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DNA ligase III antibody [1F3]

GTX70143
GeneTex
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, Neutralisation/Blocking, Other Application
Product group Antibodies
TargetLIG3
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Overview

  • Supplier
    GeneTex
  • Product Name
    DNA ligase III antibody [1F3]
  • Delivery Days Customer
    9
  • Application Supplier Note
    WB: 1:500-1:3000. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
  • Applications
    ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, Neutralisation/Blocking, Other Application
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Clone ID
    1F3
  • Concentration
    1 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID3980
  • Target name
    LIG3
  • Target description
    DNA ligase 3
  • Target synonyms
    LIG2, LIG3alpha, MTDPS20, DNA ligase 3, ligase II, DNA, ATP-dependent, ligase III, DNA, ATP-dependent, polydeoxyribonucleotide synthase [ATP] 3
  • Host
    Mouse
  • Isotype
    IgG1
  • Protein IDP49916
  • Protein Name
    DNA ligase 3
  • Scientific Description
    This gene is a member of the DNA ligase family. Each member of this family encodes a protein that catalyzes the joining of DNA ends but they each have a distinct role in DNA metabolism. The protein encoded by this gene is involved in excision repair and is located in both the mitochondria and nucleus, with translation initiation from the upstream start codon allowing for transport to the mitochondria and translation initiation from a downstream start codon allowing for transport to the nucleus. Additionally, alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008]
  • Storage Instruction
    -20°C or -80°C,2°C to 8°C
  • UNSPSC
    12352203

References

  • Rubio-Contreras D, Gómez-Herreros F. TDP1 suppresses chromosomal translocations and cell death induced by abortive TOP1 activity during gene transcription. Nat Commun. 2023,14(1):6940. doi: 10.1038/s41467-023-42622-7
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  • Nie L, Wang C, Huang M, et al. DePARylation is critical for S phase progression and cell survival. bioRxiv. 2024,:pii: 2023.07.31.551317. doi: 10.1101/2023.07.31.551317.
    Read this paper
  • Cong K, Peng M, Kousholt AN, et al. Replication gaps are a key determinant of PARP inhibitor synthetic lethality with BRCA deficiency. Mol Cell. 2021,81(15):3128-3144.e7. doi: 10.1016/j.molcel.2021.06.011
    Read this paper
  • Shamanna RA, Lu H, de Freitas JK, et al. WRN regulates pathway choice between classical and alternative non-homologous end joining. Nat Commun. 2016,7:13785. doi: 10.1038/ncomms13785
    Read this paper
  • Szczesny B, Marcatti M, Zatarain JR, et al. Inhibition of hydrogen sulfide biosynthesis sensitizes lung adenocarcinoma to chemotherapeutic drugs by inhibiting mitochondrial DNA repair and suppressing cellular bioenergetics. Sci Rep. 2016,6:36125. doi: 10.1038/srep36125
    Read this paper
  • Horton JK, Stefanick DF, Prasad R, et al. Base excision repair defects invoke hypersensitivity to PARP inhibition. Mol Cancer Res. 2014,12(8):1128-39. doi: 10.1158/1541-7786.MCR-13-0502
    Read this paper
  • Moscariello M, Iliakis G. Effects of chromatin decondensation on alternative NHEJ. DNA Repair (Amst). 2013,12(11):972-81. doi: 10.1016/j.dnarep.2013.08.004
    Read this paper
  • 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
    Read this paper
  • 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
    Read this paper
  • Paul K, Wang M, Mladenov E, et al. DNA ligases I and III cooperate in alternative non-homologous end-joining in vertebrates. PLoS One. 2013,8(3):e59505. doi: 10.1371/journal.pone.0059505
    Read this paper