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FEN1 antibody [4E7]

GTX70185
GeneTex
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry
Product group Antibodies
TargetFEN1
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Overview

  • Supplier
    GeneTex
  • Product Name
    FEN1 antibody [4E7]
  • 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, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry
  • Certification
    Research Use Only
  • Clonality
    Monoclonal
  • Concentration
    1.73 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID2237
  • Target name
    FEN1
  • Target description
    flap structure-specific endonuclease 1
  • Target synonyms
    FEN-1, MF1, RAD2, flap endonuclease 1, DNase IV, maturation factor-1
  • Host
    Mouse
  • Isotype
    IgG1
  • Protein IDP39748
  • Protein Name
    Flap endonuclease 1
  • Scientific Description
    The protein encoded by this gene removes 5 overhanging flaps in DNA repair and processes the 5 ends of Okazaki fragments in lagging strand DNA synthesis. Direct physical interaction between this protein and AP endonuclease 1 during long-patch base excision repair provides coordinated loading of the proteins onto the substrate, thus passing the substrate from one enzyme to another. The protein is a member of the XPG/RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. DNA secondary structure can inhibit flap processing at certain trinucleotide repeats in a length-dependent manner by concealing the 5 end of the flap that is necessary for both binding and cleavage by the protein encoded by this gene. Therefore, secondary structure can deter the protective function of this protein, leading to site-specific trinucleotide expansions. [provided by RefSeq, Jul 2008]
  • Storage Instruction
    -20°C or -80°C,2°C to 8°C
  • UNSPSC
    12352203

References

  • Hao Q, Zhan C, Lian C, et al. DNA repair mechanisms that promote insertion-deletion events during immunoglobulin gene diversification. Sci Immunol. 2023,8(81):eade1167. doi: 10.1126/sciimmunol.ade1167
    Read this paper
  • Ma Z, Wang W, Wang S, et al. Symmetrical dimethylation of H4R3: A bridge linking DNA damage and repair upon oxidative stress. Redox Biol. 2020,37:101653. doi: 10.1016/j.redox.2020.101653
    Read this paper
  • Li JL, Wang JP, Chang H, et al. FEN1 inhibitor increases sensitivity of radiotherapy in cervical cancer cells. Cancer Med. 2019,8(18):7774-7780. doi: 10.1002/cam4.2615
    Read this paper
  • Kanagaraj A, Sakamoto N, Que L, et al. Different antiviral activities of natural APOBEC3C, APOBEC3G, and APOBEC3H variants against hepatitis B virus. Biochem Biophys Res Commun. 2019,518(1):26-31. doi: 10.1016/j.bbrc.2019.08.003
    Read this paper
  • Kitamura K, Que L, Shimadu M, et al. Flap endonuclease 1 is involved in cccDNA formation in the hepatitis B virus. PLoS Pathog. 2018,14(6):e1007124. doi: 10.1371/journal.ppat.1007124
    Read this paper
  • Li Z, Liu B, Jin W, et al. hDNA2 nuclease/helicase promotes centromeric DNA replication and genome stability. EMBO J. 2018,37(14). doi: 10.15252/embj.201796729
    Read this paper
  • Zhang K, Keymeulen S, Nelson R, et al. Overexpression of Flap Endonuclease 1 Correlates with Enhanced Proliferation and Poor Prognosis of Non-Small-Cell Lung Cancer. Am J Pathol. 2018,188(1):242-251. doi: 10.1016/j.ajpath.2017.09.011
    Read this paper
  • Briest F, Grass I, Sedding D, et al. Mechanisms of Targeting the MDM2-p53-FOXM1 Axis in Well-Differentiated Intestinal Neuroendocrine Tumors. Neuroendocrinology. 2018,107(1):1-23. doi: 10.1159/000481506
    Read this paper
  • 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
    Read this paper
  • Sami F, Lu X, Parvathaneni S, et al. RECQ1 interacts with FEN-1 and promotes binding of FEN-1 to telomeric chromatin. Biochem J. 2015,468(2):227-44. doi: 10.1042/BJ20141021
    Read this paper