Product: FEN1 Mouse Monoclonal Antibody
Catalog: BF8322
Description: Mouse monoclonal antibody to FEN1
Application: WB
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 43kDa; 43kD(Calculated).
Uniprot: P39748

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 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

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Product Info

Source:
Mouse
Application:
WB 1:500-1:3000
*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.

Reactivity:
Human,Mouse,Rat
Clonality:
Monoclonal [AFfirm8322]
Specificity:
FEN1 Mouse Monoclonal Antibody detects endogenous levels of total FEN1
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

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

Immunogen:
Uniprot:
Gene(ID):
Description:
Flap endonuclease-1 (FEN-1) is a structure-specific nuclease with multiple functions in DNA processing pathways (1,2). The replication and DNA repair activities of FEN-1 are critical for genomic stability in the eukaryotic cell. Through interaction with proliferation cell nuclear antigen (PCNA), FEN-1 helps coordinate Okazaki fragment maturation by removing RNA-DNA primers (3). FEN-1 is also required for non-homologous end joining of double stranded DNA breaks in long patch base excision repair (4,5). The multi-functional activities of FEN-1 are regulated by various mechanisms, including protein partner interactions (6,7), post-translational modifications (8,9), and subcellular re-localization in response to cell cycle or DNA damage (10).
Sequence:
MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK

PTMs - P39748 As Substrate

Site PTM Type Enzyme
K8 Ubiquitination
S16 Phosphorylation
R19 Methylation
K24 Sumoylation
K24 Ubiquitination
K80 Acetylation
K80 Ubiquitination
K88 Sumoylation
K88 Ubiquitination
K93 Sumoylation
K99 Ubiquitination
R100 Methylation
S101 Phosphorylation
R104 Methylation
K109 Acetylation
K109 Ubiquitination
K125 Acetylation
K125 Sumoylation
K125 Ubiquitination
K128 Sumoylation
K128 Ubiquitination
K132 Ubiquitination
K135 Ubiquitination
K142 Ubiquitination
C163 S-Nitrosylation
K168 Sumoylation
K168 Ubiquitination
K171 Ubiquitination
S187 Phosphorylation P06493 (CDK1)
R192 Methylation
T195 Phosphorylation O14757 (CHEK1)
S197 Phosphorylation
K200 Acetylation
K200 Ubiquitination
K201 Acetylation
K201 Sumoylation
K201 Ubiquitination
Y234 Phosphorylation
K252 Ubiquitination
K254 Sumoylation
K254 Ubiquitination
S255 Phosphorylation
K267 Acetylation
K267 Sumoylation
K267 Ubiquitination
Y268 Phosphorylation
K277 Ubiquitination
S293 Phosphorylation
K297 Sumoylation
K297 Ubiquitination
K308 Sumoylation
K308 Ubiquitination
K314 Sumoylation
K314 Ubiquitination
S317 Phosphorylation
S329 Phosphorylation
S331 Phosphorylation
S335 Phosphorylation
T336 Phosphorylation
K345 Methylation
K345 Sumoylation
K345 Ubiquitination
S349 Phosphorylation
S351 Phosphorylation
S352 Phosphorylation
K354 Acetylation
K354 Sumoylation
K354 Ubiquitination
S363 Phosphorylation
T364 Phosphorylation
K375 Acetylation
K375 Sumoylation
K377 Acetylation
K380 Acetylation

Research Backgrounds

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 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.

PTMs:

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.

Subcellular Location:

Nucleus>Nucleolus. Nucleus>Nucleoplasm.
Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.

Mitochondrion.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

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.

Family&Domains:

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.

Restrictive clause

 

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