Recombinant protein of human f

gene_symbol：FEN1
Description：Recombinant protein of human flap structure-specific endonuclease 1 (FEN1), 20 µg
Accn：NM_004111
Unipro ID：P39748
Synonyms：FEN-1; MF1; RAD2
Species：Human
Amount：20 ug
Delivery time：4周
Expression sequence：>RC201785 protein sequence Red=Cloning site Green=Tags(s) MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYR TIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDE CKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLS RILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAH QLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSL SSAKRKEPEPKGSTKKKAKTGAAGKFKRGK TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tags：C-Myc/DDK
PredictedMW：42.4 kDa
Buffer：25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
Stability：Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
Bioactivity
Purity：> 80% as determined by SDS-PAGE and Coomassie blue staining
Concentration：>0.05 µg/µL as determined by microplate BCA method
Preparation：Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps.
Endotoxin
Shipping
Background：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]