protein

FEN1, 1-380aa, Human, E Coli

MBS203445

0.1 mg

375 USD

Recombinant Protein

FEN1, 1-380aa, Human, E Coli

FEN1

FEN-1; MF1; RAD2; Flap structure-specific endonuclease 1 DNase IV; Flap endonuclease 1; Flap structure specific endonuclease 1; hFEN1; Maturation factor 1

flap endonuclease 1; Flap endonuclease 1; flap endonuclease 1; DNase IV; FEN-1; FEN1; maturation factor 1; maturation factor-1; flap structure-specific endonuclease 1; DNase IVFlap structure-specific endonuclease 1

FEN1

FEN1; FEN1; MF1; RAD2; FEN-1;

FEN1_HUMAN

380

MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG DVLQNEEGET TSHLMGMFYR TIRMMENGIK PVYVFDGKPP QLKSGELAKR SERRAEAEKQ LQQAQAAGAE QEVEKFTKRL VKVTKQHNDE CKHLLSLMGI PYLDAPSEAE ASCAALVKAG KVYAAATEDM DCLTFGSPVL MRHLTASEAK KLPIQEFHLS RILQELGLNQ EQFVDLCILL GSDYCESIRG IGPKRAVDLI QKHKSIEEIV RRLDPNKYPV PENWLHKEAH QLFLEPEVLD PESVELKWSE PNEEELIKFM CGEKQFSEER IRSGVKRLSK SRQGSTQGRL DDFFKVTGSL SSAKRKEPEP KGSTKKKAKT GAAGKFKRGK

> 90% by SDS - PAGE

Liquid. In 20 mM Tris-HCl buffer (pH8.0) containing 1mM DTT 10% glycerol

1 mg/ml (determined by Bradford assay)

Can be stored at 4 degree C short term (1-2 weeks). For long term storage, aliquot and store at -20 degree C or -70 degree C. Avoid repeated freezing and thawing cycles.

SDS-PAGE

Antigen Species: Human

Expression System: E Coli

Enzymes & Proteases

FEN-1, also known as Flap structure-specific endonuclease 1, removes 5' overhanging flaps in DNA repair and processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis. The protein is a member of the XPG/RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. FEN-1 is highly homologous to yeast Rad2. The C-terminal region of FEN-1 may bind to PCNA, thus allowing FEN-1 to function as an exonuclease in DNA replication. Recombinant human FEN-1 protein was expressed in E.coli and purified by using conventional chromatography techniques.

Hakoyama T., et al. (2009) Nature. 462(7272):514-7. Lal A., et al. (2009) Mol Cell. 35(5):610-25.

4758356

NP_004102

NM_004111.5

42.5 kDa (380aa), confirmed by MALDI-TOF.

Base Excision Repair Pathway (105838); Base Excision Repair Pathway (83043); Base Excision Repair Pathway (451); Cell Cycle Pathway (530733); Cell Cycle, Mitotic Pathway (105765); Chromosome Maintenance Pathway (161048); DNA Repair Pathway (105837); DNA Replication Pathway (105897); DNA Replication Pathway (83039); DNA Replication Pathway (444)

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. [provided by RefSeq, Jul 2008]

FEN1: 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. Interacts with PCNA. 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 DDX11. Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily. Protein type: DNA-binding; Nucleolus; Nuclear receptor co-regulator; Ribonuclease; Deoxyribonuclease; DNA repair, damage; EC 3.1.-.-. Chromosomal Location of Human Ortholog: 11q12. Cellular Component: nucleoplasm; mitochondrion; membrane; nucleolus; plasma membrane; nucleus. Molecular Function: 5 -3 exonuclease activity; protein binding; DNA binding; 5 -flap endonuclease activity; endonuclease activity; manganese ion binding; double-stranded DNA binding; exonuclease activity; magnesium ion binding; damaged DNA binding; ribonuclease H activity; double-stranded DNA specific exodeoxyribonuclease activity. Biological Process: telomere maintenance via semi-conservative replication; DNA replication, removal of RNA primer; UV protection; base-excision repair; double-strand break repair; telomere maintenance via recombination; mitotic cell cycle; DNA strand elongation during DNA replication; DNA catabolic process, exonucleolytic; DNA repair; DNA replication; DNA catabolic process, endonucleolytic; telomere maintenance; memory

0.1 mg

375 USD

0.5 mg

925