FEN1 Antibody - #DF6309
Product: | FEN1 Antibody |
Catalog: | DF6309 |
Description: | Rabbit polyclonal antibody to FEN1 |
Application: | WB IHC |
Reactivity: | Human, Mouse, Rat |
Prediction: | Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken |
Mol.Wt.: | 43kDa; 43kD(Calculated). |
Uniprot: | P39748 |
RRID: | AB_2838275 |
Related Downloads
Protocols
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# DF6309, RRID:AB_2838275.
Fold/Unfold
DNase IV; FEN-1; FEN1; FEN1_HUMAN; Flap endonuclease 1; Flap structure specific endonuclease 1; Flap structure-specific endonuclease 1; hFEN-1; hFEN1; Maturation factor 1; MF1; Rad2;
Immunogens
- P39748 FEN1_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK
Predictions
Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.
High(score>80) Medium(80>score>50) Low(score<50) No confidence
PTMs - P39748 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
K8 | Ubiquitination | Uniprot | |
S16 | Phosphorylation | Uniprot | |
R19 | Methylation | Uniprot | |
K24 | Sumoylation | Uniprot | |
K24 | Ubiquitination | Uniprot | |
K80 | Acetylation | Uniprot | |
K80 | Ubiquitination | Uniprot | |
K88 | Sumoylation | Uniprot | |
K88 | Ubiquitination | Uniprot | |
K93 | Sumoylation | Uniprot | |
K99 | Ubiquitination | Uniprot | |
R100 | Methylation | Uniprot | |
S101 | Phosphorylation | Uniprot | |
R104 | Methylation | Uniprot | |
K109 | Acetylation | Uniprot | |
K109 | Ubiquitination | Uniprot | |
K125 | Acetylation | Uniprot | |
K125 | Sumoylation | Uniprot | |
K125 | Ubiquitination | Uniprot | |
K128 | Sumoylation | Uniprot | |
K128 | Ubiquitination | Uniprot | |
K132 | Ubiquitination | Uniprot | |
K135 | Ubiquitination | Uniprot | |
K142 | Ubiquitination | Uniprot | |
C163 | S-Nitrosylation | Uniprot | |
K168 | Sumoylation | Uniprot | |
K168 | Ubiquitination | Uniprot | |
K171 | Ubiquitination | Uniprot | |
S187 | Phosphorylation | P06493 (CDK1) | Uniprot |
R192 | Methylation | Uniprot | |
T195 | Phosphorylation | O14757 (CHEK1) | Uniprot |
S197 | Phosphorylation | Uniprot | |
K200 | Acetylation | Uniprot | |
K200 | Ubiquitination | Uniprot | |
K201 | Acetylation | Uniprot | |
K201 | Sumoylation | Uniprot | |
K201 | Ubiquitination | Uniprot | |
Y234 | Phosphorylation | Uniprot | |
K252 | Ubiquitination | Uniprot | |
K254 | Sumoylation | Uniprot | |
K254 | Ubiquitination | Uniprot | |
S255 | Phosphorylation | Uniprot | |
K267 | Acetylation | Uniprot | |
K267 | Sumoylation | Uniprot | |
K267 | Ubiquitination | Uniprot | |
Y268 | Phosphorylation | Uniprot | |
K277 | Ubiquitination | Uniprot | |
S293 | Phosphorylation | Uniprot | |
K297 | Sumoylation | Uniprot | |
K297 | Ubiquitination | Uniprot | |
K308 | Sumoylation | Uniprot | |
K308 | Ubiquitination | Uniprot | |
K314 | Sumoylation | Uniprot | |
K314 | Ubiquitination | Uniprot | |
S317 | Phosphorylation | Uniprot | |
S329 | Phosphorylation | Uniprot | |
S331 | Phosphorylation | Uniprot | |
S335 | Phosphorylation | Uniprot | |
T336 | Phosphorylation | Uniprot | |
K345 | Methylation | Uniprot | |
K345 | Sumoylation | Uniprot | |
K345 | Ubiquitination | Uniprot | |
S349 | Phosphorylation | Uniprot | |
S351 | Phosphorylation | Uniprot | |
S352 | Phosphorylation | Uniprot | |
K354 | Acetylation | Uniprot | |
K354 | Sumoylation | Uniprot | |
K354 | Ubiquitination | Uniprot | |
S363 | Phosphorylation | Uniprot | |
T364 | Phosphorylation | Uniprot | |
K375 | Acetylation | Uniprot | |
K375 | Sumoylation | Uniprot | |
K377 | Acetylation | Uniprot | |
K380 | Acetylation | Uniprot |
Research Backgrounds
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.
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.
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.
Methylation at Arg-192 by PRMT5 impedes Ser-187 phosphorylation and increases interaction with PCNA.
Nucleus>Nucleolus. Nucleus>Nucleoplasm.
Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.
Mitochondrion.
Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity. The C-terminal domain binds EP300; can bind simultaneously to both PCNA and EP300. Interacts with PCNA; can bind simultaneously to both PCNA and EP300. Interacts with DDX11; this interaction is direct and increases flap endonuclease activity of FEN1. Interacts with WDR4; regulating its endonuclease activity.
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Research Fields
· Genetic Information Processing > Replication and repair > DNA replication.
· Genetic Information Processing > Replication and repair > Base excision repair.
· Genetic Information Processing > Replication and repair > Non-homologous end-joining.
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