Recombinant Human Flap Endonuclease 1 (FEN1) Protein (His&Myc)

Name: Recombinant Human Flap Endonuclease 1 (FEN1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04735P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Flap Endonuclease 1 (FEN1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P39748
Target Symbol	FEN1
Synonyms	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
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK
Expression Range	1-380aa
Protein Length	Full Length
Mol. Weight	50.0 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	[Isoform 1]: Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.; [Isoform FENMIT]: Mitochondrion.
Protein Families	XPG/RAD2 endonuclease family, FEN1 subfamily
Database References	HGNC: 3650 OMIM: 600393 KEGG: hsa:2237 STRING: 9606.ENSP00000305480 UniGene: PMID: 29937070 FEN1 was an independent predictor of survival in pancreatic ductal adenocarcinoma PMID: 29735403 The FEN1 rs174538 A allele is a novel protective biomarker for endometriosis PMID: 29109095 This study revealed that cell apoptosis dysfunction plays a key role in the pathogenesis of LN, even though the difference in FEN1 gene 61563142-61563342 between LN patients and healthy individuals was not statistically significant. PMID: 29239254 Results suggest that FEN1 polymorphisms may reduce the risk of breast cancer in Chinese women. PMID: 27801669 FEN1 is essential for prolifera- tion and cisplatin resistance of lung cancer cells. PMID: 28371273 Our results suggest that functional polymorphism FEN1 rs174538 G>A might affect personal susceptibility to esophageal squamous cell carcinoma . This result provides a solid theoretical foundation for further clinical study using larger sample sizes. PMID: 28319330 FEN1 sculpts DNA with diffusion-limited kinetics to test DNA substrate. This DNA distortion mutually 'locks' protein and DNA conformation and enables substrate verification with extreme precision. PMID: 28230529 Notably, non-small cell lung cancer patients with FEN1-overexpressed cancers were prone to have poor differentiation and poor prognosis. Furthermore, knockdown of FEN1 resulted in G1/S or G2/M phase cell cycle arrest and suppressed in vitro cellular proliferation in NSCLC cancer cells. PMID: 29037854 Data indicate that human cancer-associated genetic alterations in the FEN1 gene can contribute substantially to cancer development. PMID: 27270424 WRN or the Bloom syndrome helicase (BLM) stimulates DNA polymerase delta progression across telomeric G-rich repeats, only WRN promotes sequential strand displacement synthesis and FEN1 cleavage. PMID: 27849570 The FEN1 rs174538 A allele is a protective biomarker for childhood ALL and this association is more significant in males and in patients at onset age of 3.5 years or older. PMID: 26708601 Data indicate that Flap endonuclease 1 (FEN1) single nucleotide polymorphisms and haplotypes are associated with gallbladder cancer risk. PMID: 26668074 the aim of the present study was to determine the role of FEN1 in the chemosensitivity of SGC7901 cells. PMID: 26718738 Binding of DNA to human FEN1 in a bent conformation occurred independently of 5'-flap accommodation and did not require active site metal ions or the presence of conserved active site residues. PMID: 26884332 In this study, we found that cohesion establishment factors, like CHlR1, cooperatively stimulate endonuclease activity of hFen1 in in vivo mimic condition, including replication protein-A-coated DNA and high salt. PMID: 26032365 Under DNA repair conditions, FEN1 efficiently repaired the 5'-phoshotyrosyl bond-containing SSB substrates in the presence of DNA ligase and DNA polymerase. PMID: 26581212 WDR4 regulates FEN1's potential DNA cleavage threat near the site of replication. PMID: 26751069 Patients with expression of both FEN1 and RAD54B were prone to have advanced nodal involvement and significantly poor prognosis. PMID: 26431531 Fen1 significantly stimulated trinucleotide repeats expansion by Pol beta, but not by the related enzyme Pol lambda. PMID: 25687118 YY1 is a transcription repressor of FEN1 regulating FEN1 levels in response to DNA damaging agents. PMID: 25885449 EXO1 and FEN1 cleaved the substrate at the boundary between the single-stranded 5' flap and the duplex, whereas FAN1 incised it three to four nucleotides in the double-stranded region. PMID: 26221031 Rate-determining step of FEN1 reflects a kinetic bias against long flaps and trinucleotide repeat sequences. PMID: 26160176 FEN1 -69G>A and 4150G>T polymorphisms may be associated with cancer susceptibility in Chinese population. PMID: 25154853 Because FEN1 mutations have been identified in human cancers, our findings raise the possibility that unresolved RNA:DNA hybrid structures contribute to the genomic instability associated with cancer PMID: 25922071 A novel method for monitoring functional lesion-specific recruitment of repair proteins in live cells. PMID: 25879709 FEN1 protein expression was evaluated in 568 oestrogen receptor (ER) negative breast cancers, 894 ER positive breast cancers and 156 ovarian epithelial cancers. FEN1 is a promising biomarker in breast and ovarian epithelial cancer. PMID: 24880630 The FEN1 E359K germline mutation disrupts the FEN1-WRN interaction and FEN1 GEN activity, causing aneuploidy-associated cancers. PMID: 24608430 the mutations of the FEN1 gene maybe a rare event in the development of hepatocellular carcinomas in Korean population PMID: 24164220 FEN1 SNPs and haplotypes were significantly associated with breast cancer risk. The risk alleles showed decreased FEN1 mRNA expression in breast tissues. PMID: 24440783 The homotrimeric proliferating cell nuclear antigen protein (PCNA) coordinates the actions of DNA polymerase, FEN1 and DNA ligase by facilitating the hand-off intermediates between each protein during Okazaki fragment maturation PMID: 22918592 Conserved basic amino acids are not required for double nucleotide unpairing and appear to act cooperatively, whereas the helical cap plays an unexpected role in hFEN1-substrate rearrangement PMID: 24126913 The data provides the first observations of unpaired conformations in DNA substrates bound to hFEN1 in the presence of catalytically inert active-site metal ions and define the role of amino acid residues and divalent metal ion cofactors in this process. PMID: 23975198 A cryptic targeting signal creates a mitochondrial FEN1 isoform with tailed R-Loop binding properties. PMID: 23675412 This study suggested that FEN1 polymorphisms and haplotypes are associated with glioma risk. PMID: 23184144 We identified small-molecule inhibitors of one such target, FEN1, and showed that these compounds were able to selectively kill human cells carrying cancer-relevant mutations. PMID: 23382697 These studies demonstrate a novel role for APC in the suppression of Fen1 activity in the BER pathway PMID: 22787431 Cell-cycle-dependent timing of FEN1 nuclease activity is essential for cell-cycle progression and the maintenance of genome stability. PMID: 22749529 The crystal structure of the complex of importin alpha with a peptide corresponding to the FEN1 nuclear localization sequence was solved. PMID: 22751659 Review: identifies superfamily motifs such as the helical gateway that select for ss-dsDNA junctions and provides key biological insights into FEN1 specificity and regulation. PMID: 22244820 Data show models for the ternary PCNA/FEN1/DNA and Rad9-Rad1-Hus1 (9-1-1 complex)/FEN1/DNA assemblies. PMID: 22586102 Data show that among the 13 SNPs in the 3 genes, only 3 were found to be polymorphic: R196K and K277R in the DFFB gene, and S12L in the EndoG gene, and all 6 SNPs in the FEN-1 gene were entirely monoallelic. PMID: 22011247 FEN1 as an important gene in human gastrointestinal oncogenesis and genetic polymorphisms in FEN1 confer susceptibility to gastrointestinal cancers. PMID: 22072618 Activity of FEN1 endonuclease on nucleosome substrates is dependent upon DNA sequence but not flap orientation. PMID: 21454907 Structural and functional analyses of human FEN1:DNA complexes show structure-specific, sequence-independent recognition for nicked dsDNA bent 100 degrees with unpaired 3' and 5' flaps. PMID: 21496641 these results show that FEN1 and telomerase association occurs throughout the S phase, with the maximum association in the mid S phase. PMID: 21345332 FEN1 10154T variant allele decreases arachidonic acid and arachidonic acid/linoleic acid in the serum phospholipids of carriers of the APOA5-1131C allele PMID: 20802161 the methylated form, but not the phosphorylated form, of FEN1 strongly interacts with proliferating cell nuclear antigen (PCNA), ensuring the 'on' and 'off' timing of its reaction PMID: 20729856 FEN1 and EXO1 can eliminate structures formed by trinucleotide repeats in the course of replication, relying on endonucleolytic and exonucleolytic activities, respectively. PMID: 20643645 FEN1 maintains stable telomeres by facilitating replication through the G-rich lagging strand telomere, thereby ensuring high fidelity telomere replication. PMID: 20551483

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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