DOCSLIB.ORG

Monoclonal Anti-Human Adipon

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Monoclonal Anti-Human Adipon monocl AAD0602 Monoclonal anti-adiponectin antibody (clone 1G12) 100ul 311-Eur ATGen onal monocl AAD0602 Monoclonal anti-adiponectin antibody (clone 1G12) 50ul 227-Eur ATGen onal monocl AAD0614 Monoclonal anti-human adiponectin antibody (clone 5H7) 100ul 311-Eur ATGen onal monocl AAD0614 Monoclonal anti-human adiponectin antibody (clone 5H7) 50ul 227-Eur ATGen onal monocl AAK0604 Monoclonal anti-human AK3 antibody (clone SJB3-36) 100ul 354-Eur ATGen onal monocl AAK0604 Monoclonal anti-human AK3 antibody (clone SJB3-36) 50ul 252-Eur ATGen onal monocl AAP0501 Monoclonal anti-human ANGPTL3 antibody (clone 1D10 ) 100ul 284-Eur ATGen onal monocl AAP0501 Monoclonal anti-human ANGPTL3 antibody (clone 1D10 ) 50ul 191-Eur ATGen onal monocl AAP0501 Monoclonal anti-human ANGPTL3 antibody (clone 1D10) 100ul 311-Eur ATGen onal monocl AAP0501 Monoclonal anti-human ANGPTL3 antibody (clone 1D10) 50ul 227-Eur ATGen onal monocl AAP0836 Monoclonal anti-human APP antibody (clone J4H9) 100ul 311-Eur ATGen onal monocl AAP0836 Monoclonal anti-human APP antibody (clone J4H9) 50ul 227-Eur ATGen onal monocl ABH0708 Monoclonal anti-human BHMT antibody (clone 3D6 ) 100ul 284-Eur ATGen onal monocl ABH0708 Monoclonal anti-human BHMT antibody (clone 3D6 ) 50ul 191-Eur ATGen onal monocl ABH0708 Monoclonal anti-human BHMT antibody (clone 3D6) 100ul 311-Eur ATGen onal monocl ABH0708 Monoclonal anti-human BHMT antibody (clone 3D6) 50ul 227-Eur ATGen onal monocl ABI0923 Monoclonal anti-human BID antibody (clone 4D3) 100ul 284-Eur ATGen onal monocl ABI0923 Monoclonal anti-human BID antibody (clone 4D3) 50ul 191-Eur ATGen onal monocl ABL0813 Monoclonal anti-BLyS antibody (clone H4-C7 ) 100ul 284-Eur ATGen onal monocl ABL0813 Monoclonal anti-BLyS antibody (clone H4-C7 ) 50ul 191-Eur ATGen onal monocl ABL0813 Monoclonal anti-BLyS antibody (clone H4-C7) 100ul 311-Eur ATGen onal monocl ABL0813 Monoclonal anti-BLyS antibody (clone H4-C7) 50ul 227-Eur ATGen onal monocl ABM0615 Monoclonal anti-human BMP7 antibody (clone 4E7) 100ul 311-Eur ATGen onal monocl ABM0615 Monoclonal anti-human BMP7 antibody (clone 4E7) 50ul 227-Eur ATGen onal monocl ABP0609 Monoclonal anti-human C_EBP- 100ul 283-Eur ATGen onal monocl ABP0609 Monoclonal anti-human C_EBP- 50ul 190-Eur ATGen onal monocl ABP0609 Monoclonal anti-human C_EBP-â antibody (clone 47A1) 50ul 201-Eur ATGen onal monocl ABP0609 Monoclonal anti-human C_EBP-â antibody (clone 47A1) 100ul 297-Eur ATGen onal monocl ABP0609 Monoclonal anti-human C_EBP-β antibody (clone 47A1) 100ul 311-Eur ATGen onal monocl ABP0609 Monoclonal anti-human C_EBP-β antibody (clone 47A1) 50ul 227-Eur ATGen onal Monoclonal anti-human a crystallin A antibody (clone monocl ACA0401 c9F2) 100ul 311-Eur ATGen onal Monoclonal anti-human a crystallin A antibody (clone monocl ACA0401 c9F2) 50ul 227-Eur ATGen onal monocl ACA0830 Monoclonal anti-human Calmodulin antibody (clone J4D8) 100ul 311-Eur ATGen onal monocl ACA0830 Monoclonal anti-human Calmodulin antibody (clone J4D8) 50ul 227-Eur ATGen onal monocl ACB0617 Monoclonal anti-human 100ul 283-Eur ATGen onal monocl ACB0617 Monoclonal anti-human 50ul 190-Eur ATGen onal Monoclonal anti-human á-Crystallin B antibody (clone monocl ACB0617 2E8) 100ul 297-Eur ATGen onal Monoclonal anti-human á-Crystallin B antibody (clone monocl ACB0617 2E8) 50ul 201-Eur ATGen onal Monoclonal anti-human α-Crystallin B antibody (clone monocl ACB0617 2E8) 100ul 311-Eur ATGen onal Monoclonal anti-human α-Crystallin B antibody (clone monocl ACB0617 2E8) 50ul 227-Eur ATGen onal Monoclonal anti-human Cyclophilin B antibody ( clone monocl ACB0825 k2E2) 100ul 311-Eur ATGen onal Monoclonal anti-human Cyclophilin B antibody ( clone monocl ACB0825 k2E2) 50ul 227-Eur ATGen onal monocl ACC0810 Monoclonal anti-human CCR6 antibody (clone 4C6 ) 100ul 284-Eur ATGen onal monocl ACC0810 Monoclonal anti-human CCR6 antibody (clone 4C6 ) 50ul 191-Eur ATGen onal monocl ACC0810 Monoclonal anti-human CCR6 antibody (clone 4C6) 100ul 311-Eur ATGen onal monocl ACC0810 Monoclonal anti-human CCR6 antibody (clone 4C6) 50ul 227-Eur ATGen onal monocl ACD0802 Monoclonal anti-human CD45 antibody (clone 3G4 ) 100ul 284-Eur ATGen onal monocl ACD0802 Monoclonal anti-human CD45 antibody (clone 3G4 ) 50ul 191-Eur ATGen onal monocl ACD0802 Monoclonal anti-human CD45 antibody (clone 3G4) 100ul 311-Eur ATGen onal monocl ACD0802 Monoclonal anti-human CD45 antibody (clone 3G4) 50ul 227-Eur ATGen onal monocl ACD0806 Monoclonal anti-human CD73 antibody (clone 2B6 ) 100ul 284-Eur ATGen onal monocl ACD0806 Monoclonal anti-human CD73 antibody (clone 2B6 ) 50ul 191-Eur ATGen onal monocl ACD0806 Monoclonal anti-human CD73 antibody (clone 2B6) 100ul 311-Eur ATGen onal monocl ACD0806 Monoclonal anti-human CD73 antibody (clone 2B6) 50ul 227-Eur ATGen onal monocl ACD0809 Monoclonal anti-human CD45 antibody (clone 2H12 ) 100ul 284-Eur ATGen onal monocl ACD0809 Monoclonal anti-human CD45 antibody (clone 2H12 ) 50ul 191-Eur ATGen onal monocl ACD0809 Monoclonal anti-human CD45 antibody (clone 2H12) 100ul 311-Eur ATGen onal monocl ACD0809 Monoclonal anti-human CD45 antibody (clone 2H12) 50ul 227-Eur ATGen onal monocl ACD0823 Monoclonal anti-human CD29 antibody (clone k2D5) 100ul 311-Eur ATGen onal monocl ACD0823 Monoclonal anti-human CD29 antibody (clone k2D5) 50ul 227-Eur ATGen onal monocl ACD0826 Monoclonal anti-human CD44 antibody (clone 5C10) 100ul 311-Eur ATGen onal monocl ACD0826 Monoclonal anti-human CD44 antibody (clone 5C10) 50ul 227-Eur ATGen onal Monoclonal anti-human Chromogranin A antibody (clone monocl ACG0921 3A5) 100ul 311-Eur ATGen onal Monoclonal anti-human Chromogranin A antibody (clone monocl ACG0921 3A5) 50ul 227-Eur ATGen onal monocl ACH0605 Monoclonal anti-human Cathepsin H antibody (clone 3G8) 100ul 311-Eur ATGen onal monocl ACH0605 Monoclonal anti-human Cathepsin H antibody (clone 3G8) 50ul 227-Eur ATGen onal Monoclonal anti-human Cathepsin D antibody (clone 4G2 monocl ACH0627 ) 100ul 284-Eur ATGen onal Monoclonal anti-human Cathepsin D antibody (clone 4G2 monocl ACH0627 ) 50ul 191-Eur ATGen onal monocl ACH0627 Monoclonal anti-human Cathepsin D antibody (clone 4G2) 100ul 311-Eur ATGen onal monocl ACH0627 Monoclonal anti-human Cathepsin D antibody (clone 4G2) 50ul 227-Eur ATGen onal monocl ACI0807 Monoclonal anti-human CIB1 antibody (clone 1D1 ) 100ul 284-Eur ATGen onal monocl ACI0807 Monoclonal anti-human CIB1 antibody (clone 1D1 ) 50ul 191-Eur ATGen onal monocl ACI0807 Monoclonal anti-human CIB1 antibody (clone 1D1) 100ul 311-Eur ATGen onal monocl ACI0807 Monoclonal anti-human CIB1 antibody (clone 1D1) 50ul 227-Eur ATGen onal monocl ACL0711 Monoclonal anti-human Clusterin antibody (clone 1A11 ) 100ul 284-Eur ATGen onal monocl ACL0711 Monoclonal anti-human Clusterin antibody (clone 1A11 ) 50ul 191-Eur ATGen onal monocl ACL0711 Monoclonal anti-human Clusterin antibody (clone 1A11) 100ul 311-Eur ATGen onal monocl ACL0711 Monoclonal anti-human Clusterin antibody (clone 1A11) 50ul 227-Eur ATGen onal monocl ACO0927 Monoclonal anti-human Cofilin 1 antibody (clone AT1C1) 100ul 284-Eur ATGen onal monocl ACO0927 Monoclonal anti-human Cofilin 1 antibody (clone AT1C1) 50ul 191-Eur ATGen onal monocl ACP0628 Monoclonal anti-human Caspase-2 antibody (clone 1C10 ) 100ul 284-Eur ATGen onal monocl ACP0628 Monoclonal anti-human Caspase-2 antibody (clone 1C10 ) 50ul 191-Eur ATGen onal monocl ACP0628 Monoclonal anti-human Caspase-2 antibody (clone 1C10) 100ul 311-Eur ATGen onal monocl ACP0628 Monoclonal anti-human Caspase-2 antibody (clone 1C10) 50ul 227-Eur ATGen onal monocl ACR0631 Monoclonal anti-human CRP antibody (clone 5A9 ) 100ul 284-Eur ATGen onal monocl ACR0631 Monoclonal anti-human CRP antibody (clone 5A9 ) 50ul 191-Eur ATGen onal monocl ACR0631 Monoclonal anti-human CRP antibody (clone 5A9) 100ul 311-Eur ATGen onal monocl ACR0631 Monoclonal anti-human CRP antibody (clone 5A9) 50ul 227-Eur ATGen onal monocl ACS0820 Monoclonal anti-human CSTB antibody (clone 2F1) 100ul 311-Eur ATGen onal monocl ACS0820 Monoclonal anti-human CSTB antibody (clone 2F1) 50ul 227-Eur ATGen onal monocl ACT0905 Monoclonal anti-human Cathepsin L antibody (clone 2H7 ) 100ul 284-Eur ATGen onal monocl ACT0905 Monoclonal anti-human Cathepsin L antibody (clone 2H7 ) 50ul 191-Eur ATGen onal monocl ACT0905 Monoclonal anti-human Cathepsin L antibody (clone 2H7) 100ul 311-Eur ATGen onal monocl ACT0905 Monoclonal anti-human Cathepsin L antibody (clone 2H7) 50ul 227-Eur ATGen onal monocl ACY0838 Monoclonal anti-human CYR61 antibody (clone3H3 ) 100ul 284-Eur ATGen onal monocl ACY0838 Monoclonal anti-human CYR61 antibody (clone3H3 ) 50ul 191-Eur ATGen onal monocl ACY0838 Monoclonal anti-human CYR61 antibody (clone3H3) 100ul 311-Eur ATGen onal monocl ACY0838 Monoclonal anti-human CYR61 antibody (clone3H3) 50ul 227-Eur ATGen onal monocl ADA0925 Monoclonal anti-human DACT3 antibody (clone 2A5) 100ul 284-Eur ATGen onal monocl ADA0925 Monoclonal anti-human DACT3 antibody (clone 2A5) 50ul 191-Eur ATGen onal recom ADI0501 Adiponectin Human, Recombinant, E.coli 0.5mg 953-Eur ATGen binant recom ADI0501 Adiponectin Human, Recombinant, E.coli 100ug 352-Eur ATGen binant mAdiponectin, 18- 247aa, Mouse, His-tagged, recom ADI0702 Recombinant, E.coli 0.5mg 863-Eur ATGen binant mAdiponectin, 18- 247aa, Mouse, His-tagged, recom ADI0702 Recombinant, E.coli 100ug 322-Eur ATGen binant Adiponectin(111-247aa; globular domain), Mouse, recom ADI3001 Recombinant, expressed in E.coli 1mg 502-Eur ATGen binant Adiponectin(111-247aa; globular domain), Mouse, recom ADI3001 Recombinant, expressed in E.coli 100ug 202-Eur ATGen binant Adiponectin(111-247aa;
Load more

Recommended publications
  • UBE2M (Mouse; Full Length), Pab
    UBE2M (mouse; full length), pAb Alternate Names: Nedd8-conjugating enzyme, Ubc12, UBC-RS2, UBC12. Cat. No. 68-0025-100 Quantity: 100 µg Lot. No. 30262 Storage: -20˚C FOR RESEARCH USE ONLY NOT FOR USE IN HUMANS CERTIFICATE OF ANALYSIS Page 1 of 2 This antibody was developed and Physical Characteristics validated by the Medical Research Council Protein Phosphorylation and Quantity: 100 μg Formulation: phosphate-buffered Ubiquitylation Unit (University of saline Dundee, Dundee, UK). Concentration: to be provided on shipping Specificity:detects Ube2M at ~22 kDa Source: sheep polyclonal antibody Reactivity: mouse; other species not Background tested. Immunogen: mouse Ube2M (residues 1-183) [GST-tagged] Stability/Storage: 12 months at The enzymes of the NEDDylation pathway -20˚C; aliquot as required play a pivotal role in a number of cellular Purification:affinity-purified using processes including the indirect regula- immobilized immunogen tion and targeting of substrate proteins for proteasomal degradation. Three classes of enzymes are involved in the process of NEDDylation; the ubiquitin-like activating Research Applications and Quality Assurance enzyme APP-BP1/Uba3 (E1), the ubiquitin- Western Immunoblotting: Immunoprecipitation: like conjugating enzymes (E2s) and pro- Use 0.5 µg/ml Not tested tein ligases (E3s). UBE2M is a member of the E2 conjugating enzyme family and the gene for human UBE2M was first de- scribed by Osaka et al. (1998) and shares Dot Blotting Analysis: By dot blot assay the specific 42% sequence identity with yeast UBE2M. recognition of recombinant A trapped ubiquitin like activation complex Ube2M protein was observed has been described for the NEDD8 pathway under native and denaturing comprising, the E1 APP-BP1/Uba3, two conditions when probed with NEDD8 molecules, UBE2M and MgATP.
    [Show full text]
  • Identification of the Binding Partners for Hspb2 and Cryab Reveals
    Brigham Young University BYU ScholarsArchive Theses and Dissertations 2013-12-12 Identification of the Binding arP tners for HspB2 and CryAB Reveals Myofibril and Mitochondrial Protein Interactions and Non- Redundant Roles for Small Heat Shock Proteins Kelsey Murphey Langston Brigham Young University - Provo Follow this and additional works at: https://scholarsarchive.byu.edu/etd Part of the Microbiology Commons BYU ScholarsArchive Citation Langston, Kelsey Murphey, "Identification of the Binding Partners for HspB2 and CryAB Reveals Myofibril and Mitochondrial Protein Interactions and Non-Redundant Roles for Small Heat Shock Proteins" (2013). Theses and Dissertations. 3822. https://scholarsarchive.byu.edu/etd/3822 This Thesis is brought to you for free and open access by BYU ScholarsArchive. It has been accepted for inclusion in Theses and Dissertations by an authorized administrator of BYU ScholarsArchive. For more information, please contact [email protected], [email protected]. Identification of the Binding Partners for HspB2 and CryAB Reveals Myofibril and Mitochondrial Protein Interactions and Non-Redundant Roles for Small Heat Shock Proteins Kelsey Langston A thesis submitted to the faculty of Brigham Young University in partial fulfillment of the requirements for the degree of Master of Science Julianne H. Grose, Chair William R. McCleary Brian Poole Department of Microbiology and Molecular Biology Brigham Young University December 2013 Copyright © 2013 Kelsey Langston All Rights Reserved ABSTRACT Identification of the Binding Partners for HspB2 and CryAB Reveals Myofibril and Mitochondrial Protein Interactors and Non-Redundant Roles for Small Heat Shock Proteins Kelsey Langston Department of Microbiology and Molecular Biology, BYU Master of Science Small Heat Shock Proteins (sHSP) are molecular chaperones that play protective roles in cell survival and have been shown to possess chaperone activity.
    [Show full text]
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
    [Show full text]
  • Material Data Sheet
    MATERIAL DATA SHEET Recombinant Human His6 UBE2N/UBE2V2 Complex Cat. # E2­666 Ubiquitin conjugating Enzyme E2N (UBE2N), also known as Ubiquitin conjugating Enzyme 13 (Ubc13), forms a functional complex with the catalytically inactive UBE2V2 (human homologue of yeast MMS2) protein (1). Human UBE2N/Ubc13 shares 100% and 99% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively, while human UBE2V2 shares 99% aa sequence identity with its mouse and rat orthologs. The UBE2N/UBE2V2 Complex functions with Ubiquitin ligases (E3s), including RNF111 and RNF8, to synthesize Lys63­linked Ubiquitin chains (2,3) that can either be unanchored or attached to target proteins (4, 5). The UBE2N/UBE2V2 complex has important roles in facilitating responses to various forms of DNA damage (2, 6). Product Information Quantity: 100 µg | 50 µg MW: 18 kDa (UBE2N), 17 kDa (UBE2V2) Source: E. coli­derived Contains an N­terminal 6­His tag Accession # P61088 (UBE2N)/Q15819 (UBE2V2) Stock: 0.88 mg/ml (25 μM) in 50 mM HEPES pH 7.5, 200 mM NaCl, 10% Glycerol (v/v), 2 mM TCEP Purity: >95%, by SDS­PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain. Rev. 5/22/2014 Page 1 of 2 www.bostonbiochem.com Boston Biochem products are available via the R&D Systems distributor network. USA & CANADA Tel: (800) 343-7475 EUROPE Tel: +44 (0)1235 529449 CHINA Tel: +86 (21) 52380373 Use & Storage Use: Recombinant Human His6­UBE2N/UBE2V2 Complex is a member of the Ubiquitin conjugating (E2) enzyme family that receives Ubiquitin from a Ubiquitin activating (E1) enzyme and subsequently interacts with a Ubiquitin ligase (E3) to conjugate Ubiquitin to substrate proteins.
    [Show full text]
  • The Ubiquitination Enzymes of Leishmania Mexicana
    The ubiquitination enzymes of Leishmania mexicana Rebecca Jayne Burge Doctor of Philosophy University of York Biology October 2020 Abstract Post-translational modifications such as ubiquitination are important for orchestrating the cellular transformations that occur as the Leishmania parasite differentiates between its main morphological forms, the promastigote and amastigote. Although 20 deubiquitinating enzymes (DUBs) have been partially characterised in Leishmania mexicana, little is known about the role of E1 ubiquitin-activating (E1), E2 ubiquitin- conjugating (E2) and E3 ubiquitin ligase (E3) enzymes in this parasite. Using bioinformatic methods, 2 E1, 13 E2 and 79 E3 genes were identified in the L. mexicana genome. Subsequently, bar-seq analysis of 23 E1, E2 and HECT/RBR E3 null mutants generated in promastigotes using CRISPR-Cas9 revealed that the E2s UBC1/CDC34, UBC2 and UEV1 and the HECT E3 ligase HECT2 are required for successful promastigote to amastigote differentiation and UBA1b, UBC9, UBC14, HECT7 and HECT11 are required for normal proliferation during mouse infection. Null mutants could not be generated for the E1 UBA1a or the E2s UBC3, UBC7, UBC12 and UBC13, suggesting these genes are essential in promastigotes. X-ray crystal structure analysis of UBC2 and UEV1, orthologues of human UBE2N and UBE2V1/UBE2V2 respectively, revealed a heterodimer with a highly conserved structure and interface. Furthermore, recombinant L. mexicana UBA1a was found to load ubiquitin onto UBC2, allowing UBC2- UEV1 to form K63-linked di-ubiquitin chains in vitro. UBC2 was also shown to cooperate with human E3s RNF8 and BIRC2 in vitro to form non-K63-linked polyubiquitin chains, but association of UBC2 with UEV1 inhibits this ability.
    [Show full text]
  • Uncovering Ubiquitin and Ubiquitin-Like Signaling Networks Alfred C
    REVIEW pubs.acs.org/CR Uncovering Ubiquitin and Ubiquitin-like Signaling Networks Alfred C. O. Vertegaal* Department of Molecular Cell Biology, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, The Netherlands CONTENTS 8. Crosstalk between Post-Translational Modifications 7934 1. Introduction 7923 8.1. Crosstalk between Phosphorylation and 1.1. Ubiquitin and Ubiquitin-like Proteins 7924 Ubiquitylation 7934 1.2. Quantitative Proteomics 7924 8.2. Phosphorylation-Dependent SUMOylation 7935 8.3. Competition between Different Lysine 1.3. Setting the Scenery: Mass Spectrometry Modifications 7935 Based Investigation of Phosphorylation 8.4. Crosstalk between SUMOylation and the and Acetylation 7925 UbiquitinÀProteasome System 7935 2. Ubiquitin and Ubiquitin-like Protein Purification 9. Conclusions and Future Perspectives 7935 Approaches 7925 Author Information 7935 2.1. Epitope-Tagged Ubiquitin and Ubiquitin-like Biography 7935 Proteins 7925 Acknowledgment 7936 2.2. Traps Based on Ubiquitin- and Ubiquitin-like References 7936 Binding Domains 7926 2.3. Antibody-Based Purification of Ubiquitin and Ubiquitin-like Proteins 7926 1. INTRODUCTION 2.4. Challenges and Pitfalls 7926 Proteomes are significantly more complex than genomes 2.5. Summary 7926 and transcriptomes due to protein processing and extensive 3. Ubiquitin Proteomics 7927 post-translational modification (PTM) of proteins. Hundreds ff fi 3.1. Proteomic Studies Employing Tagged of di erent modi cations exist. Release 66 of the RESID database1 (http://www.ebi.ac.uk/RESID/) contains 559 dif- Ubiquitin 7927 ferent modifications, including small chemical modifications 3.2. Ubiquitin Binding Domains 7927 such as phosphorylation, acetylation, and methylation and mod- 3.3. Anti-Ubiquitin Antibodies 7927 ification by small proteins, including ubiquitin and ubiquitin- 3.4.
    [Show full text]
  • WO 2019/079361 Al 25 April 2019 (25.04.2019) W 1P O PCT
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization I International Bureau (10) International Publication Number (43) International Publication Date WO 2019/079361 Al 25 April 2019 (25.04.2019) W 1P O PCT (51) International Patent Classification: CA, CH, CL, CN, CO, CR, CU, CZ, DE, DJ, DK, DM, DO, C12Q 1/68 (2018.01) A61P 31/18 (2006.01) DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, C12Q 1/70 (2006.01) HR, HU, ID, IL, IN, IR, IS, JO, JP, KE, KG, KH, KN, KP, KR, KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, (21) International Application Number: MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, PCT/US2018/056167 OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, (22) International Filing Date: SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, 16 October 2018 (16. 10.2018) TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (25) Filing Language: English (84) Designated States (unless otherwise indicated, for every kind of regional protection available): ARIPO (BW, GH, (26) Publication Language: English GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, TZ, (30) Priority Data: UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, 62/573,025 16 October 2017 (16. 10.2017) US TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, EE, ES, FI, FR, GB, GR, HR, HU, ΓΕ , IS, IT, LT, LU, LV, (71) Applicant: MASSACHUSETTS INSTITUTE OF MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, SM, TECHNOLOGY [US/US]; 77 Massachusetts Avenue, TR), OAPI (BF, BJ, CF, CG, CI, CM, GA, GN, GQ, GW, Cambridge, Massachusetts 02139 (US).
    [Show full text]
  • UBE2M Recombinant Protein Cat
    UBE2M Recombinant Protein Cat. No.: 92-178 UBE2M Recombinant Protein Specifications SPECIES: Human SOURCE SPECIES: E. coli SEQUENCE: Met1-Lys183 FUSION TAG: Tag Free TESTED APPLICATIONS: APPLICATIONS: This recombinant protein can be used for biological assays. For research use only. PREDICTED MOLECULAR 20.9 kD WEIGHT: Properties Greater than 95% as determined by reducing SDS-PAGE. PURITY: Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. PHYSICAL STATE: Liquid Supplied as a 0.2 um filtered solution of 50mM HEPES,pH 7.5,2mM DTT,150mM BUFFER: NaCl,10%glycerol . It is not recommended to reconstitute to a concentration less than 100 ug/ml. September 29, 2021 1 https://www.prosci-inc.com/ube2m-recombinant-protein-92-178.html Store at -20˚C, stable for 6 months after receipt. STORAGE CONDITIONS: Please aliquot the reconstituted solution to minimize freeze-thaw cycles. Additional Info OFFICIAL SYMBOL: UBE2M NEDD8-conjugating enzyme Ubc12, NEDD8 carrier protein, NEDD8 protein ligase, ALTERNATE NAMES: Ubiquitin-conjugating enzyme E2 M, UBC12, UBE2M ACCESSION NO.: P61081 GENE ID: 9040 Background and References UBE2M is a member of the E2 ubiquitin-conjugating enzyme family. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin- conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This protein is linked with a ubiquitin-like protein, NEDD8, which can be conjugated to cellular proteins, such as Cdc53/culin. UBE2M accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 BACKGROUND: complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4.
    [Show full text]
  • UBE2V2 Rabbit Pab
    Leader in Biomolecular Solutions for Life Science UBE2V2 Rabbit pAb Catalog No.: A6998 Basic Information Background Catalog No. Ubiquitin-conjugating enzyme E2 variant proteins constitute a distinct subfamily within A6998 the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical for the catalytic activity of Observed MW E2s. The protein encoded by this gene also shares homology with ubiquitin-conjugating 16kDa enzyme E2 variant 1 and yeast MMS2 gene product. It may be involved in the differentiation of monocytes and enterocytes. Calculated MW 16kDa Category Primary antibody Applications WB, IHC Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 7336 Q15819 IHC 1:50 - 1:200 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 1-145 of human UBE2V2 (NP_003341.1). Synonyms UBE2V2;DDVIT1;DDVit-1;EDAF-1;EDPF-1;EDPF1;MMS2;UEV-2;UEV2 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 UBE2V2 antibody (A6998) 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: 90s. Immunohistochemistry of paraffin- embedded rat spleen using UBE2V2 antibody (A6998) at dilution of 1:100 (40x lens).
    [Show full text]
  • In Silico Analysis of Regulatory Networks Underlines the Role of Mir-10B-5P and Its Target BDNF in Huntington’S Disease Sören Müller
    Müller Translational Neurodegeneration 2014, 3:17 http://www.translationalneurodegeneration.com/content/3/1/17 Translational Neurodegeneration SHORT REPORT Open Access In silico analysis of regulatory networks underlines the role of miR-10b-5p and its target BDNF in huntington’s disease Sören Müller Abstract Non-coding RNAs (ncRNAs) play various roles during central nervous system development. MicroRNAs (miRNAs) are a class of ncRNAs that exert their function together with argonaute proteins by post-transcriptional gene silencing of messenger RNAs (mRNAs). Several studies provide evidence for alterations in miRNA expression in patients with neurodegenerative diseases. Among these is huntington‘s disease (HD), a dominantly inherited fatal disorder characterized by deregulation of neuronal-specific mRNAs as well as miRNAs. Recently, next-generation sequencing (NGS) miRNA profiles from human HD and neurologically normal control brain tissues were reported. Five consistently upregulated miRNAs affect the expression of genes involved in neuronal differentiation, neurite outgrowth, cell death and survival. We re-analyzed the NGS data publicly available in array express and detected nineteen additional differentially expressed miRNAs. Subsequently, we connected these miRNAs to genes implicated in HD development and network analysis pointed to miRNA-mediated downregulation of twenty-two genes with roles in the pathogenesis as well as treatment of the disease. In silico prediction and reporter systems prove that levels of BDNF,a central node in the miRNA-mRNA regulatory network, can be post-transcriptionally controlled by upregulated miR-10b-5p and miR-30a-5p. Reduced BDNF expression is associated with neuronal dysfunction and death in HD. Moreover, the 3’UTR of CREB1 harbors a predicted binding site for these two miRNAs.
    [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]
  • Lessons from the Naked Mole Rat
    International Journal of Molecular Sciences Review DNA Homeostasis and Senescence: Lessons from the Naked Mole Rat Harvey Boughey 1,†, Mateusz Jurga 2,† and Sherif F. El-Khamisy 1,2,* 1 The Healthy Lifespan Institute and the Institute of Neuroscience, University of Sheffield, Sheffield S10 2TN, UK; hboughey1@sheffield.ac.uk 2 The Institute of Cancer Therapeutics, University of Bradford, Bradford BD7 1DP, UK; [email protected] * Correspondence: s.el-khamisy@sheffield.ac.uk; Tel.: +44-(0)-114-2222-791; Fax: +44-(0)-114-222-2850 † These authors contributed equally. Abstract: As we age, our bodies accrue damage in the form of DNA mutations. These mutations lead to the generation of sub-optimal proteins, resulting in inadequate cellular homeostasis and senescence. The build-up of senescent cells negatively affects the local cellular micro-environment and drives ageing associated disease, including neurodegeneration. Therefore, limiting the accumulation of DNA damage is essential for healthy neuronal populations. The naked mole rats (NMR) are from eastern Africa and can live for over three decades in chronically hypoxic environments. Despite their long lifespan, NMRs show little to no biological decline, neurodegeneration, or senescence. Here, we discuss molecular pathways and adaptations that NMRs employ to maintain genome integrity and combat the physiological and pathological decline in organismal function. Keywords: naked mole rat; senescence; neurodegeneration; ageing; DNA damage; DNA repair; oxidative stress; reactive oxygen species Citation: Boughey, H.; Jurga, M.; El-Khamisy, S.F. DNA Homeostasis and Senescence: Lessons from the 1. Introduction Naked Mole Rat. Int. J. Mol. Sci. 2021, An exposure to low oxygen conditions (hypoxia) perturbs oxidative phosphorylation, 22, 6011.
    [Show full text]