FEN1 (NM_004111) Human Tagged ORF Clone Lentiviral Particle

CAT#: RC201785L1V

Lenti ORF particles, FEN1 (Myc-DDK tagged) - Human flap structure-specific endonuclease 1 (FEN1), 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: Myc-DDK
• Symbol: FEN1
• Synonyms: FEN-1; MF1; RAD2
• Mammalian Cell Selection: None
• Vector: pLenti-C-Myc-DDK
• ACCN: NM_004111
• ORF Size: 1140 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC201785).
• OTI Disclaimer: The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info
• OTI Annotation: This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene.

Reference Data

• RefSeq: NM_004111.4
• RefSeq Size: 2308 bp
• RefSeq ORF: 1143 bp
• Locus ID: 2237
• UniProt ID: P39748
• Cytogenetics: 11q12.2
• Domains: HhH2, XPG_N, XPG_I
• Protein Families: Druggable Genome, Stem cell - Pluripotency
• Protein Pathways: Base excision repair, DNA replication, Non-homologous end-joining
• MW: 42.6 kDa
• Gene Summary: 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]