FEN1 Human

Flap Structure-Specific Endonuclease 1 Human Recombinant

Cat. No.

BT16013

Source

Escherichia Coli.

Synonyms

FEN-1, MF1, RAD2, Maturation Factor-1, MF-1, Flap endonuclease 1, Flap structure-specific endonuclease 1, Maturation factor 1, hFEN-1, DNase IV, FEN1.

Appearance

Sterile filtered colorless solution.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

FEN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-380 a.a.) and having a molecular mass of 42.5 kDa. The FEN1 protein is purified by standard chromatogrpahy techniques.

Product Specs

Introduction

FEN1, a crucial enzyme in DNA replication and repair, plays a vital role in removing 5' overhanging flaps during DNA repair processes and Okazaki fragment processing in lagging strand DNA synthesis. Its interaction with AP endonuclease 1 during long-patch base excision repair facilitates coordinated protein loading onto the substrate, enabling efficient substrate transfer between the enzymes. As a member of the XPG/RAD2 endonuclease family, FEN1 is one of ten essential proteins required for cell-free DNA replication. Notably, DNA secondary structures can hinder FEN1's flap processing activity at specific trinucleotide repeats. This inhibition stems from the concealment of the 5' flap end, essential for FEN1 binding and cleavage. Consequently, such secondary structures can compromise FEN1's protective function, potentially leading to site-specific trinucleotide expansions.

Description

Recombinant Human FEN1, expressed in E. coli, is a purified, non-glycosylated polypeptide chain consisting of 380 amino acids (1-380 a.a.). With a molecular weight of 42.5 kDa, this protein is purified using standardized chromatography techniques.

Physical Appearance

A clear, colorless solution that has been sterilized by filtration.

Formulation

This protein solution is supplied in a buffer containing 20mM Tris-HCl at pH 8.0, 1mM DTT, and 10% glycerol.

Stability

For short-term storage (2-4 weeks), keep the vial refrigerated at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein like 0.1% HSA or BSA is recommended for long-term storage. Avoid repeated freeze-thaw cycles.

Purity

SDS-PAGE analysis indicates a purity greater than 90.0%.

Synonyms

FEN-1, MF1, RAD2, Maturation Factor-1, MF-1, Flap endonuclease 1, Flap structure-specific endonuclease 1, Maturation factor 1, hFEN-1, DNase IV, FEN1.

Source

Escherichia Coli.

Amino Acid Sequence

MGIQGLAKLI ADVAPSAIRE NDIKSYFGRK VAIDASMSIY QFLIAVRQGG DVLQNEEGET TSHLMGMFYR TIRMMENGIK PVYVFDGKPP QLKSGELAKR SERRAEAEKQ LQQAQAAGAE QEVEKFTKRL VKVTKQHNDE CKHLLSLMGI PYLDAPSEAE ASCAALVKAG KVYAAATEDM DCLTFGSPVL MRHLTASEAK KLPIQEFHLS RILQELGLNQ EQFVDLCILL GSDYCESIRG IGPKRAVDLI QKHKSIEEIV RRLDPNKYPV PENWLHKEAH QLFLEPEVLD PESVELKWSE PNEEELIKFM CGEKQFSEER IRSGVKRLSK SRQGSTQGRL DDFFKVTGSL SSAKRKEPEP KGSTKKKAKT GAAGKFKRGK.

Product Science Overview

Introduction

Flap Structure-Specific Endonuclease 1 (FEN1) is a crucial enzyme in DNA replication and repair processes. It is a member of the XPG/RAD2 endonuclease family and is essential for maintaining genomic stability. FEN1 is known for its ability to remove 5’ overhanging flaps in DNA, which are short sections of single-stranded DNA that “hang off” due to their nucleotide bases being prevented from binding to their complementary base pair. This enzyme plays a significant role in processing the 5’ ends of Okazaki fragments during lagging strand DNA synthesis.

Function and Mechanism

FEN1’s primary function is to ensure the accurate and efficient replication of DNA. During DNA replication, the lagging strand is synthesized in short fragments known as Okazaki fragments. These fragments have 5’ overhanging flaps that need to be removed for the fragments to be joined together seamlessly. FEN1 recognizes and cleaves these flaps, allowing the DNA fragments to be properly ligated.

In addition to its role in DNA replication, FEN1 is also involved in DNA repair processes. It participates in long-patch base excision repair, where it interacts with AP endonuclease 1 to coordinate the loading of proteins onto the DNA substrate. This interaction ensures the efficient repair of damaged DNA and maintains genomic integrity.

Overexpression and Cancer

FEN1 is overexpressed in various types of cancers, including breast, prostate, stomach, neuroblastomas, pancreatic, and lung cancers. Overexpression of FEN1 can lead to the activation of the microhomology-mediated end joining (MMEJ) pathway, an inaccurate DNA repair pathway that often results in mutations. This mutagenic pathway can contribute to the development and progression of cancer.

Recombinant Human FEN1

Recombinant human FEN1 is a laboratory-produced version of the enzyme, used for research and therapeutic purposes. It is produced using recombinant DNA technology, which involves inserting the FEN1 gene into a suitable expression system, such as bacteria or yeast, to produce the enzyme in large quantities. This recombinant enzyme is used in various studies to understand its function, mechanism, and potential therapeutic applications.

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FEN1 Human

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