Analytical Data
-
Gene name
FEN1
- Application
-
Alternative Names
FEN1；RAD2;Flap endonuclease 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P39748
-
Expression Region
1-380aa
-
AA Sequence
MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK
-
Molecular Weight
50.0 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
FEN1 (Flap Endonuclease 1) is a vital enzyme involved in the DNA repair and replication processes, primarily responsible for removing RNA primers during DNA synthesis and processing Okazaki fragments on the lagging strand. The study of FEN1 has gained attention due to its critical role in maintaining genomic stability and its implications in various diseases, including cancer. Abnormal FEN1 activity has been linked to heightened susceptibility to malignancies, making it a potential target for therapeutic interventions. Understanding the structure and function of FEN1 is crucial for elucidating its mechanisms in DNA metabolism. Recent advances in recombinant protein technology have enabled the production of FEN1 in various systems, facilitating detailed biochemical and structural studies. Researchers aim to explore FEN1's catalytic mechanisms, substrate interactions, and regulatory pathways by employing techniques such as X-ray crystallography, circular dichroism, and kinetic assays. Insights gained from FEN1 research can contribute to the development of novel cancer therapies and enhance our understanding of DNA repair pathways, underscoring the enzyme's significance in molecular biology and medicine.
