USO1 Rabbit Pab

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Leader in Biomolecular Solutions for Life Science USO1 Rabbit pAb Catalog No.: A16079 Basic Information Background Catalog No. The protein encoded by this gene is a peripheral membrane protein which recycles A16079 between the cytosol and the Golgi apparatus during interphase. It is regulated by phosphorylation: dephosphorylated protein associates with the Golgi membrane and Observed MW dissociates from the membrane upon phosphorylation. Ras-associated protein 1 recruits 108kDa this protein to coat protein complex II (COPII) vesicles during budding from the endoplasmic reticulum, where it interacts with a set of COPII vesicle-associated SNAREs Calculated MW to form a cis-SNARE complex that promotes targeting to the Golgi apparatus. Alternative 107kDa/109kDa splicing results in multiple transcript variants. Category Primary antibody Applications WB,IHC,IF Cross-Reactivity Human, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 8615 O60763 IHC 1:50 - 1:100 Immunogen 1:50 - 1:100 IF Recombinant fusion protein containing a sequence corresponding to amino acids 663-962 of human USO1 (NP_003706.2). Synonyms USO1;P115;TAP;VDP Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using USO1 antibody (A16079) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (RM00020). Exposure time: 1s. Immunofluorescence analysis of HeLa cells Confocal immunofluorescence analysis of using USO1 antibody (A16079) at dilution Hela cells using USO1 antibody (A16079) at of 1:200 (60x lens). Blue: DAPI for nuclear dilution of 1:200. Blue: DAPI for nuclear staining. staining. Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..

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A Cytoskeleton-Related Gene, USO1, Is Required for Intracellular Protein
A Cytoskeleton-related Gene, USO1, Is Required for Intracellular Protein Transport in Saccharomyces cer isiae Harushi Nakajima, Aiko Hiram,* Yuri Ogawa, Tadashi Yonehara, Koji Yoda, and Makari Yamasaki Department of Agricultural Chemistry, the University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku Tokyo 113, Japan; and * Institute of Applied Microbiology, the University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku Tokyo 113, Japan Abstract. The Saccharomyces cerevisiae mutant accumulation of the ER at the restrictive temperature. strains blocked in the protein secretion pathway are Abnormally oriented bundles of microtubules were of- not able to induce sexual aggregation. We have uti- ten found in the nucleus. The US01 gene was cloned lized the defect of aggregation to concentrate the by complementation of the usol temperature-sensitive secretion-deficient cells and identified a new gene growth defect. DNA sequence analysis revealed a which functions in the process of intracellular protein hydrophilic protein of 1790 amino acids with a COOH- transport. The new mutant, usol, is temperature sensi- terminal 1,100-amino acid-long t~-helical structure tive for growth and protein secretion. At the restrictive characteristic of the coiled-coil rod region of the temperature (37°C), usol mutant accumulated the cytoskeleton-related proteins. These observations sug- core-glycosylated precursor form of the exported pro- gest that Usol protein plays a role as a cytoskeletal tein invertase in the cells. Ultrastructural study of the component in the protein transport from the ER to the mutant fixed by the freeze-substitution method re- later secretory compartments. vealed expansion of the nuclear envelope lumen and N the eukaryotic ceils, proteins destined for the extra- into the ER, sec61,62,63, ptll, and 2 have been isolated by cellular environment, plasma membrane, or lysosomes utilizing the mislocalization to the cytoplasm of prepro-a- I are first synthesized as precursor polypeptides in the factor-HIS4 or prepro-ct-factor-TRP1 fusion proteins (Deshaies cytoplasm.
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Anti-GM130 (Cis-Golgi Marker) Antibody R1608-7
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Stx5-Mediated ER-Golgi Transport in Mammals and Yeast
cells Review Stx5-Mediated ER-Golgi Transport in Mammals and Yeast Peter TA Linders 1 , Chiel van der Horst 1, Martin ter Beest 1 and Geert van den Bogaart 1,2,* 1 Tumor Immunology Lab, Radboud University Medical Center, Radboud Institute for Molecular Life Sciences, Geert Grooteplein 28, 6525 GA Nijmegen, The Netherlands 2 Department of Molecular Immunology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands * Correspondence: [email protected]; Tel.: +31-50-36-35230 Received: 8 July 2019; Accepted: 25 July 2019; Published: 26 July 2019 Abstract: The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) syntaxin 5 (Stx5) in mammals and its ortholog Sed5p in Saccharomyces cerevisiae mediate anterograde and retrograde endoplasmic reticulum (ER)-Golgi trafficking. Stx5 and Sed5p are structurally highly conserved and are both regulated by interactions with other ER-Golgi SNARE proteins, the Sec1/Munc18-like protein Scfd1/Sly1p and the membrane tethering complexes COG, p115, and GM130. Despite these similarities, yeast Sed5p and mammalian Stx5 are differently recruited to COPII-coated vesicles, and Stx5 interacts with the microtubular cytoskeleton, whereas Sed5p does not. In this review, we argue that these different Stx5 interactions contribute to structural differences in ER-Golgi transport between mammalian and yeast cells. Insight into the function of Stx5 is important given its essential role in the secretory pathway of eukaryotic cells and its involvement in infections and neurodegenerative diseases. Keywords: syntaxin 5; Golgi apparatus; endoplasmic reticulum; membrane trafficking; secretory pathway 1. Introduction The secretory pathway is essential for secretion of cytokines, hormones, growth factors, and extracellular matrix proteins, as well as for the delivery of receptors and transporters to the cell membrane and lytic proteins to endo-lysosomal compartments.
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Anti-USO1 Ponoclonal Antibody Cat: K008623P Summary
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Structural Basis for Selective Stalling of Human Ribosome Nascent Chain
bioRxiv preprint doi: https://doi.org/10.1101/315325; this version posted January 9, 2019. 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. Title: Structural basis for selective stalling of human ribosome nascent chain complexes by a drug-like molecule Authors: Wenfei Li1,2, Fred R. Ward1, Kim F. McClure3, Stacey Tsai-Lan Chang1, Elizabeth Montabana2, Spiros Liras3, Robert Dullea4 and Jamie H. D. Cate1,2,5* 1Department of Molecular & Cell Biology, University of California, Berkeley, California 94720, USA. 2Molecular Biophysics and Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA. 3Pfizer Medicinal Chemistry, Pfizer Worldwide Research and Development, Cambridge, Massachusetts 02139, United States of America. 4Cardiovascular, Metabolic and Endocrine Disease Research Unit, Pfizer Worldwide Research and Development, Cambridge, Massachusetts 02139, United States of America. 5Department of Chemistry, University of California, Berkeley, California 94720, USA. *e-mail: [email protected] bioRxiv preprint doi: https://doi.org/10.1101/315325; this version posted January 9, 2019. 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. Li et al. Abstract: Small molecules that target the ribosome generally have a global impact on protein synthesis. However, the drug-like molecule PF-06446846 (PF846) binds the human ribosome and selectively blocks the translation of a small subset of proteins by an unknown mechanism. In high-resolution cryo-electron microscopy (cryo-EM) structures of human ribosome nascent chain complexes stalled by PF846, PF846 binds in the ribosome exit tunnel in a newly-identified and eukaryotic-specific pocket formed by the 28S ribosomal RNA (rRNA), and redirects the path of the nascent polypeptide chain.
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