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DNA ligase I antibody [10H5]

GTX70141
GeneTex
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
TargetLIG1
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Overview

  • Supplier
    GeneTex
  • Product Name
    DNA ligase I antibody [10H5]
  • Delivery Days Customer
    9
  • Applications
    ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    10H5
  • Concentration
    0.5 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID3978
  • Target name
    LIG1
  • Target description
    DNA ligase 1
  • Target synonyms
    IMD96, LIGI, hLig1, DNA ligase 1, ligase I, DNA, ATP-dependent, polydeoxyribonucleotide synthase [ATP] 1
  • Host
    Mouse
  • Isotype
    IgG1
  • Protein IDP18858
  • Protein Name
    DNA ligase 1
  • Scientific Description
    This gene encodes a member of the ATP-dependent DNA ligase protein family. The encoded protein functions in DNA replication, recombination, and the base excision repair process. Mutations in this gene that lead to DNA ligase I deficiency result in immunodeficiency and increased sensitivity to DNA-damaging agents. Disruption of this gene may also be associated with a variety of cancers. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
  • Storage Instruction
    -20°C or -80°C,2°C to 8°C
  • UNSPSC
    12352203

References

  • Wei L, Ploss A. Hepatitis B virus cccDNA is formed through distinct repair processes of each strand. Nat Commun. 2021,12(1):1591. doi: 10.1038/s41467-021-21850-9
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  • Wei L, Ploss A. Core components of DNA lagging strand synthesis machinery are essential for hepatitis B virus cccDNA formation. Nat Microbiol. 2020,5(5):715-726. doi: 10.1038/s41564-020-0678-0
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  • Tsai YC, Wang YH, Liu YC. Overexpression of PCNA Attenuates Oxidative Stress-Caused Delay of Gap-Filling during Repair of UV-Induced DNA Damage. J Nucleic Acids. 2017,2017:8154646. doi: 10.1155/2017/8154646
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  • Yuan Y, Britton S, Delteil C, et al. Single-stranded DNA oligomers stimulate error-prone alternative repair of DNA double-strand breaks through hijacking Ku protein. Nucleic Acids Res. 2015,43(21):10264-76. doi: 10.1093/nar/gkv894
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  • Horton JK, Stefanick DF, Gassman NR, et al. Preventing oxidation of cellular XRCC1 affects PARP-mediated DNA damage responses. DNA Repair (Amst). 2013,12(9):774-85. doi: 10.1016/j.dnarep.2013.06.004
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  • Masaoka A, Gassman NR, Horton JK, et al. Interaction between DNA Polymerase β and BRCA1. PLoS One. 2013,8(6):e66801. doi: 10.1371/journal.pone.0066801
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  • Prasad R, Williams JG, Hou EW, et al. Pol β associated complex and base excision repair factors in mouse fibroblasts. Nucleic Acids Res. 2012,40(22):11571-82. doi: 10.1093/nar/gks898
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  • Asagoshi K, Liu Y, Masaoka A, et al. DNA polymerase beta-dependent long patch base excision repair in living cells. DNA Repair (Amst). 2010,9(2):109-19. doi: 10.1016/j.dnarep.2009.11.002
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  • Guo Z, Zheng L, Dai H, et al. Human DNA polymerase beta polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity. Nucleic Acids Res. 2009,37(10):3431-41. doi: 10.1093/nar/gkp201
    Read this paper
  • Song W, Levin DS, Varkey J, et al. A conserved physical and functional interaction between the cell cycle checkpoint clamp loader and DNA ligase I of eukaryotes. J Biol Chem. 2007,282(31):22721-30.
    Read this paper