MAD2L2 Monoclonal ANTIBODY

Total Page:16

File Type:pdf, Size:1020Kb

MAD2L2 Monoclonal ANTIBODY For Research Use Only MAD2L2 Monoclonal ANTIBODY www.ptgcn.com Catalog Number:67100-1-Ig Basic Information Catalog Number: GenBank Accession Number: CloneNo.: 67100-1-Ig BC015244 2A4C2 Size: GeneID (NCBI): Recommended Dilutions: 1000 μg/ml 10459 WB 1:5000-1:20000 Source: Full Name: IHC 1:500-1:2000 Mouse MAD2 mitotic arrest deficient-like 2 (yeast) Isotype: Calculated MW: IgG2b 211aa,24 kDa Purification Method: Observed MW: Protein A purification 24 kDa Immunogen Catalog Number: AG28233 Applications Tested Applications: Positive Controls: IHC, WB, ELISA WB : HeLa cells; Species Specificity: IHC : human lymphoma tissue; Human, mouse, rat Note-IHC: suggested angen retrieval with TE buffer pH 9.0; (*) Alternavely, angen retrieval may be performed with citrate buffer pH 6.0 MAD family, together with BUB and Mps1,Cdc20k, play roles in the mitotic spindle checkpoint. MAD2L2 is one of the MAD family. It can mediate the second Background Information polymerase switching in translation DNA synthesis by mediating the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1. Through regulation of the JNK-mediate phosphorylation and activation of the transcriptional activator ELK1, MAD2L2 involves in cellular response to DNA damage. Also it has role in the progression of cell cycle and peithelial-mesenchymal transdifferentiation. Storage: Storage Store at -20ºC. Stable for one year after shipment. Storage Buffer: PBS with 0.1% sodium azide and 50% glycerol pH 7.3. Aliquoting is unnecessary for -20ºC storage For technical support and original validation data for this product please contact: This product is exclusively available under T: 4006900926 E: [email protected] W: ptgcn.com Proteintech Group brand and is not available to purchase from any other manufacturer. Selected Validation Data Various lysates were subjected to SDS PAGE Immunohistochemical analysis of paraffin- followed by western blot with 67100-1-Ig (MAD2L2 embedded human lymphoma tissue slide using antibody) at dilution of 1:20000 incubated at room 67100-1-Ig (MAD2L2 antibody) at dilution of temperature for 1.5 hours 1:1000 (under 40x lens). heat mediated antigen retrieved with Tris-EDTA buffer(pH9)..
Recommended publications
  • Ubiquitinated Proliferating Cell Nuclear Antigen Activates Translesion DNA Polymerases ␩ and REV1
    Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases ␩ and REV1 Parie Garg and Peter M. Burgers* Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid, St. Louis, MO 63110 Edited by Jerard Hurwitz, Memorial Sloan–Kettering Cancer Center, New York, NY, and approved November 4, 2005 (received for review July 14, 2005) In response to DNA damage, the Rad6͞Rad18 ubiquitin-conjugat- and requiring additional activation by the Cdc7͞Dbf4 protein ing complex monoubiquitinates the replication clamp proliferating kinase that normally functions in cell cycle progression (5, 12). cell nuclear antigen (PCNA) at Lys-164. Although ubiquitination of It is this complex pathway that mainly contributes to DNA PCNA is recognized as an essential step in initiating postreplication damage induced mutagenesis in eukaryotic cells. Although repair, the mechanistic relevance of this modification has remained normally involved in lagging strand DNA replication, the high- elusive. Here, we describe a robust in vitro system that ubiquiti- fidelity Pol ␦ is also required for damage-induced mutagenesis. nates yeast PCNA specifically on Lys-164. Significantly, only those The functions of Pol ␨ and Rev1 appear to be uniquely confined PCNA clamps that are appropriately loaded around effector DNA to mutagenesis. Pol ␨ is an error-prone DNA polymerase that can by its loader, replication factor C, are ubiquitinated. This observa- bypass damage (13). Rev1 is a deoxycytidyl transferase that tion suggests that, in vitro, only PCNA present at stalled replication shows the highest catalytic activity opposite template guanines forks is ubiquitinated. Ubiquitinated PCNA displays the same and abasic sites (14, 15). Rev1 is primarily responsible for replicative functions as unmodified PCNA.
    [Show full text]
  • Jimmunol.0901240.Full.Pdf
    A Critical Role for REV1 in Regulating the Induction of C:G Transitions and A:T Mutations during Ig Gene Hypermutation This information is current as Keiji Masuda, Rika Ouchida, Yingqian Li, Xiang Gao, of September 24, 2021. Hiromi Mori and Ji-Yang Wang J Immunol published online 8 July 2009 http://www.jimmunol.org/content/early/2009/07/08/jimmuno l.0901240 Downloaded from Supplementary http://www.jimmunol.org/content/suppl/2009/07/07/jimmunol.090124 Material 0.DC1 http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on September 24, 2021 *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2009 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. Published July 8, 2009, doi:10.4049/jimmunol.0901240 The Journal of Immunology A Critical Role for REV1 in Regulating the Induction of C:G Transitions and A:T Mutations during Ig Gene Hypermutation Keiji Masuda,* Rika Ouchida,* Yingqian Li,†* Xiang Gao,† Hiromi Mori,* and Ji-Yang Wang1* REV1 is a deoxycytidyl transferase that catalyzes the incorporation of deoxycytidines opposite deoxyguanines and abasic sites.
    [Show full text]
  • Identification of Conserved Genes Triggering Puberty in European Sea
    Blázquez et al. BMC Genomics (2017) 18:441 DOI 10.1186/s12864-017-3823-2 RESEARCHARTICLE Open Access Identification of conserved genes triggering puberty in European sea bass males (Dicentrarchus labrax) by microarray expression profiling Mercedes Blázquez1,2* , Paula Medina1,2,3, Berta Crespo1,4, Ana Gómez1 and Silvia Zanuy1* Abstract Background: Spermatogenesisisacomplexprocesscharacterized by the activation and/or repression of a number of genes in a spatio-temporal manner. Pubertal development in males starts with the onset of the first spermatogenesis and implies the division of primary spermatogonia and their subsequent entry into meiosis. This study is aimed at the characterization of genes involved in the onset of puberty in European sea bass, and constitutes the first transcriptomic approach focused on meiosis in this species. Results: European sea bass testes collected at the onset of puberty (first successful reproduction) were grouped in stage I (resting stage), and stage II (proliferative stage). Transition from stage I to stage II was marked by an increase of 11ketotestosterone (11KT), the main fish androgen, whereas the transcriptomic study resulted in 315 genes differentially expressed between the two stages. The onset of puberty induced 1) an up-regulation of genes involved in cell proliferation, cell cycle and meiosis progression, 2) changes in genes related with reproduction and growth, and 3) a down-regulation of genes included in the retinoic acid (RA) signalling pathway. The analysis of GO-terms and biological pathways showed that cell cycle, cell division, cellular metabolic processes, and reproduction were affected, consistent with the early events that occur during the onset of puberty.
    [Show full text]
  • Human Pol Ζ Purified with Accessory Subunits Is Active in Translesion DNA Synthesis and Complements Pol Η in Cisplatin Bypass
    Human Pol ζ purified with accessory subunits is active in translesion DNA synthesis and complements Pol η in cisplatin bypass Young-Sam Lee1, Mark T. Gregory, and Wei Yang2 Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 Contributed by Wei Yang, December 27, 2013 (sent for review December 5, 2013) DNA polymerase ζ (Pol ζ) is a eukaryotic B-family DNA polymerase a nucleotide opposite either a cis–syn thymine or a 6-4 photo- that specializes in translesion synthesis and is essential for normal product (23). Genetic data indicate that a complete lesion bypass embryogenesis. At a minimum, Pol ζ consists of a catalytic subunit event may require two TLS DNA polymerases (24)—one for Rev3 and an accessory subunit Rev7. Mammalian Rev3 contains nucleotide incorporation opposite a lesion (insertion step) and >3,000 residues and is twice as large as the yeast homolog. To the other for the subsequent primer extension (extension step). date, no vertebrate Pol ζ has been purified for biochemical char- The insertion step of TLS is often accomplished by a Y-family acterization. Here we report purification of a series of human Rev3 polymerase, whose active site is uncommonly large, solvent- deletion constructs expressed in HEK293 cells and identification of exposed, and flexible (25). Studies of another B-family TLS DNA a minimally catalytically active human Pol ζ variant. With a tagged polymerase from Escherichia coli (Pol II) show that it efficiently form of an active Pol ζ variant, we isolated two additional acces- extends a DNA primer after a lesion by looping out the damaged sory subunits of human Pol ζ, PolD2 and PolD3.
    [Show full text]
  • Gene Section Review
    Atlas of Genetics and Cytogenetics in Oncology and Haematology OPEN ACCESS JOURNAL AT INIST-CNRS Gene Section Review MAD2L1 (mitotic arrest deficient 2, yeast, human homolog like-1) Elizabeth M. Petty, Kenute Myrie Division of Medical Genetics Departments of Human Genetics and Internal Medicine University of Michigan Medical School 1150 West Medical Center Drive, 4301 MSRB III, Ann Arbor, Michigan 48109- 0638, USA (EMP, KM) Published in Atlas Database: March 2001 Online updated version : http://AtlasGeneticsOncology.org/Genes/MAD2L1ID304.html DOI: 10.4267/2042/37729 This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 France Licence. © 2001 Atlas of Genetics and Cytogenetics in Oncology and Haematology Identity Other names: HsMAD2; MAD2; MAD2A HGNC (Hugo): MAD2L1 Shadded boxes (1-5) depict the 5 exons of MAD2L1. The black Location : 4q27 triangle indicates a del A mutation that was found in the CAL51 Local order: As noted on the GM99-GB4 breast cancer cell line. Open triangkes depict the locations of Chromosome 4 map: Position: 548.24 (cR3000) Lod identified sequence variants. Figure is not drawn to scale. score: 1.16 Reference Interval: D4S2945-D4S430 Transcription (115.1-125.1 cM) It is located within the NCBI BAC MAD2L1 has 5 coding exons. No alternative splicing genomic contig: NT_006302.2 which is part of the has been described. Regulation of its transcription in homo sapiens chromosome 4 sequence segment. human cells is currently poorly understood. Note: MAD2L1 was intially (and errounously) mapped by fluorescence in situ hybridization (FISH) to 5q23- Protein q31. Subsequent comprehensive mapping studies using somatic cell hybrid analysis, radiation hybrid (RH) Description mapping, and FISH localized it to 4q27.
    [Show full text]
  • Anti-MAD2L2 Monoclonal Antibody, Clone FQS24768 (DCABH-6886) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
    Anti-MAD2L2 monoclonal antibody, clone FQS24768 (DCABH-6886) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Rabbit Monoclonal to Mad2L2 Antigen Description Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation. Immunogen Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) within Human Mad2L2 aa 150 to the C-terminus. The exact sequence is proprietary.Database link: Q9UI95 Isotype IgG Source/Host Rabbit Species Reactivity Mouse, Rat, Human Clone FQS24768 Purity Protein A purified Conjugate Unconjugated Applications IP, ICC/IF, Flow Cyt, IHC-P, WB Positive Control K562, SW480, Hela, Molt-4 cell lysates, human ovarian carcinoma tissue, Hela cells, Format Liquid Size 100 μl Buffer Preservative: 0.01% Sodium azide; Constituents: 59% PBS, 0.05% BSA, 40% Glycerol 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Preservative 0.01% Sodium Azide Storage Store at +4°C short term (1-2 weeks).
    [Show full text]
  • DNA Polymerase Ι Compensates for Fanconi Anemia Pathway Deficiency by Countering DNA Replication Stress
    DNA polymerase ι compensates for Fanconi anemia pathway deficiency by countering DNA replication stress Rui Wanga, Walter F. Lenoirb,c, Chao Wanga, Dan Sua, Megan McLaughlinb, Qianghua Hua, Xi Shena, Yanyan Tiana, Naeh Klages-Mundta,c, Erica Lynna, Richard D. Woodc,d, Junjie Chena,c, Traver Hartb,c, and Lei Lia,c,e,1 aDepartment of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030; bDepartment of Bioinformatics and Computational Biology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030; cThe University of Texas MD Anderson Cancer Center University of Texas Health Science Center at Houston Graduate School of Biomedical Sciences, Houston, TX 77030; dDepartment of Epigenetics and Molecular Carcinogenesis, The University of Texas MD Anderson Cancer Center, Houston, TX 77030; and eLife Sciences Institute, Zhejiang University, Hangzhou, China 310058 Edited by Wei Yang, NIH, Bethesda, MD, and approved November 12, 2020 (received for review May 8, 2020) Fanconi anemia (FA) is caused by defects in cellular responses to proteins, required in homologous recombination (FANCD1/ DNA crosslinking damage and replication stress. Given the con- BRCA2, FANCO/RAD51C, FANCJ/BARD1, and FANCR/ stant occurrence of endogenous DNA damage and replication fork RAD51) (22–26). stress, it is unclear why complete deletion of FA genes does not In addition to the direct role in crosslinking damage repair, have a major impact on cell proliferation and germ-line FA patients FA pathway components are linked to the protection of repli- are able to progress through development well into their adult- cation fork integrity during replication interruption that is not hood.
    [Show full text]
  • Y-Family DNA Polymerases in Escherichia Coli
    Y-family DNA polymerases in Escherichia coli The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Jarosz, Daniel F. et al. “Y-family DNA Polymerases in Escherichia Coli.” Trends in Microbiology 15.2 (2007): 70–77. Web. 13 Apr. 2012. © 2007 Elsevier Ltd. As Published http://dx.doi.org/10.1016/j.tim.2006.12.004 Publisher Elsevier Version Final published version Citable link http://hdl.handle.net/1721.1/70041 Terms of Use Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. Review TRENDS in Microbiology Vol.15 No.2 Y-family DNA polymerases in Escherichia coli Daniel F. Jarosz1, Penny J. Beuning2,3, Susan E. Cohen2 and Graham C. Walker2 1 Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA 2 Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA 3 Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA 02115, USA The observation that mutations in the Escherichia coli that is also lexA-independent [4]. This might have genes umuC+ and umuD+ abolish mutagenesis induced particularly important implications for bacteria living by UV light strongly supported the counterintuitive under conditions of nutrient starvation. The SOS response notion that such mutagenesis is an active rather than also seems to be oscillatory at the single-cell level, and this passive process. Genetic and biochemical studies have oscillation is dependent on the umuDC genes [5].
    [Show full text]
  • Ubiquitin and Ubiquitin-Like Proteins Are Essential Regulators of DNA Damage Bypass
    cancers Review Ubiquitin and Ubiquitin-Like Proteins Are Essential Regulators of DNA Damage Bypass Nicole A. Wilkinson y, Katherine S. Mnuskin y, Nicholas W. Ashton * and Roger Woodgate * Laboratory of Genomic Integrity, National Institute of Child Health and Human Development, National Institutes of Health, 9800 Medical Center Drive, Rockville, MD 20850, USA; [email protected] (N.A.W.); [email protected] (K.S.M.) * Correspondence: [email protected] (N.W.A.); [email protected] (R.W.); Tel.: +1-301-435-1115 (N.W.A.); +1-301-435-0740 (R.W.) Co-first authors. y Received: 29 August 2020; Accepted: 29 September 2020; Published: 2 October 2020 Simple Summary: Ubiquitin and ubiquitin-like proteins are conjugated to many other proteins within the cell, to regulate their stability, localization, and activity. These modifications are essential for normal cellular function and the disruption of these processes contributes to numerous cancer types. In this review, we discuss how ubiquitin and ubiquitin-like proteins regulate the specialized replication pathways of DNA damage bypass, as well as how the disruption of these processes can contribute to cancer development. We also discuss how cancer cell survival relies on DNA damage bypass, and how targeting the regulation of these pathways by ubiquitin and ubiquitin-like proteins might be an effective strategy in anti-cancer therapies. Abstract: Many endogenous and exogenous factors can induce genomic instability in human cells, in the form of DNA damage and mutations, that predispose them to cancer development. Normal cells rely on DNA damage bypass pathways such as translesion synthesis (TLS) and template switching (TS) to replicate past lesions that might otherwise result in prolonged replication stress and lethal double-strand breaks (DSBs).
    [Show full text]
  • Managing DNA Polymerases: Coordinating DNA Replication, DNA Repair, and DNA Recombination
    Colloquium Managing DNA polymerases: Coordinating DNA replication, DNA repair, and DNA recombination Mark D. Sutton and Graham C. Walker* Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139 Two important and timely questions with respect to DNA replica- A Superfamily of DNA Polymerases Involved in Replication of Imper- tion, DNA recombination, and DNA repair are: (i) what controls fect DNA Templates. Recently, the field of translesion DNA which DNA polymerase gains access to a particular primer-termi- synthesis and induced mutagenesis has generated a great deal of nus, and (ii) what determines whether a DNA polymerase hands off excitement because of the discovery that key gene products its DNA substrate to either a different DNA polymerase or to a required for these processes, in both prokaryotes (9, 10) and in different protein(s) for the completion of the specific biological eukaryotes (11, 12), possess an intrinsic DNA polymerase ac- process? These questions have taken on added importance in light tivity (refs. 6, 7, and 13–20 and reviewed in refs. 21–24). A of the fact that the number of known template-dependent DNA common, defining feature of these DNA polymerases is a polymerases in both eukaryotes and in prokaryotes has grown remarkable ability to replicate imperfect DNA templates. De- tremendously in the past two years. Most notably, the current list pending on the DNA polymerase, these include templates such now includes a completely new family of enzymes that are capable as those containing a misaligned primer–template junction (13), of replicating imperfect DNA templates. This UmuC-DinB-Rad30- an abasic site (6, 7), a cyclobutane dimer (15, 16, 25), or a pyrimidine–pyrimidone (6–4) photoproduct (25).
    [Show full text]
  • Shieldin Complex Promotes DNA End-Joining and Counters Homologous Recombination in BRCA1-Null Cells
    This is a repository copy of Shieldin complex promotes DNA end-joining and counters homologous recombination in BRCA1-null cells. White Rose Research Online URL for this paper: http://eprints.whiterose.ac.uk/136933/ Version: Accepted Version Article: Dev, H, Chiang, T-WW, Lescale, C et al. (27 more authors) (2018) Shieldin complex promotes DNA end-joining and counters homologous recombination in BRCA1-null cells. Nature Cell Biology, 20. pp. 954-965. ISSN 1465-7392 https://doi.org/10.1038/s41556-018-0140-1 © 2018 Springer Nature Limited. This is an author produced version of a paper published in Nature Cell Biology. Uploaded in accordance with the publisher's self-archiving policy. Reuse Items deposited in White Rose Research Online are protected by copyright, with all rights reserved unless indicated otherwise. They may be downloaded and/or printed for private study, or other acts as permitted by national copyright laws. The publisher or other rights holders may allow further reproduction and re-use of the full text version. This is indicated by the licence information on the White Rose Research Online record for the item. Takedown If you consider content in White Rose Research Online to be in breach of UK law, please notify us by emailing [email protected] including the URL of the record and the reason for the withdrawal request. [email protected] https://eprints.whiterose.ac.uk/ 1 Shieldin complex promotes DNA end-joining and counters 2 homologous recombination in BRCA1-null cells 3 4 Harveer Dev1,2, Ting-Wei Will Chiang1Y, Chloe Lescale3Y, Inge de Krijger4Y, Alistair G.
    [Show full text]
  • A Causal Gene Network with Genetic Variations Incorporating Biological Knowledge and Latent Variables
    A CAUSAL GENE NETWORK WITH GENETIC VARIATIONS INCORPORATING BIOLOGICAL KNOWLEDGE AND LATENT VARIABLES By Jee Young Moon A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy (Statistics) at the UNIVERSITY OF WISCONSIN–MADISON 2013 Date of final oral examination: 12/21/2012 The dissertation is approved by the following members of the Final Oral Committee: Brian S. Yandell. Professor, Statistics, Horticulture Alan D. Attie. Professor, Biochemistry Karl W. Broman. Professor, Biostatistics and Medical Informatics Christina Kendziorski. Associate Professor, Biostatistics and Medical Informatics Sushmita Roy. Assistant Professor, Biostatistics and Medical Informatics, Computer Science, Systems Biology in Wisconsin Institute of Discovery (WID) i To my parents and brother, ii ACKNOWLEDGMENTS I greatly appreciate my adviser, Prof. Brian S. Yandell, who has always encouraged, inspired and supported me. I am grateful to him for introducing me to the exciting research areas of statis- tical genetics and causal gene network analysis. He also allowed me to explore various statistical and biological problems on my own and guided me to see the problems in a bigger picture. Most importantly, he waited patiently as I progressed at my own pace. I would also like to thank Dr. Elias Chaibub Neto and Prof. Xinwei Deng who my adviser arranged for me to work together. These three improved my rigorous writing and thinking a lot when we prepared the second chapter of this dissertation for publication. It was such a nice opportunity for me to join the group of Prof. Alan D. Attie, Dr. Mark P. Keller, Prof. Karl W. Broman and Prof.
    [Show full text]