Human Protein Product Data

Total Page:16

File Type:pdf, Size:1020Kb

Human Protein Product Data OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for AR09845PU-L Peflin / PEF1 (1-284, His-tag) Human Protein Product data: Product Type: Recombinant Proteins Description: Peflin / PEF1 (1-284, His-tag) human recombinant protein, 0.25 mg Species: Human Expression Host: E. coli Tag: His-tag Predicted MW: 34.5 kDa Concentration: lot specific Purity: >85% Buffer: Presentation State: Purified State: Liquid purified protein Buffer System: 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 50% glycerol, 0.2M NaCl Preparation: Liquid purified protein Protein Description: Recombinant human PEF1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Storage: Store undiluted at 2-8°C for up to two weeks or (in aliquots) at -20°C or -70°C for longer. Avoid repeated freezing and thawing. Stability: Shelf life: one year from despatch. RefSeq: NP_001346580 Locus ID: 553115 Cytogenetics: 1p35.2 Synonyms: ABP32; PEF1A Summary: This gene encodes a calcium-binding protein belonging to the penta-EF-hand protein family. The encoded protein has been shown to form a heterodimer with the programmed cell death 6 gene product and may modulate its function in Ca(2+) signaling. Alternative splicing results in multiple transcript variants and a pseudogene has been identified on chromosome 1. [provided by RefSeq, May 2010] This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 Peflin / PEF1 (1-284, His-tag) Human Protein – AR09845PU-L Product images: This product is to be used for laboratory only. Not for diagnostic or therapeutic use. ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 2 / 2.
Recommended publications
  • Noelia Díaz Blanco
    Effects of environmental factors on the gonadal transcriptome of European sea bass (Dicentrarchus labrax), juvenile growth and sex ratios Noelia Díaz Blanco Ph.D. thesis 2014 Submitted in partial fulfillment of the requirements for the Ph.D. degree from the Universitat Pompeu Fabra (UPF). This work has been carried out at the Group of Biology of Reproduction (GBR), at the Department of Renewable Marine Resources of the Institute of Marine Sciences (ICM-CSIC). Thesis supervisor: Dr. Francesc Piferrer Professor d’Investigació Institut de Ciències del Mar (ICM-CSIC) i ii A mis padres A Xavi iii iv Acknowledgements This thesis has been made possible by the support of many people who in one way or another, many times unknowingly, gave me the strength to overcome this "long and winding road". First of all, I would like to thank my supervisor, Dr. Francesc Piferrer, for his patience, guidance and wise advice throughout all this Ph.D. experience. But above all, for the trust he placed on me almost seven years ago when he offered me the opportunity to be part of his team. Thanks also for teaching me how to question always everything, for sharing with me your enthusiasm for science and for giving me the opportunity of learning from you by participating in many projects, collaborations and scientific meetings. I am also thankful to my colleagues (former and present Group of Biology of Reproduction members) for your support and encouragement throughout this journey. To the “exGBRs”, thanks for helping me with my first steps into this world. Working as an undergrad with you Dr.
    [Show full text]
  • Identification of Promoter Regions in the Human Genome by Using a Retroviral Plasmid Library-Based Functional Reporter Gene Assa
    Downloaded from genome.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Methods Identification of Promoter Regions in the Human Genome by Using a Retroviral Plasmid Library-Based Functional Reporter Gene Assay Shirin Khambata-Ford,1,5 Yueyi Liu,2 Christopher Gleason,1 Mark Dickson,3 Russ B. Altman,2 Serafim Batzoglou,4 and Richard M. Myers1,3,6 1Department of Genetics, 2Stanford Medical Informatics, 3Stanford Human Genome Center, Stanford University School of Medicine, Stanford, California 94305, USA; 4Department of Computer Science, Stanford University, Stanford, California 94305, USA Attempts to identify regulatory sequences in the human genome have involved experimental and computational methods such as cross-species sequence comparisons and the detection of transcription factor binding-site motifs in coexpressed genes. Although these strategies provide information on which genomic regions are likely to be involved in gene regulation, they do not give information on their functions. We have developed a functional selection for promoter regions in the human genome that uses a retroviral plasmid library-based system. This approach enriches for and detects promoter function of isolated DNA fragments in an in vitro cell culture assay. By using this method, we have discovered likely promoters of known and predicted genes, as well as many other putative promoter regions based on the presence of features such as CpG islands. Comparison of sequences of 858 plasmid clones selected by this assay with the human genome draft sequence indicates that a significantly higher percentage of sequences align to the 500-bp segment upstream of the transcription start sites of known genes than would be expected from random genomic sequences.
    [Show full text]
  • Proquest Dissertations
    RICE UNIVERSITY Molecular Basis of Gene Dosage Sensitivity by Jianping Chen A THESIS SUBMITTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE Doctor of Philosophy APPROVED, THESIS COMMITTEE: Ariel Fernandez, Chair Karl F. Hasselmann Professor Department of Bioengineering Rice University rn'idtfP h.tQsJUW*- Michael W. Deem, John W. Cox Professor Department of Bioengineering Department of Physics and Astronomy Rice Universit ^engineering at Rice University Jiochemistry at Baylor College of Medicine Axxttig- «J^gb/uv Laura Segaton, T.N. Law Assistant Professor Chemical and Biomolecular Engineering Rice University HOUSTON, TEXAS JANUARY 2009 UMI Number: 3362141 INFORMATION TO USERS The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleed-through, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. UMI® UMI Microform 3362141 Copyright 2009 by ProQuest LLC All rights reserved. This microform edition is protected against unauthorized copying under Title 17, United States Code. ProQuest LLC 789 East Eisenhower Parkway P.O. Box 1346 Ann Arbor, Ml 48106-1346 ABSTRACT Molecular Basis of Gene Dosage Sensitivity by JianpingChen Deviation of gene expression from normal levels has been associated with diseases. Both under- and overexpression of genes could lead to deleterious biological consequences. Dosage balance has been proposed to be a key issue of determining gene expression pheno- type.
    [Show full text]
  • Identification of Biomarkers of Metastatic Disease in Uveal
    Identification of biomarkers of metastatic disease in uveal melanoma using proteomic analyses Thesis submitted in accordance with the requirements of the University of Liverpool for the degree of Doctor in Philosophy Martina Angi June 2015 To Mario, the wind beneath my wings 2 Acknowledgments First and foremost, I would like to acknowledge my primary supervisor, Prof. Sarah Coupland, for encouraging me to undergo a PhD and for supporting me in this long journey. I am truly grateful to Dr Helen Kalirai for being the person I could always turn to, for a word of advice on cell culture as much as on parenting skills. I would also like to acknowledge Prof. Bertil Damato for being an inspiration and a mentor; and Dr Sarah Lake and Dr Joseph Slupsky for their precious advice. I would like to thank Dawn, Haleh, Fidan and Fatima for becoming my family away from home, and the other members of the LOORG for the fruitful discussions and lovely cakes. I would like to acknowledge Prof. Heinrich Heimann and the clinical team at LOOC, especially Sisters Hebbar, Johnston, Hachuela and Kaye, for their admirable dedication to UM patients and for their invaluable support to clinical research. I would also like to thank the members of staff in St Paul’s theatre and Simon Biddolph and Anna Ikin in Pathology for their precious help in sample collection. I am grateful to Dr Rosalind Jenkins who guided my first steps in the mysterious word of proteomics, and to Dr Deb Simpsons and Prof. Rob Beynon for showing me its beauty.
    [Show full text]
  • Anti-PEF1 / Peflin Antibody (ARG42993)
    Product datasheet [email protected] ARG42993 Package: 100 μl anti-PEF1 / Peflin antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes PEF1 / Peflin Tested Reactivity Hu, Ms, Rat Tested Application FACS, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name PEF1 / Peflin Antigen Species Human Immunogen Synthetic peptide of Human PEF1 / Peflin. Conjugation Un-conjugated Alternate Names ABP32; PEF1A; Peflin; PEF protein with a long N-terminal hydrophobic domain; Penta-EF hand domain- containing protein 1 Application Instructions Application table Application Dilution FACS 1:20 WB 1:1000 - 1:5000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control K562 Calculated Mw 30 kDa Observed Size ~ 31 kDa Properties Form Liquid Purification Affinity purified. Buffer 50 nM Tris-Glycine (pH 7.4), 0.15M NaCl, 0.01% Sodium azide, 40% Glycerol and 0.05% BSA. Preservative 0.01% Sodium azide Stabilizer 40% Glycerol and 0.05% BSA 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. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. www.arigobio.com 1/2 Note For laboratory research only, not for drug, diagnostic or other use. Bioinformation Gene Symbol PEF1 Gene Full Name penta-EF-hand domain containing 1 Background This gene encodes a calcium-binding protein belonging to the penta-EF-hand protein family.
    [Show full text]
  • Characterizing the Chlamydia Trachomatis Inclusion Membrane Proteome
    Characterizing the Chlamydia trachomatis inclusion membrane proteome Mary Dickinson A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy University of Washington 2019 Reading committee Kevin Hybiske, Chair Lee Ann Campbell David Sherman Program Authorized to Offer Degree: Pathobiology ©Copyright 2019 Mary Dickinson ii University of Washington Abstract Characterizing the Chlamydia trachomatis inclusion membrane proteome Mary Dickinson Chair of the Supervisory Committee: Kevin Hybiske Pathobiology Program, Department of Medicine Chlamydia trachomatis is the most common cause of bacterial sexually transmitted infection, responsible for millions of infections each year. Despite this high prevalence, the elucidation of the molecular mechanisms of Chlamydia pathogenesis has been difficult due to limitations in genetic tools and its intracellular developmental cycle. Within a host epithelial cell, chlamydiae replicate within a vacuole called the inclusion. Many Chlamydia–host interactions are thought to be mediated by the Inc family of type III secreted proteins that are anchored in the inclusion membrane, but their array of host targets are largely unknown. To investigate how the inclusion membrane proteome changes over the course of an infected cell, we have adapted the APEX system of proximity-dependent biotinylation. APEX is capable of specifically labeling proteins within a 20 nm radius in living cells. We transformed C. trachomatis to express the enzyme APEX fused to known inclusion membrane proteins, allowing biotinylation and purification of inclusion-associated proteins. Using quantitative mass spectrometry against APEX labeled samples, we identified over 400 proteins associated with the inclusion membrane at early, middle, and late stages of epithelial cell infection. This system was iii sensitive enough to detect inclusion interacting proteins early in the developmental cycle, at 8 hours post infection, a previously intractable time point.
    [Show full text]
  • NIH Public Access Author Manuscript J Proteome Res
    NIH Public Access Author Manuscript J Proteome Res. Author manuscript; available in PMC 2013 June 03. NIH-PA Author ManuscriptPublished NIH-PA Author Manuscript in final edited NIH-PA Author Manuscript form as: J Proteome Res. 2010 March 5; 9(3): 1402–1415. doi:10.1021/pr900932y. Proteomic dissection of cell type-specific H2AX-interacting protein complex associated with hepatocellular carcinoma Xiaoli Yang1, Peng Zou1, Jun Yao1, Dong Yun1, Huimin Bao1, Ruyun Du1, Jing Long1, and Xian Chen1,2,* 1Department of Chemistry and Institute of Biomedical Sciences, Fudan University, Shanghai, China 2Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, USA Abstract The replacement histone variant H2AX senses DNA double-strand breaks (DSBs) and recruits characteristic sets of proteins at its phosphorylated (γ-H2AX) foci for concurrent DNA repair. We reasoned that the H2AX interaction network, or interactome formed in the tumor-associated DNA DSB environment such as in hepatocellular carcinoma (HCC) cells, where pre-neoplastic lesions frequently occur, is indicative of HCC pathogenic status. By using an in vivo dual-tagging quantitative proteomic method, we identified 102 H2AX-specific interacting partners in HCC cells that stably expressed FLAG-tagged H2AX at close to the endogenous level. Using bioinformatics tools for data-dependent network analysis, we further found binary relationships among these interactors in defined pathway modules, implicating H2AX in a multi-functional role of coordinating a variety of biological pathways involved in DNA damage recognition and DNA repair, apoptosis, nucleic acid metabolism, Ca2+-binding signaling, cell cycle, etc. Furthermore our observations suggest that these pathways interconnect through key pathway components or H2AX interactors.
    [Show full text]
  • Global Proteomic Detection of Native, Stable, Soluble Human Protein Complexes
    GLOBAL PROTEOMIC DETECTION OF NATIVE, STABLE, SOLUBLE HUMAN PROTEIN COMPLEXES by Pierre Claver Havugimana A thesis submitted in conformity with the requirements for the degree of Doctor of Philosophy Graduate Department of Molecular Genetics University of Toronto © Copyright by Pierre Claver Havugimana 2012 Global Proteomic Detection of Native, Stable, Soluble Human Protein Complexes Pierre Claver Havugimana Doctor of Philosophy Graduate Department of Molecular Genetics University of Toronto 2012 Abstract Protein complexes are critical to virtually every biological process performed by living organisms. The cellular “interactome”, or set of physical protein-protein interactions, is of particular interest, but no comprehensive study of human multi-protein complexes has yet been reported. In this Thesis, I describe the development of a novel high-throughput profiling method, which I term Fractionomic Profiling-Mass Spectrometry (or FP-MS), in which biochemical fractionation using non-denaturing high performance liquid chromatography (HPLC), as an alternative to affinity purification (e.g. TAP tagging) or immuno-precipitation, is coupled with tandem mass spectrometry-based protein identification for the global detection of stably- associated protein complexes in mammalian cells or tissues. Using a cell culture model system, I document proof-of-principle experiments confirming the suitability of this method for monitoring large numbers of soluble, stable protein complexes from either crude protein extracts or enriched sub-cellular compartments. Next, I document how, using orthogonal functional genomics information generated in collaboration with computational biology groups as filters, we applied FP-MS co-fractionation profiling to construct a high-quality map of 622 predicted unique soluble human protein complexes that could be biochemically enriched from HeLa and HEK293 nuclear and cytoplasmic extracts.
    [Show full text]
  • Atlas Journal
    Atlas of Genetics and Cytogenetics in Oncology and Haematology Home Genes Leukemias Solid Tumours Cancer-Prone Deep Insight Portal Teaching X Y 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 NA Atlas Journal Atlas Journal versus Atlas Database: the accumulation of the issues of the Journal constitutes the body of the Database/Text-Book. TABLE OF CONTENTS Volume 12, Number 5, Sep-Oct 2008 Previous Issue / Next Issue Genes XAF1 (XIAP associated factor-1) (17p13.2). Stéphanie Plenchette, Wai Gin Fong, Robert G Korneluk. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 668-673. [Full Text] [PDF] URL : http://atlasgeneticsoncology.org/Genes/XAF1ID44095ch17p13.html WWP1 (WW domain containing E3 ubiquitin protein ligase 1) (8q21.3). Ceshi Chen. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 674-680. [Full Text] [PDF] URL : http://atlasgeneticsoncology.org/Genes/WWP1ID42993ch8q21.html TSPAN1 (tetraspanin 1) (1p34.1). David Murray, Peter Doran. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 681-683. [Full Text] [PDF] URL : http://atlasgeneticsoncology.org/Genes/TSPAN1ID44178ch1p34.html TCL1B (T-cell leukemia/lymphoma 1B) (14q32.13). Herbert Eradat, Michael A Teitell. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 684-686. [Full Text] [PDF] URL : http://atlasgeneticsoncology.org/Genes/TCL1BID354ch14q32.html PVRL4 (poliovirus receptor-related 4) (1q23.3). Marc Lopez. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 687-690. [Full Text] [PDF] URL : http://atlasgeneticsoncology.org/Genes/PVRL4ID44141ch1q23.html PTTG1IP (pituitary tumor-transforming 1 interacting protein) (21q22.3). Vicki Smith, Chris McCabe. Atlas Genet Cytogenet Oncol Haematol 2008; 12 (5): 691-694.
    [Show full text]
  • Association of PDCD6 Polymorphisms with the Risk of Cancer: Evidence from a Meta-Analysis
    www.oncotarget.com Oncotarget, 2018, Vol. 9, (No. 37), pp: 24857-24868 Review Association of PDCD6 polymorphisms with the risk of cancer: Evidence from a meta-analysis Mohammad Hashemi1,2, Gholamreza Bahari2, Jarosław Markowski3, Andrzej Małecki4, Marek J. Łos5,8 and Saeid Ghavami6,7 1Cellular and Molecular Research Center, Zahedan University of Medical Sciences, Zahedan, Iran 2Department of Clinical Biochemistry, School of Medicine, Zahedan University of Medical Sciences, Zahedan, Iran 3ENT Department, School of Medicine, Medical University of Silesia in Katowice, Katowice, Poland 4Faculty of Physiotherapy, The Jerzy Kukuczka Academy of Physical Education in Katowice, Katowice, Poland 5Department of Molecular Biology, School of Pharmacy with the Division of Laboratory Medicine in Sosnowiec, Medical University of Silesia in Katowice, Katowice, Poland 6Department of Human Anatomy and Cell Science, Max Rady College of Medicine, Rady Faculty of Health Sciences, University of Manitoba, Winnipeg, MB, Canada 7Health Policy Research Center, Institute of Health, Shiraz University of Medical Sciences, Shiraz, Iran 8Centre de Biophysique Moléculaire, CNRS, Rue Charles Sadron, Orleans, France Correspondence to: Mohammad Hashemi, email: [email protected]; [email protected] Marek J. Łos, email: [email protected] Keywords: PDCD6; meta-analysis; cancer; risk; endometrial cancer Received: January 08, 2018 Accepted: April 12, 2018 Published: May 15, 2018 Copyright: Hashemi et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License 3.0 (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. ABSTRACT This study was designed to evaluate the relationship between Programmed cell death protein 6 (PDCD6) polymorphisms and cancer susceptibility.
    [Show full text]
  • Characterization of the Regulation of the Er Stress Response by the Dna Repair Enzyme Aag
    DECIPHERING THE CROSSTALK: CHARACTERIZATION OF THE REGULATION OF THE ER STRESS RESPONSE BY THE DNA REPAIR ENZYME AAG Clara Forrer Charlier Faculty of Health and Medical Sciences Department of Biochemistry and Physiology This thesis is submitted for the degree of Doctor of Philosophy June 2018 DECIPHERING THE CROSSTALK: CHARACTERIZATION OF THE REGULATION OF THE ER STRESS RESPONSE BY THE DNA REPAIR ENZYME AAG- Clara Forrer Charlier – June 2018 SUMMARY The genome is a very dynamic store of genetic information and constantly threatened by endogenous and exogenous damaging agents. To maintain fidelity of the information stored, several robust and overlapping repair pathways, such as the Base Excision Repair (BER) pathway, have evolved. The main BER glycosylase responsible for repairing alkylation DNA damage is the alkyladenine DNA glycosylase (AAG). Repair initiated by AAG can lead to accumulation of cytotoxic intermediates. Here, we report the involvement of AAG in the elicitation of the unfolded protein response (UPR), a mechanism triggered to restore proteostasis in the cell whose dysfunction is implicated in diseases like diabetes, Alzheimer’s disease and cancer. Firstly, we determined that not only human ARPE-19 cells were capable of eliciting the UPR, but that an alkylating agent, methyl methanesulfonate (MMS), also triggers the response, and that in the absence of AAG the response is greatly diminished. Our luciferase reporter assay indicates that the response is activated on multiple branches (IRE1 and ATF6) on both AAG-proficient and deficient cells. Although no transcriptional induction of UPR markers was detected by RT-qPCR at 6 hours post MMS treatment, preliminary western-blot data at 6 and 24h, show activation of key UPR markers (p-eIF2α, BiP and XBP-1) upon MMS treatment in wild-type cells and little or no activation on AAG -/-.
    [Show full text]
  • 1817 Alg-2, a Multifunctional
    [Frontiers in Bioscience 9, 1817-1832, May 1, 2004] ALG-2, A MULTIFUNCTIONAL CALCIUM BINDING PROTEIN? Svetlana Tarabykina 1, Jens Mollerup, Pernille Winding and Martin W. Berchtold Department of Molecular Cell Biology, Institute of Molecular Biology, University of Copenhagen, Øster Farimagsgade 2A, 1353 Copenhagen K, Denmark, 1 Novo Nordisk A/S, Dept. of Cancer and ImmunoBiology, Novo Nordisk Park, G8.1.21, 2760 Måløv, Denmark TABLE OF CONTENTS 1. Abstract 2. Introduction 3. ALG-2 is a high affinity calcium binding protein of the PEF family 3.1. Ca2+-dependent conformational changes 4. The three dimensional structure of ALG-2 differs from that of other PEF proteins 5. ALG-2 forms stable homodimers 6. Heterodimerization of ALG-2 and structural requirements for target interaction 7. Ubiquitous expression of ALG-2 and Ca2+-dependent subcellular localisation 7.1. Antibodies against ALG-2 7.2. Ca2+-dependent translocation of ALG-2 and other PEF proteins 8. Possible functions of ALG-2 8.1. Apoptosis 8.2. Proliferation 8.3. Exocytosis / endocytosis / protein trafficking 8.4. Development 9. ALG-2 is evolutionarily conserved 10. ALG-2 gene disruption reveals no phenotype 11. Perspectives 12. Acknowledgements 13. References 1. ABSTRACT ALG-2 was originally discovered as a pro- ALG-2, an EF-hand type calcium binding protein, seemed apoptotic protein in a genetic screen. Due to its ability to to have a pro-apoptotic function ALG-3, a truncated form bind calcium with high affinity it was postulated to provide of the familial Alzheimer´s disease gene presenilin 2, a link between the known effect of calcium in programmed rescued T cells from apoptosis induced by cross-linking of cell death and the molecular death execution machinery.
    [Show full text]