Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
host | mouse |
isotype | IgG1 |
clonality | monoclonal |
concentration | 1 mg/mL |
applications | ICC/IF, WB |
reactivity | Fen-1 |
available sizes | 100 µg |
mouse anti-Fen-1 monoclonal antibody (4E7) 3657
$503.00
Antibody summary
- Mouse monoclonal to Fen-1
- Suitable for: WB,ICC/IF,IP
- Isotype: IgG1
- 100 µg
mouse anti-Fen-1 monoclonal antibody (4E7) 3657
antibody |
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Tested applications WB,ICC/IF,IP |
Recommended dilutions Immunoblotting: use at 1-5 ug/mL. Positive controls: MCF-7 cells and recombinant fusion protein. |
Immunogen Recombinant human FEN-1 protein (aa 1-380) purified from baculovirus-infected Sf-9 cells. |
Size and concentration 100µg and lot specific |
Form liquid |
Storage Instructions This antibody is stable for at least one (1) year at -20°C. Avoid multiple freeze- thaw cycles. |
Storage buffer 10 mM PBS, pH 7.4. |
Purity immunogen affinity purification |
Clonality monoclonal |
Isotype IgG1 |
Compatible secondaries goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody 5486 goat anti-mouse IgG, H&L chain specific, biotin conjugated, Conjugate polyclonal antibody 2685 goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody 7854 goat anti-mouse IgG, H&L chain specific, peroxidase conjugated polyclonal antibody, crossabsorbed 1706 goat anti-mouse IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1716 goat anti-mouse IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1721 |
Isotype control Mouse monocolonal IgG1 - Isotype Control |
target relevance |
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Protein names Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (DNase IV) (Flap structure-specific endonuclease 1) (Maturation factor 1) (MF1) (hFEN-1) |
Gene names FEN1,FEN1 RAD2 |
Protein family XPG/RAD2 endonuclease family, FEN1 subfamily |
Mass 42593Da |
Function FUNCTION: 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 structures 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. {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:10744741, ECO:0000269|PubMed:11986308, ECO:0000269|PubMed:18443037, ECO:0000269|PubMed:20729856, ECO:0000269|PubMed:26751069, ECO:0000269|PubMed:7961795, ECO:0000269|PubMed:8621570}. |
Subellular location SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.; SUBCELLULAR LOCATION: [Isoform FENMIT]: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:23675412}. |
Structure SUBUNIT: Interacts with PCNA (PubMed:11430825, PubMed:15616578, PubMed:26760506, PubMed:9305916). Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer (PubMed:15616578). PCNA stimulates the nuclease activity without altering cleavage specificity (PubMed:15616578). The C-terminal domain binds EP300; can bind simultaneously to both PCNA and EP300 (PubMed:11430825). Interacts with DDX11; this interaction is direct and increases flap endonuclease activity of FEN1 (PubMed:18499658). Interacts with WDR4; regulating its endonuclease activity (PubMed:26751069). Interacts with POLB (PubMed:19336415, PubMed:26760506). {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:11430825, ECO:0000269|PubMed:15616578, ECO:0000269|PubMed:18499658, ECO:0000269|PubMed:19336415, ECO:0000269|PubMed:26751069, ECO:0000269|PubMed:26760506, ECO:0000269|PubMed:9305916}. |
Post-translational modification PTM: Acetylated by EP300. Acetylation inhibits both endonuclease and exonuclease activity. Acetylation also reduces DNA-binding activity but does not affect interaction with PCNA or EP300. {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:11430825}.; PTM: Phosphorylation upon DNA damage induces relocalization to the nuclear plasma. Phosphorylation at Ser-187 by CDK2 occurs during late S-phase and results in dissociation from PCNA. {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856}.; PTM: Methylation at Arg-192 by PRMT5 impedes Ser-187 phosphorylation and increases interaction with PCNA. {ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856}. |
Target Relevance information above includes information from UniProt accession: P39748 |
The UniProt Consortium |
Data
Publications
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