FEN1 antibody

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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.
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | flap structure-specific endonuclease 1 (FEN1) |
Host | Rabbit |
Reactivity | Human, Mouse |
Recommended Dilution | WB: 1:500 - 1:2000; IHC: 1:50 - 1:200; IF: 1:10 - 1:100; IP : 1:50 - 1:200 |
Clonality | polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Observed MW | 42 kDa |
Purity | ≥95% as determined by SDS-PAGE |
Purification | Immunogen affinity purified |
Size 1 | 100µg |
Form | liquid |
Tested Applications | ELISA, WB, IHC, IF, IP |
Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months (Avoid repeated freeze / thaw cycles.) |
UniProt ID | P39748 |
Gene ID | 2237 |
Alias | Flap endonuclease 1 (FEN-1),DNase IV,Flap structure-specific endonuclease 1,Maturation factor 1 (MF1, hFEN-1),FEN1,RAD2 |
Background | Antibody anti-FEN1 |
Status | RUO |
Note | Mol. Weight 42 kDa |
Descripción
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Human FEN1 (Flap endonuclease 1) ELISA Kit
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FEN1 antibody
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.
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