FEN1 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P39748 |
---|---|
Clone Names | 80317176 |
Gene ID | 2237 |
---|---|
Other Names | Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}, FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140}, 31-- {ECO:0000255|HAMAP-Rule:MF_03140}, DNase IV, Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140}, Maturation factor 1, MF1, hFEN-1, FEN1 {ECO:0000255|HAMAP-Rule:MF_03140}, RAD2 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2856c was selected from the Center region of human FEN1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | FEN1 {ECO:0000255|HAMAP-Rule:MF_03140} |
---|---|
Synonyms | RAD2 |
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. |
Cellular Location | [Isoform 1]: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Background
FEN1 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. This 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.
References
Hiraoka L.R., Harrington J.J., Gerhard D.S., Genomics 25:220-225(1995) Robins P., Pappin D.J.C., Wood R.D., Lindahl T.J. Biol. Chem. 269:28535-28538(1994) Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A.,J. Biol. Chem. 272:24522-24529(1997)
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.