Analytical Data
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Gene name
Flap endonuclease 1/FEN-1
- Application
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Alternative Names
MF1; RAD2; Maturation Factor-1; DNase IV
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P39748
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Expression Region
Met1~Thr195
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Molecular Weight
26kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Flap endonuclease 1 (FEN-1) is a crucial enzyme involved in DNA replication and repair processes. It plays a significant role in the maturation of Okazaki fragments during lagging strand synthesis, where it removes RNA primers and any flap structures generated during DNA synthesis. FEN-1 is a multifunctional protein that also participates in mechanisms like DNA damage response and the maintenance of genomic stability. Dysregulation or mutations in the FEN-1 gene have been implicated in various diseases, including cancer, making it a potential target for therapeutic interventions. The study of recombinant FEN-1 is essential for understanding its enzymatic mechanisms, interaction partners, and regulatory pathways. It also offers insights into its structural properties, which are vital for developing inhibitors that could be used in clinical applications. Through biochemical assays and structural biology techniques, researchers are investigating how FEN-1's activity is modulated by different cofactors and how it coordinates its functions with other proteins in the DNA damage repair pathways. Overall, understanding FEN-1 at the molecular level may contribute to the development of novel strategies for cancer therapy and the enhancement of genome integrity.
