KPNA5 Antibody Cat

Total Page:16

File Type:pdf, Size:1020Kb

KPNA5 Antibody Cat KPNA5 Antibody Cat. No.: 26-913 KPNA5 Antibody Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human Antibody produced in rabbits immunized with a synthetic peptide corresponding a region IMMUNOGEN: of human KPNA5. TESTED APPLICATIONS: ELISA, WB KPNA5 antibody can be used for detection of KPNA5 by ELISA at 1:312500. KPNA5 APPLICATIONS: antibody can be used for detection of KPNA5 by western blot at 1 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 - 100,000. POSITIVE CONTROL: 1) Cat. No. 1205 - Jurkat Cell Lysate PREDICTED MOLECULAR 61 kDa WEIGHT: Properties PURIFICATION: Antibody is purified by peptide affinity chromatography method. CLONALITY: Polyclonal CONJUGATE: Unconjugated PHYSICAL STATE: Liquid September 30, 2021 1 https://www.prosci-inc.com/kpna5-antibody-26-913.html Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% BUFFER: sucrose. CONCENTRATION: batch dependent For short periods of storage (days) store at 4˚C. For longer periods of storage, store STORAGE CONDITIONS: KPNA5 antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles. Additional Info OFFICIAL SYMBOL: KPNA5 ALTERNATE NAMES: KPNA5, IPOA6, SRP6 ACCESSION NO.: NP_002260 PROTEIN GI NO.: 39812229 GENE ID: 3841 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References The transport of molecules between the nucleus and the cytoplasm in eukaryotic cells is mediated by the nuclear pore complex (NPC) which consists of 60-100 proteins and is probably 120 million daltons in molecular size. Small molecules (up to 70 kD) can pass through the nuclear pore by nonselective diffusion; larger molecules are transported by an active process. Most nuclear proteins contain short basic amino acid sequences known as nuclear localization signals (NLSs). KPNA5 protein belongs to the importin alpha protein family and is thought to be involved in NLS-dependent protein import into the nucleus.The transport of molecules between the nucleus and the cytoplasm in eukaryotic BACKGROUND: cells is mediated by the nuclear pore complex (NPC) which consists of 60-100 proteins and is probably 120 million daltons in molecular size. Small molecules (up to 70 kD) can pass through the nuclear pore by nonselective diffusion; larger molecules are transported by an active process. Most nuclear proteins contain short basic amino acid sequences known as nuclear localization signals (NLSs). KPNA5 protein belongs to the importin alpha protein family and is thought to be involved in NLS-dependent protein import into the nucleus. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. REFERENCES: 1) Singh, A.P., (2007) Cell 131 (3), 492-504. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 30, 2021 2 https://www.prosci-inc.com/kpna5-antibody-26-913.html.
Recommended publications
  • Global Characteristics of Csig-Associated Gene Expression Changes in Human Hek293 Cells and the Implications for Csig Regulating Cell Proliferation and Senescence
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Frontiers - Publisher Connector ORIGINAL RESEARCH published: 15 May 2015 doi: 10.3389/fendo.2015.00069 Global characteristics of CSIG-associated gene expression changes in human HEK293 cells and the implications for CSIG regulating cell proliferation and senescence Liwei Ma, Wenting Zhao, Feng Zhu, Fuwen Yuan, Nan Xie, Tingting Li, Pingzhang Wang and Tanjun Tong* Research Center on Aging. Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Edited by: Beijing, China Wen Zhou, Columbia University, USA Reviewed by: Cellular senescence-inhibited gene (CSIG), also named as ribosomal_L1 domain-contain- Jian Zhong, ing 1 (RSL1D1), is implicated in various processes including cell cycle regulation, cellular Mayo Clinic, USA Xiaoxu Zheng, senescence, apoptosis, and tumor metastasis. However, little is known about the regulatory University of Maryland Baltimore, USA mechanism underlying its functions. To screen important targets and signaling pathways Wensi Tao, University of Miami, USA modulated by CSIG, we compared the gene expression profiles in CSIG-silencing and control *Correspondence: HEK293 cells using Affymetrix microarray Human Genome U133 Plus 2.0 GeneChips. A Tanjun Tong, total of 590 genes displayed statistically significant expression changes, with 279 genes Department of Biochemistry and up-regulated and 311 down-regulated, respectively. These genes are involved in a broad array Molecular Biology, Research Center on Aging, Peking University Health of biological processes, mainly in transcriptional regulation, cell cycle, signal transduction, Science Center, 38 Xueyuan Road, oxidation reduction, development, and cell adhesion.
    [Show full text]
  • Nuclear Import Protein KPNA7 and Its Cargos Acta Universitatis Tamperensis 2346
    ELISA VUORINEN Nuclear Import Protein KPNA7 and its Cargos ELISA Acta Universitatis Tamperensis 2346 ELISA VUORINEN Nuclear Import Protein KPNA7 and its Cargos Diverse roles in the regulation of cancer cell growth, mitosis and nuclear morphology AUT 2346 AUT ELISA VUORINEN Nuclear Import Protein KPNA7 and its Cargos Diverse roles in the regulation of cancer cell growth, mitosis and nuclear morphology ACADEMIC DISSERTATION To be presented, with the permission of the Faculty Council of the Faculty of Medicine and Life Sciences of the University of Tampere, for public discussion in the auditorium F114 of the Arvo building, Arvo Ylpön katu 34, Tampere, on 9 February 2018, at 12 o’clock. UNIVERSITY OF TAMPERE ELISA VUORINEN Nuclear Import Protein KPNA7 and its Cargos Diverse roles in the regulation of cancer cell growth, mitosis and nuclear morphology Acta Universitatis Tamperensis 2346 Tampere University Press Tampere 2018 ACADEMIC DISSERTATION University of Tampere, Faculty of Medicine and Life Sciences Finland Supervised by Reviewed by Professor Anne Kallioniemi Docent Pia Vahteristo University of Tampere University of Helsinki Finland Finland Docent Maria Vartiainen University of Helsinki Finland The originality of this thesis has been checked using the Turnitin OriginalityCheck service in accordance with the quality management system of the University of Tampere. Copyright ©2018 Tampere University Press and the author Cover design by Mikko Reinikka Acta Universitatis Tamperensis 2346 Acta Electronica Universitatis Tamperensis 1851 ISBN 978-952-03-0641-0 (print) ISBN 978-952-03-0642-7 (pdf) ISSN-L 1455-1616 ISSN 1456-954X ISSN 1455-1616 http://tampub.uta.fi Suomen Yliopistopaino Oy – Juvenes Print Tampere 2018 441 729 Painotuote CONTENTS List of original communications ................................................................................................
    [Show full text]
  • (KPNA7), a Divergent Member of the Importin a Family of Nuclear Import
    Kelley et al. BMC Cell Biology 2010, 11:63 http://www.biomedcentral.com/1471-2121/11/63 RESEARCH ARTICLE Open Access Karyopherin a7 (KPNA7), a divergent member of the importin a family of nuclear import receptors Joshua B Kelley1, Ashley M Talley1, Adam Spencer1, Daniel Gioeli2, Bryce M Paschal1,3* Abstract Background: Classical nuclear localization signal (NLS) dependent nuclear import is carried out by a heterodimer of importin a and importin b. NLS cargo is recognized by importin a, which is bound by importin b. Importin b mediates translocation of the complex through the central channel of the nuclear pore, and upon reaching the nucleus, RanGTP binding to importin b triggers disassembly of the complex. To date, six importin a family members, encoded by separate genes, have been described in humans. Results: We sequenced and characterized a seventh member of the importin a family of transport factors, karyopherin a 7 (KPNA7), which is most closely related to KPNA2. The domain of KPNA7 that binds Importin b (IBB) is divergent, and shows stronger binding to importin b than the IBB domains from of other importin a family members. With regard to NLS recognition, KPNA7 binds to the retinoblastoma (RB) NLS to a similar degree as KPNA2, but it fails to bind the SV40-NLS and the human nucleoplasmin (NPM) NLS. KPNA7 shows a predominantly nuclear distribution under steady state conditions, which contrasts with KPNA2 which is primarily cytoplasmic. Conclusion: KPNA7 is a novel importin a family member in humans that belongs to the importin a2 subfamily. KPNA7 shows different subcellular localization and NLS binding characteristics compared to other members of the importin a family.
    [Show full text]
  • Primepcr™Assay Validation Report
    PrimePCR™Assay Validation Report Gene Information Gene Name karyopherin alpha 5 (importin alpha 6) Gene Symbol KPNA5 Organism Human Gene Summary The transport of molecules between the nucleus and the cytoplasm in eukaryotic cells is mediated by the nuclear pore complex (NPC) which consists of 60-100 proteins and is probably 120 million daltons in molecular size. Small molecules (up to 70 kD) can pass through the nuclear pore by nonselective diffusion; larger molecules are transported by an active process. Most nuclear proteins contain short basic amino acid sequences known as nuclear localization signals (NLSs). KPNA5 protein belongs to the importin alpha protein family and is thought to be involved in NLS-dependent protein import into the nucleus. Gene Aliases IPOA6, SRP6 RefSeq Accession No. NC_000006.11, NT_025741.15 UniGene ID Hs.182971 Ensembl Gene ID ENSG00000196911 Entrez Gene ID 3841 Assay Information Unique Assay ID qHsaCEP0055392 Assay Type Probe - Validation information is for the primer pair using SYBR® Green detection Detected Coding Transcript(s) ENST00000368564, ENST00000392517, ENST00000356348 Amplicon Context Sequence CCCCAGCATTGTACCTCAGGTGGATGAAAACCAACAACAGTTTATATTTCAGCAG CAGGAAGCACCAATGGATGGATTTCAACTTTAACTTACTGGAGGAAAAAAAATTT ATGGCTAAAAA Amplicon Length (bp) 91 Chromosome Location 6:117053399-117053519 Assay Design Exonic Purification Desalted Validation Results Efficiency (%) 94 R2 0.9992 cDNA Cq 23.2 Page 1/5 PrimePCR™Assay Validation Report cDNA Tm (Celsius) 79 gDNA Cq 24.6 Specificity (%) 100 Information to assist
    [Show full text]
  • Human Induced Pluripotent Stem Cell–Derived Podocytes Mature Into Vascularized Glomeruli Upon Experimental Transplantation
    BASIC RESEARCH www.jasn.org Human Induced Pluripotent Stem Cell–Derived Podocytes Mature into Vascularized Glomeruli upon Experimental Transplantation † Sazia Sharmin,* Atsuhiro Taguchi,* Yusuke Kaku,* Yasuhiro Yoshimura,* Tomoko Ohmori,* ‡ † ‡ Tetsushi Sakuma, Masashi Mukoyama, Takashi Yamamoto, Hidetake Kurihara,§ and | Ryuichi Nishinakamura* *Department of Kidney Development, Institute of Molecular Embryology and Genetics, and †Department of Nephrology, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan; ‡Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Hiroshima, Japan; §Division of Anatomy, Juntendo University School of Medicine, Tokyo, Japan; and |Japan Science and Technology Agency, CREST, Kumamoto, Japan ABSTRACT Glomerular podocytes express proteins, such as nephrin, that constitute the slit diaphragm, thereby contributing to the filtration process in the kidney. Glomerular development has been analyzed mainly in mice, whereas analysis of human kidney development has been minimal because of limited access to embryonic kidneys. We previously reported the induction of three-dimensional primordial glomeruli from human induced pluripotent stem (iPS) cells. Here, using transcription activator–like effector nuclease-mediated homologous recombination, we generated human iPS cell lines that express green fluorescent protein (GFP) in the NPHS1 locus, which encodes nephrin, and we show that GFP expression facilitated accurate visualization of nephrin-positive podocyte formation in
    [Show full text]
  • The Consensus Coding Sequences of Human Breast and Colorectal Cancers Tobias Sjöblom,1* Siân Jones,1* Laura D
    The Consensus Coding Sequences of Human Breast and Colorectal Cancers Tobias Sjöblom,1* Siân Jones,1* Laura D. Wood,1* D. Williams Parsons,1* Jimmy Lin,1 Thomas Barber,1 Diana Mandelker,1 Rebecca J. Leary,1 Janine Ptak,1 Natalie Silliman,1 Steve Szabo,1 Phillip Buckhaults,2 Christopher Farrell,2 Paul Meeh,2 Sanford D. Markowitz,3 Joseph Willis,4 Dawn Dawson,4 James K. V. Willson,5 Adi F. Gazdar,6 James Hartigan,7 Leo Wu,8 Changsheng Liu,8 Giovanni Parmigiani,9 Ben Ho Park,10 Kurtis E. Bachman,11 Nickolas Papadopoulos,1 Bert Vogelstein,1† Kenneth W. Kinzler,1† Victor E. Velculescu1† 1Ludwig Center and Howard Hughes Medical Institute, Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, Baltimore, MD 21231, USA. 2Department of Pathology and Microbiology, Center for Colon Cancer Research, and South Carolina Cancer Center, Division of Basic Research, University of South Carolina School of Medicine, Columbia, SC 29229, USA. 3Department of Medicine, Ireland Cancer Center, and Howard Hughes Medical Institute, Case Western Reserve University and University Hospitals of Cleveland, Cleveland, OH 44106, USA. 4Department of Pathology and Ireland Cancer Center, Case Western Reserve University and University Hospitals of Cleveland, Cleveland, OH 44106, USA. 5Harold C. Simmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. 6Hamon Center for Therapeutic Oncology Research and Department of Pathology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. 7Agencourt Bioscience Corporation, Beverly, MA 01915, USA. 8SoftGenetics LLC, State College, PA 16803, USA. 9Departments of Oncology, Biostatistics, and Pathology, Johns Hopkins Medical Institutions, Baltimore, MD 21205, USA.
    [Show full text]
  • Global Patterns of Changes in the Gene Expression Associated with Genesis of Cancer a Dissertation Submitted in Partial Fulfillm
    Global Patterns Of Changes In The Gene Expression Associated With Genesis Of Cancer A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy at George Mason University By Ganiraju Manyam Master of Science IIIT-Hyderabad, 2004 Bachelor of Engineering Bharatiar University, 2002 Director: Dr. Ancha Baranova, Associate Professor Department of Molecular & Microbiology Fall Semester 2009 George Mason University Fairfax, VA Copyright: 2009 Ganiraju Manyam All Rights Reserved ii DEDICATION To my parents Pattabhi Ramanna and Veera Venkata Satyavathi who introduced me to the joy of learning. To friends, family and colleagues who have contributed in work, thought, and support to this project. iii ACKNOWLEDGEMENTS I would like to thank my advisor, Dr. Ancha Baranova, whose tolerance, patience, guidance and encouragement helped me throughout the study. This dissertation would not have been possible without her ever ending support. She is very sincere and generous with her knowledge, availability, compassion, wisdom and feedback. I would also like to thank Dr. Vikas Chandhoke for funding my research generously during my doctoral study at George Mason University. Special thanks go to Dr. Patrick Gillevet, Dr. Alessandro Giuliani, Dr. Maria Stepanova who devoted their time to provide me with their valuable contributions and guidance to formulate this project. Thanks to the faculty of Molecular and Micro Biology (MMB) department, Dr. Jim Willett and Dr. Monique Vanhoek in embedding valuable thoughts to this dissertation by being in my dissertation committee. I would also like to thank the present and previous doctoral program directors, Dr. Daniel Cox and Dr. Geraldine Grant, for facilitating, allowing, and encouraging me to work in this project.
    [Show full text]
  • Anti-KPNA5 / IPOA6 Antibody (ARG55275)
    Product datasheet [email protected] ARG55275 Package: 50 μg anti-KPNA5 / IPOA6 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes KPNA5 / IPOA6 Tested Reactivity Hu, Ms Tested Application ICC/IF, IHC-P, WB Specificity This antibody is predicted to not cross-react with other Importin alpha family members. Host Rabbit Clonality Polyclonal Isotype IgG Target Name KPNA5 / IPOA6 Antigen Species Human Immunogen Synthetic peptide (18 aa) within aa. 50-100 of Human KPNA5. Conjugation Un-conjugated Alternate Names SRP6; IPOA6; Importin subunit alpha-6; Karyopherin subunit alpha-5 Application Instructions Application table Application Dilution ICC/IF 5 - 20 μg/ml IHC-P 5 μg/ml WB 1 μg/ml Application Note IHC-P: Antigen retrieval: Heat-induced antigen retrieval. * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control EL4 Cell Lysate Calculated Mw 60 kDa Properties Form Liquid Purification Affinity purification with immunogen. Buffer PBS and 0.02% Sodium azide Preservative 0.02% 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 www.arigobio.com 1/3 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 Database links GeneID: 3841 Human Swiss-port # O15131 Human Gene Symbol KPNA5 Gene Full Name karyopherin alpha 5 (importin alpha 6) Background The transport of molecules between the nucleus and the cytoplasm in eukaryotic cells is mediated by the nuclear pore complex (NPC) which consists of 60-100 proteins and is probably 120 million daltons in molecular size.
    [Show full text]
  • BIG3 Inhibits the Estrogen-Dependent Nuclear Translocation of PHB2 Via Multiple Karyopherin-Alpha Proteins in Breast Cancer Cells
    RESEARCH ARTICLE BIG3 Inhibits the Estrogen-Dependent Nuclear Translocation of PHB2 via Multiple Karyopherin-Alpha Proteins in Breast Cancer Cells Nam-Hee Kim1,2, Tetsuro Yoshimaru1, Yi-An Chen3, Taisuke Matsuo1¤, Masato Komatsu1, Yasuo Miyoshi4, Eiji Tanaka2, Mitsunori Sasa5, Kenji Mizuguchi3, Toyomasa Katagiri1* 1 Division of Genome Medicine, Institute for Genome Research, Tokushima University, Tokushima, Japan, 2 Department of Orthodontics and Dentofacial Orthopedics, Institute of Biomedical Sciences, Tokushima University Graduate School, Tokushima, Japan, 3 National Institute of Biomedical Innovation, Osaka, Japan, 4 Department of Surgery, Division of Breast and Endocrine Surgery, Hyogo College of Medicine, Hyogo, Japan, 5 Department of Surgery, Tokushima Breast Care Clinic, Tokushima, Japan ¤ Current address: Department of Advanced Pharmaceutics, School of Pharmacy, Iwate Medical University, Iwate, Japan * [email protected] OPEN ACCESS Citation: Kim N-H, Yoshimaru T, Chen Y-A, Matsuo T, Komatsu M, Miyoshi Y, et al. (2015) BIG3 Inhibits Abstract the Estrogen-Dependent Nuclear Translocation of PHB2 via Multiple Karyopherin-Alpha Proteins in We recently reported that brefeldin A-inhibited guanine nucleotide-exchange protein 3 Breast Cancer Cells. PLoS ONE 10(6): e0127707. (BIG3) binds Prohibitin 2 (PHB2) in cytoplasm, thereby causing a loss of function of the doi:10.1371/journal.pone.0127707 PHB2 tumor suppressor in the nuclei of breast cancer cells. However, little is known regard- Academic Editor: Hong Wanjin, Institute of ing the mechanism by which BIG3 inhibits the nuclear translocation of PHB2 into breast Molecular and Cell Biology, Biopolis, UNITED cancer cells. Here, we report that BIG3 blocks the estrogen (E2)-dependent nuclear import STATES of PHB2 via the karyopherin alpha (KPNA) family in breast cancer cells.
    [Show full text]
  • Host Protein Interactions
    scientificscientificreport report Structure homology and interaction redundancy for discovering virus–host protein interactions Benoıˆt de Chassey 1,Laure`ne Meyniel-Schicklin 2,3, Anne Aublin-Gex 2,3, Vincent Navratil 2,3,w, Thibaut Chantier 2,3, Patrice Andre´1,2,3 &VincentLotteau2,3+ 1Hospices Civils de Lyon, Hoˆpital de la Croix-Rousse, Laboratoire de virologie, Lyon , 2Inserm, U1111, Lyon , and 3Universite´ de Lyon, Lyon, France Virus–host interactomes are instrumental to understand global purification coupled to mass spectrometry, led to the publication perturbations of cellular functions induced by infection and of the first virus–host interactomes [3–4]. Although incorporation discover new therapies. The construction of such interactomes is, of data from different methods or variation of the same method [5] however, technically challenging and time consuming. Here we has improved the quality of the data sets, diversification of describe an original method for the prediction of high-confidence methods is still clearly needed to generate high-quality interactions between viral and human proteins through comprehensive virus–host interactomes. In addition, regarding a combination of structure and high-quality interactome data. the size of host genome and the huge diversity of viruses, millions Validation was performed for the NS1 protein of the influenza of binary interactions remain to be tested. Therefore, accurate and virus, which led to the identification of new host factors that rapid methods for the identification of cellular interactors control viral replication. controlling viral replication is a major issue and a crucial step Keywords: interactome; prediction; protein interaction; towards the selection of original therapeutic targets and drug structure; virus development.
    [Show full text]
  • Rabbit Anti-KPNA5 Antibody-SL16805R
    SunLong Biotech Co.,LTD Tel: 0086-571- 56623320 Fax:0086-571- 56623318 E-mail:[email protected] www.sunlongbiotech.com Rabbit Anti-KPNA5 antibody SL16805R Product Name: KPNA5 Chinese Name: KPNA5蛋白抗体 IMA5_HUMAN; Importin alpha 6; Importin subunit alpha 6; Importin subunit alpha-6; IPOA 6; IPOA6; Karyopherin alpha 5; Karyopherin alpha 5 importin alpha 6; Alias: Karyopherin subunit alpha 5; Karyopherin subunit alpha-5; KPNA 5; KPNA5; SRP 6; SRP6. Organism Species: Rabbit Clonality: Polyclonal React Species: Human,Mouse,Rat,Chicken,Pig,Cow,Horse,Rabbit,Sheep, ELISA=1:500-1000IHC-P=1:400-800IHC-F=1:400-800ICC=1:100-500IF=1:100- 500(Paraffin sections need antigen repair) Applications: not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user. Molecular weight: 52kDa Cellular localization: cytoplasmic Form: Lyophilized or Liquid Concentration: 1mg/ml immunogen: KLHwww.sunlongbiotech.com conjugated synthetic peptide derived from human KPNA5:1-100/538 Lsotype: IgG Purification: affinity purified by Protein A Storage Buffer: 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year Storage: when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. PubMed: PubMed The transport of molecules between the nucleus and the cytoplasm in eukaryotic cells is mediated by the nuclear pore complex (NPC) which consists of 60-100 proteins and is Product Detail: probably 120 million daltons in molecular size.
    [Show full text]
  • Product Data Sheet
    LD Biopharma, Inc. 9924 Mesa Rim Road Suite B San Diego, CA 92121 Tel: 858-876-8266 http://www.ldbiopharma.com - PRODUCT DATA SHEET - Name of Product: Recombinant Human KPNA5 Protein Catalog Number: hRP-1475 Manufacturer: LD Biopharma, Inc. Introduction The transport of molecules between the nucleus and the cytoplasm in eukaryotic cells is mediated by the nuclear pore complex (NPC) which consists of 60-100 proteins and is probably 120 million Daltons in molecular size. Small molecules (up to 70 kD) can pass through the nuclear pore by nonselective diffusion; larger molecules are transported by an active process. Most nuclear proteins contain short basic amino acid sequences known as nuclear localization signals (NLSs). Human importing subunit alpha-6 (IPOS6, also named as KPNA5) protein belongs to the importin alpha protein family and is thought to be involved in NLS-dependent protein import into the nucleus. Recent structure/ functional study of Ebola eVP24 / KPNA5 interaction indicated that KPNA5 interacts with NLS domain using different KPNA5 domains for selective nuclei transportation, such as Ebola eVP24 protein binds to KPNA5 region to selective compete with phosphorylated STAT1 for blocking host cell intrinsic innate immunity. Full-length human KPNA5 cDNA ( 538aa, derived from BC047409 ) was constructed with fully codon optimization strategy and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at its N-terminal. This protein is expressed in E.coli as inclusion bodies. The final product was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified. Gene Symbol: KPNA5 (IPOA6; SRP6) Accession Number: NP_002260 Species: Human Size: 50 µg / Vial Composition: 1.0 mg/ml, sterile-filtered, in 20 mM pH 8.0 Tris-HCl Buffer, with proprietary formulation of NaCl, KCl, EDTA, Sucrose, DTT .
    [Show full text]