Technical Data
FEN1, ID (Flap Endonuclease 1, Flap Structure-specific Endonuclease 1, Maturation Factor 1, MF1, DNase IV, hFEN-1, RAD2)
FEN1 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. This 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.

Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilution:
ELISA: 1:1,000
Western Blot: 1:50-1:100
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
200ul-20CBlue IceHumanRabbit
As reported
Synthetic peptide selected from the Center region of human FEN1 (KLH).
Purified by ammonium sulfate precipitation.
Supplied as a liquid in PBS, 0.09% sodium azide.
Recognizes human FEN1.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Hiraoka L.R., Harrington J.J., Gerhard D.S., Genomics 25:220-225(1995). 2. Robins P., Pappin D.J.C., Wood R.D., Lindahl T.J. Biol. Chem. 269:28535-28538(1994). 3. Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A.,J. Biol. Chem. 272:24522-24529(1997).