MGSSHHHHHH SSGLVPRGSH MGSMERIEGA SVGRCAASPY LRPLTLHYRQ NGAQKSWDFM KTHDSVTVLL FNSSRRSLVL VKQFRPAVYA GEVERRFPGS LAAVDQDGPR ELQPALPGSA GVTVELCAGL VDQPGLSLEE VACKEAWEEC GYHLAPSDLR RVATYWSGVG LTGSRQTMFY TEVTDAQRSG PGGGLVEEGE LIEVVHLPLE GAQAFADDPD IPKTLGVIFG VSWFLSQVAP NLDLQ.
Human recombinant NUDT14 is typically produced in Escherichia coli (E. coli) as a non-glycosylated polypeptide chain. The recombinant protein often includes additional tags for purification purposes. For instance, NUDT14 can be expressed as an N-terminal GST-fusion protein or with a His-tag at the N-terminus . The molecular weight of the recombinant NUDT14 protein can vary depending on the tags used, but it generally ranges from 26.5 kDa to 50.9 kDa .
NUDT14 specifically hydrolyzes ADP-ribose to AMP and ribose-5-phosphate. This activity is essential for maintaining cellular homeostasis by regulating the levels of ADP-ribose, which can be a byproduct of various metabolic processes. By controlling ADP-ribose levels, NUDT14 helps prevent the accumulation of potentially toxic intermediates that could disrupt cellular functions.
The activity of NUDT14 is significant in various physiological processes, including:
Recombinant NUDT14 is widely used in research to study its enzymatic properties, substrate specificity, and role in cellular metabolism. It is also utilized in structural biology to understand the molecular mechanisms underlying its function. The availability of recombinant NUDT14 allows for detailed biochemical and biophysical analyses, which can provide insights into its potential as a therapeutic target.
In summary, Nudix Type Motif 14 (Human Recombinant) is a vital enzyme with significant roles in cellular metabolism, DNA repair, and signal transduction. Its recombinant form, produced in E. coli, is a valuable tool for scientific research, enabling a deeper understanding of its functions and potential applications in medicine.