TREX2 Human

TREX2 is a 3’-5’ exonuclease, meaning it degrades DNA from the 3’ end towards the 5’ end. This activity is essential for removing mismatched, modified, fragmented, and normal nucleotides, thereby producing the appropriate 3’ termini for subsequent steps in DNA metabolic pathways . TREX2 is involved in several critical cellular processes, including DNA replication, repair, and recombination .

The human recombinant form of TREX2 is typically expressed in E. coli. The recombinant protein is a single, non-glycosylated polypeptide chain containing 256 amino acids and has a molecular mass of approximately 28.0 kDa . It is often fused to a 20 amino acid His-tag at the N-terminus to facilitate purification using chromatographic techniques .

The TREX2 protein solution is formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 200mM NaCl, 5mM DTT, and 30% glycerol . The protein is highly pure, with a purity greater than 95% as determined by SDS-PAGE . For storage, it is recommended to keep the protein at -20°C for long-term stability, and to avoid multiple freeze-thaw cycles .

TREX2 plays a pivotal role in DNA repair mechanisms. By eliminating mismatched and damaged nucleotides, it helps maintain genomic stability and prevents mutations that could lead to diseases such as cancer . The enzyme’s activity is crucial for the proper functioning of DNA replication and recombination processes, ensuring the fidelity of genetic information passed on during cell division .

Due to its critical role in DNA repair, TREX2 is a subject of extensive research. Understanding its function and regulation can provide insights into the mechanisms of genomic maintenance and the development of therapeutic strategies for diseases associated with DNA repair defects. Recombinant TREX2 is used in various biochemical assays and research studies to investigate its enzymatic properties and interactions with other proteins involved in DNA metabolism .