Analytical Data
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Gene name
DUT
- Application
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Alternative Names
DUT;Deoxyuridine 5'-triphosphate nucleotidohydrolase. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P33316
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Expression Region
1-252aa
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AA Sequence
MTPLCPRPALCYHFLTSLLRSAMQNARGARQRAEAAVLSGPGPPLGRAAQHGIPRPLSSAGRLSQGCRGASTVGAAGWKGELPKAGGSPAPGPETPAISPSKRARPAEVGGMQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of recombinant proteins, particularly those derived from the DUT (deoxyuridine triphosphate nucleotidohydrolase) enzyme, has gained significant importance in molecular biology and biotechnology. DUT is crucial in nucleotide metabolism, playing a vital role in maintaining dUTP levels within cells, thereby preventing the incorporation of uracil into DNA and preserving genomic integrity. Understanding DUT’s structure and function can provide insights into its role in various cellular processes, including DNA repair and replication. Researchers have focused on the recombinant expression of DUT to study its biochemical properties, regulatory mechanisms, and interactions with other biomolecules. Advances in recombinant DNA technology have enabled the production of large quantities of these proteins, facilitating extensive characterization studies. Additionally, exploring DUT as a potential target for therapeutic interventions in diseases associated with DNA damage and replication errors, such as cancer, highlights the clinical relevance of this research. By employing various expression systems and purification techniques, scientists aim to elucidate the enzymatic activity of DUT, its structural determinants, and its potential as a drug target, contributing to broader efforts in drug discovery and development. The ongoing research endeavors in this area not only enhance our understanding of DUT but also pave the way for novel therapeutic strategies harnessing recombinant proteins.











