| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Flap endonuclease 1; FEN-1; DNase IV; Flap structure-specific endonuclease 1; Maturation factor 1; MF1; hFEN-1 |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | E.coli-derived human FEN1 recombinant protein (Position: Q4-E300). |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
Anti-FEN1 Antibody Picoband® is an antibody for FEN1 detection raised in Rabbit (Polyclonal, Rabbit IgG), with reported reactivity: Human,Mouse,Rat. Commonly used in WB, IHC, IF, ICC, Flow Cytometry, ELISA workflows.
Key elements and design rationale
- Target: FEN1 (flap structure-specific endonuclease 1); UniProt: P39748
- Antibody format: Rabbit, Polyclonal, Rabbit IgG
- Molecular weight: 43 kDa, calculated 75679 MW
- Applications: WB, IHC, IF, ICC, Flow Cytometry, ELISA
Vendor description (summary): Boster Bio Anti-FEN1 Antibody Picoband® catalog # A01484-1.
Biological background
Biological context: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Expression and localization notes: cellular localization: Membrane ; Multi-pass membrane protein ., tissue context: Predominantly expressed in the liver (PubMed:11099417, PubMed:11452359). Low expression levels in the small intestine and colon (PubMed:11099417). Very low levels in other tissues, including brain, heart and spleen (PubMed:11452359)..
Common research applications
- Western blotting (WB): Compare FEN1 levels across samples and conditions using appropriate loading and biological controls.
- Immunohistochemistry (IHC): Evaluate spatial distribution of FEN1 in tissue sections, considering fixation and antigen retrieval effects.
- Immunofluorescence / ICC: Assess subcellular localization patterns and co-localization with compartment markers in cultured cells.
- Flow cytometry: Quantify FEN1-positive populations in single-cell suspensions with appropriate gating and controls.
- ELISA: Use antibody-based detection formats to assess antigen presence or binding in plate-based assays.
Notes for experimental interpretation
- Account for isoforms, post-translational modifications, and sample-specific processing that can shift apparent molecular weight or epitope accessibility.
- Use positive/negative biological controls where possible (e.g., known-expressing cells/tissues, knockdown/knockout models) and include appropriate secondary-only/isotype controls for imaging workflows.
Additional product notes (from provided fields)
- Specificity: No cross reactivity with other proteins.
- Background: Flap endonuclease 1 is an enzyme that in humans is encoded by the FEN1 gene. It is mapped to 11q12.2. 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. 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.
- Cross reactivity: No cross-reactivity with other proteins.
- Cellular localization: Membrane ; Multi-pass membrane protein .
- Tissue details: Predominantly expressed in the liver (PubMed:11099417, PubMed:11452359). Low expression levels in the small intestine and colon (PubMed:11099417). Very low levels in other tissues, including brain, heart and spleen (PubMed:11452359).
- Research category: Atherosclerosis,Cancer,Cancer Metabolism,Cardiovascular,Cholesterol Metabolism,Heart Disease,Lipid and Lipoprotein Metabolism,Lipid Metabolism,Lipids/Lipoproteins,Metabolic Signaling Pathway,Metabolic Signaling Pathways,Metabolism,Metabolism of Lipids and Lipoproteins,Pathways and Processes,Signal Transduction
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
