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IHC-P analysis of human tonsil tissue using GTX22175 RPA32 antibody [9H8].
IHC-P analysis of human tonsil tissue using GTX22175 RPA32 antibody [9H8].
IHC-P analysis of human tonsil tissue using GTX22175 RPA32 antibody [9H8].

RPA32 antibody [9H8]

GTX22175
GeneTex
ApplicationsImmunoFluorescence, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityHuman, Monkey
TargetRPA2
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Overview

  • Supplier
    GeneTex
  • Product Name
    RPA32 antibody [9H8]
  • Delivery Days Customer
    9
  • Application Supplier Note
    IHC-P: 1:50-1:100. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
  • Applications
    ImmunoFluorescence, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    9H8
  • Conjugate
    Unconjugated
  • Gene ID6118
  • Target name
    RPA2
  • Target description
    replication protein A2
  • Target synonyms
    REPA2, RP-A p32, RP-A p34, RPA32, replication protein A 32 kDa subunit, RF-A protein 2, replication factor A protein 2, replication protein A 34 kDa subunit
  • Host
    Mouse
  • Isotype
    IgG1
  • Protein IDP15927
  • Protein Name
    Replication protein A 32 kDa subunit
  • Scientific Description
    This gene encodes a subunit of the heterotrimeric Replication Protein A (RPA) complex, which binds to single-stranded DNA (ssDNA), forming a nucleoprotein complex that plays an important role in DNA metabolism, being involved in DNA replication, repair, recombination, telomere maintenance, and co-ordinating the cellular response to DNA damage through activation of the ataxia telangiectasia and Rad3-related protein (ATR) kinase. The RPA complex protects single-stranded DNA from nucleases, prevents formation of secondary structures that would interfere with repair, and co-ordinates the recruitment and departure of different genome maintenance factors. The heterotrimeric complex has two different modes of ssDNA binding, a low-affinity and high-affinity mode, determined by which oligonucleotide/oligosaccharide-binding (OB) domains of the complex are utilized, and differing in the length of DNA bound. This subunit contains a single OB domain that participates in high-affinity DNA binding and also contains a winged helix domain at its carboxy terminus, which interacts with many genome maintenance protein. Post-translational modifications of the RPA complex also plays a role in co-ordinating different damage response pathways. [provided by RefSeq, Sep 2017]
  • Reactivity
    Human, Monkey
  • Storage Instruction
    2°C to 8°C
  • UNSPSC
    12352203

References

  • Evangelista FM, Maglott-Roth A, Stierle M, et al. Transcription and mRNA export machineries SAGA and TREX-2 maintain monoubiquitinated H2B balance required for DNA repair. J Cell Biol. 2018,217(10):3382-3397. doi: 10.1083/jcb.201803074
    Read this paper
  • Nera B, Huang HS, Lai T, et al. Elevated levels of TRF2 induce telomeric ultrafine anaphase bridges and rapid telomere deletions. Nat Commun. 2015,6:10132. doi: 10.1038/ncomms10132
    Read this paper
  • Smith S, Reuven N, Mohni KN, et al. Structure of the herpes simplex virus 1 genome: manipulation of nicks and gaps can abrogate infectivity and alter the cellular DNA damage response. J Virol. 2014,88(17):10146-56. doi: 10.1128/JVI.01723-14
    Read this paper
  • Zhou Y, Caron P, Legube G, et al. Quantitation of DNA double-strand break resection intermediates in human cells. Nucleic Acids Res. 2014,42(3):e19. doi: 10.1093/nar/gkt1309
    Read this paper
  • Mohni KN, Smith S, Dee AR, et al. Herpes simplex virus type 1 single strand DNA binding protein and helicase/primase complex disable cellular ATR signaling. PLoS Pathog. 2013,9(10):e1003652. doi: 10.1371/journal.ppat.1003652
    Read this paper
  • Mohni KN, Dee AR, Smith S, et al. Efficient herpes simplex virus 1 replication requires cellular ATR pathway proteins. J Virol. 2013,87(1):531-42. doi: 10.1128/JVI.02504-12
    Read this paper
  • Mohni KN, Livingston CM, Cortez D, et al. ATR and ATRIP are recruited to herpes simplex virus type 1 replication compartments even though ATR signaling is disabled. J Virol. 2010,84(23):12152-64. doi: 10.1128/JVI.01643-10
    Read this paper