NUDT1 Human

NUDT1 hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 8-oxo-dATP, into their corresponding monophosphates. This activity prevents the incorporation of these oxidized nucleotides into DNA, which could otherwise lead to mutations and genomic instability . The enzyme is predominantly found in the cytoplasm, with some presence in the mitochondria, indicating its role in sanitizing nucleotide pools for both nuclear and mitochondrial genomes .

NUDT1 is expressed at higher levels in proliferating cells compared to resting cells, highlighting its importance in rapidly dividing tissues. This differential expression suggests that NUDT1 is particularly crucial in preventing mutagenesis during DNA replication and transcription .

The human recombinant form of NUDT1 is typically produced in Escherichia coli and is a single, non-glycosylated polypeptide chain containing 176 amino acids. It is often fused with a 20 amino acid His tag at the N-terminus to facilitate purification . The enzyme has a molecular mass of approximately 20.1 kDa .

The recombinant NUDT1 is purified using proprietary chromatographic techniques to achieve a purity greater than 95%, as determined by SDS-PAGE . The enzyme is formulated in a solution containing Tris-HCl buffer, glycerol, dithiothreitol (DTT), and sodium chloride (NaCl) to ensure stability and activity .

NUDT1 is widely used in laboratory research to study its role in DNA repair and mutagenesis. Its ability to hydrolyze oxidized nucleotides makes it a valuable tool for understanding the mechanisms of genomic maintenance and the prevention of diseases such as cancer and neurodegeneration .