Flap Structure Specific Endonuclease 1 (FEN1) Antibody
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Description
Rabbit polyclonal antibody against FEN1 protein. Immunogen region is Internal.
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Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Flap Structure Specific Endonuclease 1 (FEN1) |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Recommended Dilution | WB: 1/500 - 1/3000, IHC: 1/50 - 1/100, IF/ICC: 1/100 - 1/500, ELISA: 1/5000. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Purification | Purified from rabbit antiserum by affinity chromatography using epitope-specific immunogen. |
| Size 1 | 10 µg |
| Size 2 | 100 µg |
| Size 3 | 200 µg |
| Size 4 | 300 µg |
| Size 5 | 1 mg |
| Form | Liquid |
| Tested Applications | ELISA, WB, IHC, IF/ICC |
| Buffer | PBS (without Mg<sup>2+</sup> and Ca<sup>2+</sup>), pH 7.4, 150 mM NaCl, 0.02% sodium azide, 50% glycerol. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P39748 |
| Background | Antibody anti-FEN1 |
| Status | RUO |
| Note | Concentration: 1 mg/ml - |
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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