-2 microglobulin 1452428_a_at AI848245 1.75334941 4 3.2 4 3.2316485 1.07398E-09 5.69E-08 Man2b1 8 84.4 mannosidase 2, alpha B1 1416340_a_at H4049B01 3.75722111 3.87309653 2.1 1.6 2.84852656 5.32443E-07 1.58E-05 1110032A03Rik 9 50.9 RIKEN cDNA 1110032A03 gene 1417211_a_at H4035E05 4 1.66015788 4 1.7 2.82772795 2.94266E-05 0.000527 NA 9 48.5 --- 1456111_at 3.43701477 1.85785922 4 2 2.8237185 9.97969E-08 3.48E-06 Scn4b 9 45.3 Sodium channel, type IV, beta 1434008_at AI844796 3.79536664 1.63774235 3.3 2.3 2.75319499 1.48057E-08 6.21E-07 polypeptide Gadd45gip1 8 84.1 RIKEN cDNA 2310040G17 gene 1417619_at 4 3.38875643 1.4 2 2.69163229 8.84279E-06 0.0001904 BC056474 15 12.1 Mus musculus cDNA clone 1424117_at H3030A06 3.95752801 2.42838452 1.9 2.2 2.62132809 1.3344E-08 5.66E-07 MGC:67360 IMAGE:6823629, complete cds NA 4 153 guanine nucleotide binding protein, 1454696_at -3.46081884 -4 -1.3 -1.6 -2.6026947 8.58458E-05 0.0012617 beta 1 Gnb1 4 153 guanine nucleotide binding protein, 1417432_a_at H3094D02 -3.13334396 -4 -1.6 -1.7 -2.5946297 1.04542E-05 0.0002202 beta 1 Gadd45gip1 8 84.1 RAD23a homolog (S.
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Allosteric Activation of the Nitric Oxide Receptor Soluble Guanylate Cyclase
RESEARCH ARTICLE Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy Benjamin G Horst1†, Adam L Yokom2,3†, Daniel J Rosenberg4,5, Kyle L Morris2,3‡, Michal Hammel4, James H Hurley2,3,4,5*, Michael A Marletta1,2,3* 1Department of Chemistry, University of California, Berkeley, Berkeley, United States; 2Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States; 3Graduate Group in Biophysics, University of California, Berkeley, Berkeley, United States; 4Molecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, United States; 5California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, United States Abstract Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO) in mammalian nitric oxide signaling. We determined structures of full-length Manduca sexta sGC in both inactive and active states using cryo-electron microscopy. NO and the sGC-specific stimulator YC-1 induce a 71˚ rotation of the heme-binding b H-NOX and PAS domains. Repositioning of the b *For correspondence: H-NOX domain leads to a straightening of the coiled-coil domains, which, in turn, use the motion to [email protected] (JHH); move the catalytic domains into an active conformation. YC-1 binds directly between the b H-NOX [email protected] (MAM) domain and the two CC domains. The structural elongation of the particle observed in cryo-EM was †These authors contributed corroborated in solution using small angle X-ray scattering (SAXS). These structures delineate the equally to this work endpoints of the allosteric transition responsible for the major cyclic GMP-dependent physiological Present address: ‡MRC London effects of NO.
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Purinergic Receptor Transactivation by the Β2-Adrenergic Receptor Increases Intracellular Ca2+ in Non-Excitable Cells
Molecular Pharmacology Fast Forward. Published on March 9, 2017 as DOI: 10.1124/mol.116.106419 This article has not been copyedited and formatted. The final version may differ from this version. MOLPHARM/2016/106419 Title page: Purinergic receptor transactivation by the β2-adrenergic receptor increases intracellular Ca2+ in non-excitable cells. Wayne Stallaert, Emma T van der Westhuizen, Anne-Marie Schönegge, Bianca Plouffe, Mireille Downloaded from Hogue, Viktoria Lukashova, Asuka Inoue, Satoru Ishida, Junken Aoki, Christian Le Gouill & Michel Bouvier. molpharm.aspetjournals.org Department of Biochemistry, Université de Montréal, Montréal, QC, Canada (WS, ETvdW, A- MS, BP, MB). Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, QC, Canada (WS, ETvdW, A-MS, BP, MH, VL, CLG, MB). Monash Institute for at ASPET Journals on September 30, 2021 Pharmaceutical Sciences, Monash University, Parkville, Victoria, Australia (ETvdW). Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Miyagi, Japan (AI, SI, JA). Japan Science and Technology Agency (JST), Precursory Research for Embryonic Science and Technology (PRESTO), Kawaguchi, Saitama, Japan (AI). Japan Agency for Medical Research and Development, Core Research for Evolutional Science and Technology (AMED-CREST), Chiyoda-ku, Tokyo, Japan (JA). 1 Molecular Pharmacology Fast Forward. Published on March 9, 2017 as DOI: 10.1124/mol.116.106419 This article has not been copyedited and formatted. The final version may differ from this version. MOLPHARM/2016/106419 Running title page: a) Running title: β2AR transactivation of purinergic receptors b) Corresponding author: Michel Bouvier, IRIC - Université de Montréal, P.O. Box 6128 Succursale Centre-Ville, Montréal, Qc. Canada, H3C 3J7. Tel: +1-514-343-6319.
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Antagonism of Forkhead Box Subclass O Transcription Factors Elicits Loss of Soluble Guanylyl Cyclase Expression S
Supplemental material to this article can be found at: http://molpharm.aspetjournals.org/content/suppl/2019/04/15/mol.118.115386.DC1 1521-0111/95/6/629–637$35.00 https://doi.org/10.1124/mol.118.115386 MOLECULAR PHARMACOLOGY Mol Pharmacol 95:629–637, June 2019 Copyright ª 2019 by The Author(s) This is an open access article distributed under the CC BY-NC Attribution 4.0 International license. Antagonism of Forkhead Box Subclass O Transcription Factors Elicits Loss of Soluble Guanylyl Cyclase Expression s Joseph C. Galley, Brittany G. Durgin, Megan P. Miller, Scott A. Hahn, Shuai Yuan, Katherine C. Wood, and Adam C. Straub Heart, Lung, Blood and Vascular Medicine Institute (J.C.G., B.G.D., M.P.M., S.A.H., S.Y., K.C.W., A.C.S.) and Department of Pharmacology and Chemical Biology (J.C.G., A.C.S.), University of Pittsburgh, Pittsburgh, Pennsylvania Received November 29, 2018; accepted March 31, 2019 Downloaded from ABSTRACT Nitric oxide (NO) stimulates soluble guanylyl cyclase (sGC) protein expression showed a concentration-dependent down- activity, leading to elevated intracellular cyclic guano- regulation. Consistent with the loss of sGC a and b mRNA and sine 39,59-monophosphate (cGMP) and subsequent vascular protein expression, pretreatment of vascular smooth muscle smooth muscle relaxation. It is known that downregulation of cells with the FoxO inhibitor decreased sGC activity mea- sGC expression attenuates vascular dilation and contributes to sured by cGMP production following stimulation with an NO molpharm.aspetjournals.org the pathogenesis of cardiovascular disease. However, it is not donor.
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Structure/Function of the Soluble Guanylyl Cyclase Catalytic Domain
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HHS Public Access Author manuscript Author ManuscriptAuthor Manuscript Author Clin Genet Manuscript Author . Author manuscript; Manuscript Author available in PMC 2017 October 01. Published in final edited form as: Clin Genet. 2016 October ; 90(4): 351–360. doi:10.1111/cge.12739. Disrupted Nitric Oxide Signaling due to GUCY1A3 Mutations Increases Risk for Moyamoya Disease, Achalasia and Hypertension Stephanie Wallace1, Dong-chuan Guo1, Ellen Regalado1, Lauren Mellor-Crummey1, Michael Banshad2, Deborah A. Nickerson2, Robert Dauser3, Neil Hanchard4, Ronit Marom4, Emil Martin1, Vladimir Berka1, Iraida Sharina1, Vijeya Ganesan5, Dawn Saunders6, Shaine Morris7, and Dianna M. Milewicz, MD1 1Division of Medical Genetics, Cardiology, and Hematology, Department of Internal Medicine, University of Texas Health Science Center, Houston, Texas 2Department of Genome Sciences, University of Washington, Seattle, Washington 3Department of Neurosurgery, Texas Children’s Hospital, Houston, Texas 4Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 5Neuroscience Unit, University College of London Institute of Child Health, London, UK 6Department of Radiology, Great Ormond Street Hospital, London, UK 7Department of Pediatrics – Cardiology, Texas Children's Hospital and Baylor College of Medicine, Houston, Texas Abstract Moyamoya disease (MMD) is a progressive vasculopathy characterized by occlusion of the terminal portion of the internal carotid arteries and its branches, and the formation of compensatory moyamoya collateral vessels. Homozygous mutations in GUCY1A3 have been reported as a cause of MMD and achalasia. Probands (n = 96) from unrelated families underwent sequencing of GUCY1A3. Functional studies were performed to confirm the pathogenicity of identified GUCY1A3 variants. Two affected individuals from unrelated families were found to have compound heterozygous mutations in GUCY1A3.
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Comparative Gene Expression Analysis of the Amygdala in Autistic Rat Models Produced by Pre- and Post-Natal Exposures to Valproic Acid
The Journal of Toxicological Sciences (J. Toxicol. Sci.) 391 Vol.38, No.3, 391-402, 2013 Toxicomics Report Comparative gene expression analysis of the amygdala in autistic rat models produced by pre- and post-natal exposures to valproic acid Atsuko Oguchi-Katayama1, Akihiko Monma2, Yuko Sekino1, Toru Moriguchi2 and Kaoru Sato1 1Laboratory of Neuropharmacology, Division of Pharmacology, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158-8501, Japan 2Department of Food and Life Sciences, Azabu University, 1-17-71 Fuchinobe, Tyuoku, Sagamihara-shi, Kanagawa 252-5201, Japan (Received October 24, 2012; Accepted March 14, 2013) ABSTRACT — Gene expression profiles in the amygdala of juvenile rats were compared between the two autistic rat models for mechanistic insights into impaired social behavior and enhanced anxiety in autism. The rats exposed to VPA by intraperitoneal administration to their dams at embryonic day (E) 12 were used as a model for autism (E2IP), and those by subcutaneous administration at postnatal day (P) 14 (P14SC) were used as a model for regressive autism; both of the models show impaired social behavior and enhanced anxiety as symptoms. Gene expression profiles in the amygdala of the rats (E12IP and P14SC) were analyzed by microarray and compared to each other. Only two genes, Neu2 and Mt2a, showed significant changes in the same direction in both of the rat models, and there were little similari- ties in the overall gene expression profiles between them. It was considered that gene expression chang- es per se in the amygdala might be an important cause for impaired social behavior and enhanced anxiety, rather than expression changes of particular genes.
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Polyclonal Antibody to Guanylate Cyclase Soluble GUCY1A3 - Aff - Purified
OriGene Technologies, Inc. OriGene Technologies GmbH 9620 Medical Center Drive, Ste 200 Schillerstr. 5 Rockville, MD 20850 32052 Herford UNITED STATES GERMANY Phone: +1-888-267-4436 Phone: +49-5221-34606-0 Fax: +1-301-340-8606 Fax: +49-5221-34606-11 [email protected] [email protected] AP20764PU-N Polyclonal Antibody to Guanylate cyclase soluble GUCY1A3 - Aff - Purified Alternate names: GCS-alpha-1, GCS-alpha-3, GUC1A3, GUCSA3, GUCY1A1, Guanylate cyclase soluble subunit alpha-3, Soluble guanylate cyclase large subunit, sGC alpha Quantity: 0.1 mg Concentration: 1.0 mg/ml Background: Guanylate cyclases belong to the adenylyl cyclase class-4/guanylyl cyclase family. There are two forms of guanylate cyclase, a soluble form (GCS or sGC), which act as receptors for nitric oxide and a membrane-bound receptor form (GC), which are peptide hormone receptors. The GC-C protein is composed of an extracellular domain, a single transmembrane domain, and a cytoplasmic region consisting of a kinase-like domain and a catalytic domain. It is expressed as two differentially glycosylated forms, a 130 kDa precursor form present in the endoplasmic reticulum and a 145 kDa form present on the plasma membrane. Ligand binding to the extracellular domain of GC-C promotes the accumulation of cGMP. GC-C acts as the receptor for heatstable enterotoxins, small peptides secreted by some pathogenic strains of E. coli that cause severe secretory diarrhea. GC-C also binds to guanylin and uroguanylin peptides, which modulate renal function in response to oral salt load. Uniprot ID: Q02108 NCBI: NP_000847 GeneID: 2982 Host: Rabbit Immunogen: Synthetic peptide, corresponding to amino acids 400-450 of Human GCS-α-1.
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Supplemental Material
Supplemental Table 1. Genes activated by alcohol in cultured cortical neurons, as assessed by micro-array analysis. Gene Description Genbank Acc No Folds of increase Gpnmb glycoprotein (transmembrane) nmb NM_053110 2.58 Lyzs lysozyme NM_017372 2.36 Gpnmb glycoprotein (transmembrane) nmb NM_053110 2.33 Gpnmb glycoprotein (transmembrane) nmb NM_053110 2.27 Gpm6a glycoprotein m6a NM_153581 2.05 Mtap1b microtubule-associated protein 1 B NM_008634 2.00 Gfap glial fibrillary acidic protein NM_010277 1.94 C1qg complement component 1, q subcomponent, C chain NM_007574 1.90 C1qb complement component 1, q subcomponent, beta polypeptide, mRNA NM_009777 1.87 Laptm5 lysosomal-associated protein transmembrane 5 NM_010686 1.82 Apoc1 apolipoprotein C-I NM_007469 1.81 Lgals3 lectin, galactose binding, soluble 3 NM_010705 1.81 Fcer1g Fc receptor, IgE, high affinity I, gamma polypeptide NM_010185 1.81 Cd68 CD68 antigen NM_009853 1.81 Apoe apolipoprotein E NM_009696 1.76 C1qa complement component 1, q subcomponent, alpha polypeptide NM_007572 1.75 Lgmn legumain NM_011175 1.74 Msr2 macrophage scavenger receptor 2 NM_030707 1.72 Trem2 triggering receptor expressed on myeloid cells 2 NM_031254 1.72 Serpina3n serine (or cysteine) peptidase inhibitor, clade A, member 3N NM_009252 1.71 Igf1 insulin-like growth factor 1, transcript variant 1 NM_010512 1.71 Ctsz cathepsin Z NM_022325 1.71 Adfp adipose differentiation related protein NM_007408 1.69 Pdgfra platelet derived growth factor receptor, alpha polypeptide NM_011058 1.67 Mmp12 matrix metallopeptidase 12 NM_008605
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Cocoa procyanidins modulate transcriptional pathways linked to inflammation and metabolism in human dendritic cells Article Accepted Version Midttun, H. L. E., Ramsay, A., Mueller-Harvey, I. and Williams, A. R. (2018) Cocoa procyanidins modulate transcriptional pathways linked to inflammation and metabolism in human dendritic cells. Food & Function, 5. pp. 2883-2890. ISSN 2042-650X doi: https://doi.org/10.1039/C8FO00387D Available at http://centaur.reading.ac.uk/76829/ It is advisable to refer to the publisher’s version if you intend to cite from the work. See Guidance on citing . To link to this article DOI: http://dx.doi.org/10.1039/C8FO00387D Publisher: Royal Society of Chemistry All outputs in CentAUR are protected by Intellectual Property Rights law, including copyright law. Copyright and IPR is retained by the creators or other copyright holders. Terms and conditions for use of this material are defined in the End User Agreement . www.reading.ac.uk/centaur CentAUR Central Archive at the University of Reading Reading’s research outputs online Cocoa procyanidins modulate transcriptional pathways linked to inflammation and metabolism in human dendritic cells Helene L.E. Midttun1, Aina Ramsay2, Irene Mueller-Harvey2, Andrew R. Williams1* 1Department of Veterinary and Animal Sciences, University of Copenhagen, Frederiksberg, Denmark 2Chemistry and Biochemistry Laboratory, School of Agriculture, Policy and Development, University of Reading, Reading, United Kingdom *[email protected] Abstract Foods rich in polyphenols such as procyanidins (PC) have been proposed to have anti-inflammatory properties, and we have previously reported inhibition of lipopolysaccharide (LPS)-induced inflammatory cytokine secretion in human dendritic cells (DCs) by PC derived from cocoa.
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Transcriptome Profiling Reveals the Complexity of Pirfenidone Effects in IPF
ERJ Express. Published on August 30, 2018 as doi: 10.1183/13993003.00564-2018 Early View Original article Transcriptome profiling reveals the complexity of pirfenidone effects in IPF Grazyna Kwapiszewska, Anna Gungl, Jochen Wilhelm, Leigh M. Marsh, Helene Thekkekara Puthenparampil, Katharina Sinn, Miroslava Didiasova, Walter Klepetko, Djuro Kosanovic, Ralph T. Schermuly, Lukasz Wujak, Benjamin Weiss, Liliana Schaefer, Marc Schneider, Michael Kreuter, Andrea Olschewski, Werner Seeger, Horst Olschewski, Malgorzata Wygrecka Please cite this article as: Kwapiszewska G, Gungl A, Wilhelm J, et al. Transcriptome profiling reveals the complexity of pirfenidone effects in IPF. Eur Respir J 2018; in press (https://doi.org/10.1183/13993003.00564-2018). This manuscript has recently been accepted for publication in the European Respiratory Journal. It is published here in its accepted form prior to copyediting and typesetting by our production team. After these production processes are complete and the authors have approved the resulting proofs, the article will move to the latest issue of the ERJ online. Copyright ©ERS 2018 Copyright 2018 by the European Respiratory Society. Transcriptome profiling reveals the complexity of pirfenidone effects in IPF Grazyna Kwapiszewska1,2, Anna Gungl2, Jochen Wilhelm3†, Leigh M. Marsh1, Helene Thekkekara Puthenparampil1, Katharina Sinn4, Miroslava Didiasova5, Walter Klepetko4, Djuro Kosanovic3, Ralph T. Schermuly3†, Lukasz Wujak5, Benjamin Weiss6, Liliana Schaefer7, Marc Schneider8†, Michael Kreuter8†, Andrea Olschewski1,
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Supplemental Figures 04 12 2017
Jung et al. 1 SUPPLEMENTAL FIGURES 2 3 Supplemental Figure 1. Clinical relevance of natural product methyltransferases (NPMTs) in brain disorders. (A) 4 Table summarizing characteristics of 11 NPMTs using data derived from the TCGA GBM and Rembrandt datasets for 5 relative expression levels and survival. In addition, published studies of the 11 NPMTs are summarized. (B) The 1 Jung et al. 6 expression levels of 10 NPMTs in glioblastoma versus non‐tumor brain are displayed in a heatmap, ranked by 7 significance and expression levels. *, p<0.05; **, p<0.01; ***, p<0.001. 8 2 Jung et al. 9 10 Supplemental Figure 2. Anatomical distribution of methyltransferase and metabolic signatures within 11 glioblastomas. The Ivy GAP dataset was downloaded and interrogated by histological structure for NNMT, NAMPT, 12 DNMT mRNA expression and selected gene expression signatures. The results are displayed on a heatmap. The 13 sample size of each histological region as indicated on the figure. 14 3 Jung et al. 15 16 Supplemental Figure 3. Altered expression of nicotinamide and nicotinate metabolism‐related enzymes in 17 glioblastoma. (A) Heatmap (fold change of expression) of whole 25 enzymes in the KEGG nicotinate and 18 nicotinamide metabolism gene set were analyzed in indicated glioblastoma expression datasets with Oncomine. 4 Jung et al. 19 Color bar intensity indicates percentile of fold change in glioblastoma relative to normal brain. (B) Nicotinamide and 20 nicotinate and methionine salvage pathways are displayed with the relative expression levels in glioblastoma 21 specimens in the TCGA GBM dataset indicated. 22 5 Jung et al. 23 24 Supplementary Figure 4.
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