NUDT10 Human

NUDT10 is a single, non-glycosylated polypeptide chain containing 172 amino acids, with a molecular mass of approximately 19.5 kDa . It is produced in E. coli and is fused to an 8 amino acid His-tag at the C-terminus, which facilitates its purification through chromatographic techniques .

The primary function of NUDT10 is to hydrolyze diphosphoinositol polyphosphates, which are involved in various cellular processes including signal transduction, energy metabolism, and apoptosis. Specifically, NUDT10 acts as a diphosphoinositol polyphosphate phosphohydrolase (DIPP), breaking down these complex molecules into simpler forms that the cell can utilize or regulate more easily.

Recombinant NUDT10 is typically produced using bacterial expression systems, such as E. coli. The protein is expressed, harvested, and purified using affinity chromatography, leveraging the His-tag for efficient isolation . The purified protein is then formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 20% glycerol, 0.1M NaCl, and 1mM DTT to maintain its stability and activity .

For storage, NUDT10 is kept at temperatures below -18°C to prevent degradation and maintain its functional integrity. It is important to avoid freeze-thaw cycles, as these can lead to protein denaturation and loss of activity .

NUDT10 is widely used in biochemical and cellular research to study the metabolism and regulation of diphosphoinositol polyphosphates. By understanding how NUDT10 and related enzymes function, researchers can gain insights into the broader roles of these molecules in cellular physiology and pathology. This knowledge can potentially lead to the development of new therapeutic strategies for diseases where diphosphoinositol polyphosphate metabolism is disrupted.