RAD23A Antibody Cat

Total Page:16

File Type:pdf, Size:1020Kb

RAD23A Antibody Cat RAD23A Antibody Cat. No.: 29-716 RAD23A Antibody Antibody used in IHC on Human Lung at 4.0-8.0 ug/ml. Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Dog, Human, Mouse, Rat Antibody produced in rabbits immunized with a synthetic peptide corresponding a region IMMUNOGEN: of human RAD23A. TESTED APPLICATIONS: ELISA, IHC, WB RAD23A antibody can be used for detection of RAD23A by ELISA at 1:62500. RAD23A APPLICATIONS: antibody can be used for detection of RAD23A by western blot at 2.5 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 40 kDa WEIGHT: September 25, 2021 1 https://www.prosci-inc.com/rad23a-antibody-29-716.html Properties PURIFICATION: Antibody is purified by protein A chromatography method. CLONALITY: Polyclonal CONJUGATE: Unconjugated PHYSICAL STATE: Liquid 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: RAD23A antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles. Additional Info OFFICIAL SYMBOL: RAD23A ALTERNATE NAMES: RAD23A, HHR23A, MGC111083, HR23A ACCESSION NO.: NP_005044 PROTEIN GI NO.: 4826964 GENE ID: 5886 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References RAD23A is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair (NER). This protein was shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, as well as with ubiquitin protein ligase E6AP, and thus suggests that this protein may be involved in the ubiquitin mediated proteolytic pathway in cells.The protein encoded by BACKGROUND: this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair (NER). This protein was shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, as well as with ubiquitin protein ligase E6AP, and thus suggests that this protein may be involved in the ubiquitin mediated proteolytic pathway in cells. REFERENCES: 1) Ju, D. (2006) Biochem. Biophys. Res. Commun. 341 (2), 648-652. ANTIBODIES FOR RESEARCH USE ONLY. September 25, 2021 2 https://www.prosci-inc.com/rad23a-antibody-29-716.html For additional information, visit ProSci's Terms & Conditions Page. September 25, 2021 3 https://www.prosci-inc.com/rad23a-antibody-29-716.html.
Recommended publications
  • Case-Control Analysis Identifies Shared Properties of Rare Germline Variation in Cancer Predisposing Genes
    Case-control analysis identifies shared properties of rare germline variation in cancer predisposing genes Mykyta Artomov1,2, Vijai Joseph3, Grace Tiao1,2, Tinu Thomas3, Kasmintan Schrader3, Robert J. Klein3, Adam Kiezun2, Namrata Gupta2, Lauren MarGolin2, Alexander J. StratiGos4, Ivana Kim5, Kristen Shannon6, Leif W. Ellisen6,7, Daniel Haber6,7,8, Gad Getz2, Hensin Tsao9,10, Steven M. Lipkin11, David Altshuler2, Kenneth Offit*3,12 and Mark J. Daly*1,2 1Analytic and Translational Genetics Unit, MGH, Boston, MA, USA 2Broad Institute, CambridGe, MA, USA 3 Clinical Genetics Research Laboratory, Department of Medicine, Memorial Sloan KetterinG Cancer Center, New York, NY, USA 41st Department of DermatoloGy-VenereoloGy, National and Kapodistrian University of Athens School of Medicine, Andreas SyGros Hospital, Athens, Greece 5 Retina Service, Massachusetts Eye and Ear Infirmary, Boston, MA, USA 6 Massachusetts General Hospital Cancer Center, Boston, MA, USA 7 Harvard Medical School, Boston, MA, USA 8 Howard HuGhes Medical Institute, Chevy Chase, Maryland 20815, USA 9 Department of DermatoloGy, Wellman Center for Photomedicine, MGH, Boston, MA, USA 10 Melanoma Genetics ProGram, MGH Cancer Center, MGH, Boston, MA, USA 11 Department of Medicine, ProGram in Mendelian Genetics, Weill-Cornell Medicine, New York, NY, USA 12 Cancer BioloGy and Genetics ProGram, Sloan KetterinG Institute, New York, NY, USA Correspondence: Mark J. Daly, 185 CambridGe St, CPZN-6823A, Boston, MA, 02114, USA; [email protected]; phone: (617)-726-5936 Kenneth Offit, Memorial Sloan KetterinG Cancer Center, 1275 York Avenue, New York, NY, 10065; [email protected]; phone: (212)-639-2000 Authors declare no conflict of interests SUPPLEMENTARY INFORMATION Patient cohorts .........................................................................................................................................
    [Show full text]
  • RAD23A Antibody (N-Term) Blocking Peptide Synthetic Peptide Catalog # Bp2173a
    10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 RAD23A Antibody (N-term) Blocking Peptide Synthetic peptide Catalog # BP2173a Specification RAD23A Antibody (N-term) Blocking RAD23A Antibody (N-term) Blocking Peptide - Peptide - Background Product Information RAD223A is one of two human homologs of Primary Accession P54725 Saccharomyces cerevisiae Rad23, a protein Other Accession NP_005044 involved in nucleotide excision repair (NER). This protein was shown to interact with, and elevate the nucleotide excision activity of RAD23A Antibody (N-term) Blocking Peptide - Additional Information 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein Gene ID 5886 contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S Other Names proteasome, as well as with ubiquitin protein UV excision repair protein RAD23 homolog ligase E6AP, and thus suggests that this A, HR23A, hHR23A, RAD23A protein may be involved in the ubiquitin Target/Specificity mediated proteolytic pathway in cells. The synthetic peptide sequence used to generate the antibody <a href=/product/pr RAD23A Antibody (N-term) Blocking oducts/AP2173a>AP2173a</a> was Peptide - References selected from the N-term region of human RAD23A . A 10 to 100 fold molar excess to Mueller, T.D., et al., EMBO J. 22(18):4634-4645 antibody is recommended. Precise (2003).Mueller, T.D., et al., J. Mol. Biol. conditions should be optimized for a 319(5):1243-1255 (2002).Elder, R.T., et al., particular assay. Nucleic Acids Res. 30(2):581-591 (2002).Chen, L., et al., EMBO Rep.
    [Show full text]
  • An Overview of DNA Repair Mechanisms in Plants Compared to Mammals
    Cell. Mol. Life Sci. (2017) 74:1693–1709 DOI 10.1007/s00018-016-2436-2 Cellular and Molecular Life Sciences REVIEW Protecting DNA from errors and damage: an overview of DNA repair mechanisms in plants compared to mammals Claudia P. Spampinato1 Received: 8 August 2016 / Revised: 1 December 2016 / Accepted: 5 December 2016 / Published online: 20 December 2016 Ó Springer International Publishing 2016 Abstract The genome integrity of all organisms is con- methods and reporter systems for gene expression and stantly threatened by replication errors and DNA damage function studies. Here, I provide a current understanding of arising from endogenous and exogenous sources. Such base DNA repair genes in plants, with a special focus on A. pair anomalies must be accurately repaired to prevent thaliana. It is expected that this review will be a valuable mutagenesis and/or lethality. Thus, it is not surprising that resource for future functional studies in the DNA repair cells have evolved multiple and partially overlapping DNA field, both in plants and animals. repair pathways to correct specific types of DNA errors and lesions. Great progress in unraveling these repair mecha- Keywords DNA repair Á Photolyases Á BER Á NER Á nisms at the molecular level has been made by several MMR Á HR Á NHEJ talented researchers, among them Tomas Lindahl, Aziz Sancar, and Paul Modrich, all three Nobel laureates in Chemistry for 2015. Much of this knowledge comes from Introduction studies performed in bacteria, yeast, and mammals and has impacted research in plant systems. Two plant features All organisms are constantly exposed to environmental should be mentioned.
    [Show full text]
  • RAD23A Polyclonal Antibody
    For Research Use Only RAD23A Polyclonal antibody Catalog Number:11364-1-AP 2 Publications www.ptgcn.com Catalog Number: GenBank Accession Number: Recommended Dilutions: Basic Information 11364-1-AP BC014026 WB 1:500-1:1000 Size: GeneID (NCBI): 227 μg/ml 5886 Source: Full Name: Rabbit RAD23 homolog A (S. cerevisiae) Isotype: Calculated MW: IgG 40 kDa Purification Method: Observed MW: Antigen affinity purification 55 kDa Immunogen Catalog Number: AG1907 Applications Tested Applications: Positive Controls: WB, ELISA WB : mouse testis tissue; Cited Applications: WB Species Specificity: human, mouse, rat Cited Species: human RAD23A, also named as HHR23A, belongs to the RAD23 family. It is a multiubiquitin chain receptor involved in Background Information modulation of proteasomal degradation. RAD23A binds to 'Lys-48'-linked polyubiquitin chains in a length- dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. It is proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. It is involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC. It is also involved in vpr-dependent replication of HIV-1 in non- proliferating cells and primary macrophages and is required for the association of HIV-1 vpr with the host proteasome. This antibody is a rabbit polyclonal antibody raised against full length RAD23A of human origin. Notable Publications Author Pubmed ID Journal Application Lihua Song 26095601 Cancer Lett WB Xiaofei Zhang 28190767 Mol Cell WB Storage: Storage Store at -20ºC.
    [Show full text]
  • 24555 Rad23a (D7U7Z) Rabbit Mab
    Revision 1 C 0 2 - t Rad23A (D7U7Z) Rabbit mAb a e r o t S Orders: 877-616-CELL (2355) [email protected] 5 Support: 877-678-TECH (8324) 5 5 Web: [email protected] 4 www.cellsignal.com 2 # 3 Trask Lane Danvers Massachusetts 01923 USA For Research Use Only. Not For Use In Diagnostic Procedures. Applications: Reactivity: Sensitivity: MW (kDa): Source/Isotype: UniProt ID: Entrez-Gene Id: WB, IP H M R Mk Endogenous 52 Rabbit IgG P54725 5886 Product Usage Information 2. Masutani, C. et al. (1994) EMBO J 13, 1831-43. 3. Walters, K.J. et al. (2003) Proc Natl Acad Sci U S A 100, 12694-9. Application Dilution 4. Elsasser, S. et al. (2002) Nat Cell Biol 4, 725-30. 5. Raasi, S. et al. (2005) Nat Struct Mol Biol 12, 708-14. Western Blotting 1:1000 6. Nathan, J.A. et al. (2013) EMBO J 32, 552-65. Immunoprecipitation 1:50 7. Elsasser, S. et al. (2004) J Biol Chem 279, 26817-22. 8. Ng, J.M. et al. (2003) Genes Dev 17, 1630-45. Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody. Specificity / Sensitivity Rad23A (D7U7Z) Rabbit mAb recognizes endogenous levels of total Rad23A protein. This antibody does not cross-react with Rad23B. Species Reactivity: Human, Mouse, Rat, Monkey Source / Purification Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gln214 of human Rad23A protein.
    [Show full text]
  • Human DNA Repair Genes Relatively Late-Diverging, Major Eukaryotic Taxa Whose Exact Order of Radiation Is Difficult to Deter- Richard D
    A NALYSIS OF G ENOMIC I NFORMATION likely GTPases, as indicated by the activity of CIITA 27. L. Aravind, H. Watanabe, D. J. Lipman, E. V. Koonin, of the Integrated Protein Index and A. Uren for critical and HET-E [E. V. Koonin, L. Aravind, Trends Biochem. Proc. Natl. Acad. Sci. U.S.A. 97, 11319 (2000). reading of the manuscript and useful comments. The Sci. 25, 223 (2000)]. 28. J. R. Brown, W. F. Doolittle, Microbiol. Mol. Biol. Rev. release of the unpublished WormPep data set by The 14. T. L. Beattie, W. Zhou, M. O. Robinson, L. Harrington, 61, 456 (1997). Sanger Center is acknowledged and greatly appreciated. Curr. Biol. 8, 177 (1998). 29. We thank E. Birney and A. Bateman (The Sanger Center, 15. E. Diez, Z. Yaraghi, A. MacKenzie, P. Gros, J. Immunol. Hinxton, UK) for kindly providing the preliminary version 25 October 2000; accepted 18 January 2001 164, 1470 (2000). 16. A. M. Verhagen et al., Cell 102, 43 (2000). 17. L. Goyal, K. McCall, J. Agapite, E. Hartwieg, H. Steller, EMBO J. 19, 589 (2000). 18. The eukaryotic crown group is the assemblage of Human DNA Repair Genes relatively late-diverging, major eukaryotic taxa whose exact order of radiation is difficult to deter- Richard D. Wood,1* Michael Mitchell,2 John Sgouros,2 mine with confidence. The crown group includes the 1 multicellular eukaryotes (animals, fungi, and plants) Tomas Lindahl and some unicellular eukaryotic lineages such as slime molds and Acanthamoebae [A. H. Knoll, Science 256, 622 (1992); S. Kumar, A. Rzhetsky, J. Mol.
    [Show full text]
  • Rad23a Rabbit Mab
    Leader in Biomolecular Solutions for Life Science Rad23A Rabbit mAb Catalog No.: A5147 Recombinant Basic Information Background Catalog No. The protein encoded by this gene is one of two human homologs of Saccharomyces A5147 cerevisiae Rad23, a protein involved in nucleotide excision repair. Proteins in this family have a modular domain structure consisting of an ubiquitin-like domain (UbL), Observed MW ubiquitin-associated domain 1 (UbA1), XPC-binding domain and UbA2. The protein 50KDa encoded by this gene plays an important role in nucleotide excision repair and also in delivery of polyubiquitinated proteins to the proteasome. Alternative splicing results in Calculated MW multiple transcript variants encoding multiple isoforms. [provided by RefSeq, Jun 2012] 55kDa Category Primary antibody Applications WB,IF Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 5886 P54725 IF 1:50 - 1:200 Immunogen A synthesized peptide derived from human Rad23A Synonyms HHR23A; HR23A 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,0.05% BSA,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using Rad23A Rabbit mAb (A5147) 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: 1min. Western blot analysis of extracts of various cell lines, using Rad23A Rabbit mAb (A5147) at 1:1000 dilution.
    [Show full text]
  • Autism and Cancer Share Risk Genes, Pathways, and Drug Targets
    TIGS 1255 No. of Pages 8 Forum Table 1 summarizes the characteristics of unclear whether this is related to its signal- Autism and Cancer risk genes for ASD that are also risk genes ing function or a consequence of a second for cancers, extending the original finding independent PTEN activity, but this dual Share Risk Genes, that the PI3K-Akt-mTOR signaling axis function may provide the rationale for the (involving PTEN, FMR1, NF1, TSC1, and dominant role of PTEN in cancer and Pathways, and Drug TSC2) was associated with inherited risk autism. Other genes encoding common Targets for both cancer and ASD [6–9]. Recent tumor signaling pathways include MET8[1_TD$IF],[2_TD$IF] genome-wide exome-sequencing studies PTK7, and HRAS, while p53, AKT, mTOR, Jacqueline N. Crawley,1,2,* of de novo variants in ASD and cancer WNT, NOTCH, and MAPK are compo- Wolf-Dietrich Heyer,3,4 and have begun to uncover considerable addi- nents of signaling pathways regulating Janine M. LaSalle1,4,5 tional overlap. What is surprising about the the nuclear factors described above. genes in Table 1 is not necessarily the Autism is a neurodevelopmental number of risk genes found in both autism Autism is comorbid with several mono- and cancer, but the shared functions of genic neurodevelopmental disorders, disorder, diagnosed behaviorally genes in chromatin remodeling and including Fragile X (FMR1), Rett syndrome by social and communication genome maintenance, transcription fac- (MECP2), Phelan-McDermid (SHANK3), fi de cits, repetitive behaviors, tors, and signal transduction pathways 15q duplication syndrome (UBE3A), and restricted interests. Recent leading to nuclear changes [7,8].
    [Show full text]
  • Proteins Containing Ubiquitin-Like (Ubl) Domains Not Only Bind to 26S Proteasomes but Also Induce Their Activation
    Proteins containing ubiquitin-like (Ubl) domains not only bind to 26S proteasomes but also induce their activation Galen A. Collinsa,b and Alfred L. Goldberga,b,1 aBlavatnick Institute, Harvard Medical School, Boston, MA 02115; and bDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115 Contributed by Alfred L. Goldberg, January 7, 2020 (sent for review September 9, 2019; reviewed by Ramanujan S. Hegde and Kylie J. Walters) During protein degradation by the ubiquitin–proteasome pathway, in over 60 human proteins, is defined by its structural similarity latent 26S proteasomes in the cytosol must assume an active form. to ubiquitin. Like ubiquitin and its homologs (e.g., SUMO and Proteasomes are activated when ubiquitylated substrates bind to Nedd8), the Ubl domain contains five β-sheets surrounding an them and interact with the proteasome-bound deubiquitylase α-helix in what is called a β-grasp fold (16). Unlike ubiquitin-family Usp14/Ubp6. The resulting increase in the proteasome’s degradative members, Ubl-containing proteins cannot be conjugated to other activity was recently shown to be mediated by Usp14’s ubiquitin-like proteins. Instead, the Ubl domain promotes noncovalent binding to (Ubl) domain, which, by itself, can trigger proteasome activation. other proteins, especially the 26S proteasome (17). In yeast, the Many other proteins with diverse cellular functions also contain fusion of any yeast Ubl domain to a loosely folded protein will Ubl domains and can associate with 26S proteasomes. We therefore target it to proteasomes for degradation without ubiquitylation (18). tested if various Ubl-containing proteins that have important roles Recent tomographic electron microscopy of cultured neurons in protein homeostasis or disease also activate 26S proteasomes.
    [Show full text]
  • TARGETED PROTEIN DEGRADATION Targeted Protein Degradation
    TARGETED PROTEIN DEGRADATION Targeted Protein Degradation The Bio-Techne family of brands offer a unique portfolio of high-quality reagents, instruments and services for researchers working in the rapidly growing field of Targeted Protein Degradation. Bio-Techne provides a bespoke range of tools and reagents, including Active Degraders, TAG Degradation Platform (aTAG, dTAG), Degrader Building Blocks, Assays for Protein Degradation, Ubiquitin Proteasome System Proteins and Assays, and Custom Degrader Services. Visit tocris.com/tpd Table of Contents Introduction to Targeted Protein Degradation ............................................................................................................................................................3 Active Degraders ...........................................................................................................................................................................................................4 Degrader Negative Controls .........................................................................................................................................................................................4 Degrader Building Blocks ............................................................................................................................................................................................5 TAG Degradation Platform .........................................................................................................................................................................................6-7
    [Show full text]
  • Differential Mechanisms of Tolerance to Extreme Environmental
    www.nature.com/scientificreports OPEN Diferential mechanisms of tolerance to extreme environmental conditions in tardigrades Dido Carrero*, José G. Pérez-Silva , Víctor Quesada & Carlos López-Otín * Tardigrades, also known as water bears, are small aquatic animals that inhabit marine, fresh water or limno-terrestrial environments. While all tardigrades require surrounding water to grow and reproduce, species living in limno-terrestrial environments (e.g. Ramazzottius varieornatus) are able to undergo almost complete dehydration by entering an arrested state known as anhydrobiosis, which allows them to tolerate ionic radiation, extreme temperatures and intense pressure. Previous studies based on comparison of the genomes of R. varieornatus and Hypsibius dujardini - a less tolerant tardigrade - have pointed to potential mechanisms that may partially contribute to their remarkable ability to resist extreme physical conditions. In this work, we have further annotated the genomes of both tardigrades using a guided approach in search for novel mechanisms underlying the extremotolerance of R. varieornatus. We have found specifc amplifcations of several genes, including MRE11 and XPC, and numerous missense variants exclusive of R. varieornatus in CHEK1, POLK, UNG and TERT, all of them involved in important pathways for DNA repair and telomere maintenance. Taken collectively, these results point to genomic features that may contribute to the enhanced ability to resist extreme environmental conditions shown by R. varieornatus. Tardigrades are small
    [Show full text]
  • Vpr and Its Cellular Interaction Partners: R We There Yet?
    cells Review Vpr and Its Cellular Interaction Partners: R We There Yet? Helena Fabryova and Klaus Strebel * Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bldg. 4, Room 312, 4 Center Drive, MSC 0460, Bethesda, MD 20892, USA; [email protected] * Correspondence: [email protected]; Tel.: +1-(301)-496-3132; Fax: +1-(301)-480-2716 Received: 2 October 2019; Accepted: 23 October 2019; Published: 24 October 2019 Abstract: Vpr is a lentiviral accessory protein that is expressed late during the infection cycle and is packaged in significant quantities into virus particles through a specific interaction with the P6 domain of the viral Gag precursor. Characterization of the physiologically relevant function(s) of Vpr has been hampered by the fact that in many cell lines, deletion of Vpr does not significantly affect viral fitness. However, Vpr is critical for virus replication in primary macrophages and for viral pathogenesis in vivo. It is generally accepted that Vpr does not have a specific enzymatic activity but functions as a molecular adapter to modulate viral or cellular processes for the benefit of the virus. Indeed, many Vpr interacting factors have been described by now, and the goal of this review is to summarize our current knowledge of cellular proteins targeted by Vpr. Keywords: HIV-1; Vpr; accessory genes; host restriction factors 1. Introduction Primate lentiviruses are a group of retroviruses that cause slowly progressing, often incurable diseases. A characteristic feature of these viruses is the presence of accessory genes that vary in number from virus to virus (Figure1).
    [Show full text]