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Mouse Anti-FEN1 Recombinant Antibody (CBXF-0489) (CBMAB-F2299-CQ)

This product is a mouse antibody that recognizes FEN1. The antibody CBXF-0489 can be used for immunoassay techniques such as: ICC, WB.
See all FEN1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-0489
Antibody Isotype
IgG
Application
ICC, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4, 50% glycerol
Preservative
0.02% sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Flap Structure-Specific Endonuclease 1
Introduction
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.
Entrez Gene ID
2237
UniProt ID
P39748
Alternative Names
Flap Structure-Specific Endonuclease 1; DNase IV; Maturation Factor-1; FEN-1; RAD2; MF1;
Research Area
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.
Biological Process
Base-excision repair, gap-filling Source: Reactome
DNA repair Source: ProtInc
DNA replication Source: ProtInc
DNA replication, removal of RNA primer Source: UniProtKB
Double-strand break repair Source: ProtInc
Double-strand break repair via homologous recombination Source: Reactome
Memory Source: Ensembl
Nucleic acid phosphodiester bond hydrolysis Source: UniProtKB
Positive regulation of sister chromatid cohesion Source: UniProtKB
Telomere maintenance via semi-conservative replication Source: Reactome
UV protection Source: ProtInc
Cellular Location
Isoform 1: Nucleolus; Nucleoplasm. Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.
Isoform FENMIT: Mitochondrion
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.
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.

Liao, C., Talluri, S., Mu, S., Kumar, S., Potluri, L. B., Shi, J., ... & Munshi, N. C. (2022). Flap Structure-Specific Endonuclease 1 Coordinates with a Helicase (ASCC3) to Drive Genomic Instability, Proliferation and Poor Clinical Outcome in Myeloma. Blood, 140(Supplement 1), 9963-9963.

Wei, X. R., Meng, Y., Xu, Q., Hu, J., & Zhang, C. Y. (2022). Label-free and homogeneous detection of flap endonuclease 1 by ligation-promoted hyperbranched rolling circle amplification platform. Talanta, 243, 123342.

Zhao, M., Ji, H., Fu, Q., Cheng, Q., Zhang, Y., & Yang, Y. (2021). MicroRNA-134-3p inhibits ovarian cancer progression by targeting flap structure-specific endonuclease 1 in vitro. Oncology Reports, 45(1), 119-128.

Schilling, E. M., Scherer, M., Rothemund, F., & Stamminger, T. (2021). Functional regulation of the structure-specific endonuclease FEN1 by the human cytomegalovirus protein IE1 suggests a role for the re-initiation of stalled viral replication forks. PLoS Pathogens, 17(3), e1009460.

Li, B., Zhang, P., Zhou, B., Xie, S., Xia, A., Suo, T., ... & Zhang, X. (2021). Fluorometric detection of cancer marker FEN1 based on double-flapped dumbbell DNA nanoprobe functionalized with silver nanoclusters. Analytica Chimica Acta, 1148, 238194.

Yang, H., Wang, C., Xu, E., Wei, W., Liu, Y., & Liu, S. (2021). Dual-mode FEN1 activity detection based on Nt. BstNBI-induced tandem signal amplification. Analytical Chemistry, 93(16), 6567-6572.

Wei, Q., Shen, J., Wang, D., Han, X., Shi, J., Zhao, L., & Teng, Y. (2021). A bibliometric analysis of researches on flap endonuclease 1 from 2005 to 2019. BMC cancer, 21(1), 1-14.

Zhong, G., Wang, Y., Wei, H., Chen, M., Lin, H., Huang, Z., ... & Lin, J. (2021). The Clinical Significance of the Expression of FEN1 in Primary Osteosarcoma. International Journal of General Medicine, 14, 6477.

Zhang, H., Ba, S., Mahajan, D., Lee, J. Y., Ye, R., Shao, F., ... & Li, T. (2018). Versatile types of DNA-based nanobiosensors for specific detection of cancer biomarker FEN1 in living cells and cell-free systems. Nano Letters, 18(11), 7383-7388.

Kitamura, K., Que, L., Shimadu, M., Koura, M., Ishihara, Y., Wakae, K., ... & Muramatsu, M. (2018). Flap endonuclease 1 is involved in cccDNA formation in the hepatitis B virus. PLoS pathogens, 14(6), e1007124.

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For research use only. Not intended for any clinical use.

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