Recombinant Human FEN1
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Product specifications
| Category | Proteins and Peptides |
| Host | E.Coli |
| Reactivity | Human |
| Assay Data | Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg/ml by gently pipetting 2-3 times, don't vortex. |
| Recommended Dilution | ¥ |
| Isotype | ¥ |
| Clone ID | ¥ |
| Observed MW | 56.3 kDa |
| Expression | 1-316 |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Size 1 | 50μg |
| Size 2 | 200μg |
| Size 3 | 1mg |
| Form | Lyophilized powder |
| Tested Applications | Western Blot, ELISA |
| Buffer | Lyophilized from a 0.2 μm filtered solution in 10 mM Hepes, 500 mM NaCl with 5% trehalose, pH 7.4. |
| Availability | 7 days |
| Storage | The lyophilized protein is stable at -20 °C for up to 1 year. After reconstitution, the protein solution is stable at -20 to -80 °C for 3 months or 1 week at 2 to 8 °C under sterile conditions. For extended storage, it is recommended to further dilute in working aliquots, avoid repeated freeze/thaw cycle. |
| UniProt ID | P39748-2 |
| Alias | DNase IV, FEN 1, FEN1, Flap endonuclease 1, flap structure endonuclease 1, hFEN 1, Maturation factor 1, MF1, RAD2 |
| Background | Protein FEN1 |
| Status | RUO |
| Note | Tag : N-terminal His-IF2DI Tag |
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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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