Analytical Data
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基因名
dUTPase/DUT
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简介
Deoxyuridine 5'-triphosphate nucleotidohydrolase (DUT) is an essential enzyme of nucleotide metabolism, as DUT hydrolyzes dUTP to dUMP and pyrophosphate, preventing uracil misincorporation into DNA efficiently and provides dUMP for thymidylate biosynthesis. DUT also prevents dimerization of PPAR and retinoid X receptor and is essential for embryonic development as well. dUTPase/DUT Protein, Human is the recombinant human-derived dUTPase/DUT protein, expressed by E. coli , with tag free.
- Application
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别名
rHuDeoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial/DUT; Deoxyuridine 5'-Triphosphate Nucleotidohydrolase Mitochondrial; dUTPase; dUTP Pyrophosphatase; DUT
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种属
Human
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表达系统
E. coli
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P33316-2
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表达区间
M1-N164
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蛋白长度
Full Length of Isoform-2
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分子量
18.0 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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Protein Description
dUTPase (deoxyuridine triphosphate nucleotidohydrolase), an essential enzyme, plays a critical role in maintaining DNA integrity by preventing the incorporation of uracil into DNA during replication. It catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate, thus regulating the intracellular levels of dUTP and fostering a balanced nucleotide pool essential for accurate DNA synthesis. Abnormal dUTPase activity has been linked to various diseases, including cancer, highlighting its potential as a therapeutic target. Moreover, understanding the structure and function of dUTPase is instrumental in deciphering its mechanisms and interactions within cellular pathways. Research on recombinant dUTPase/DUT proteins has gained momentum, utilizing techniques such as protein expression in bacterial systems, purification methods, and functional assays to elucidate its biochemical properties and interaction with other cellular components. Such studies not only advance our comprehension of nucleotide metabolism but also pave the way for the development of novel inhibitors that might serve as lead compounds in drug design. Integrating structural biology approaches, including X-ray crystallography and cryo-electron microscopy, complements these efforts, offering insights into the enzyme's active site and substrate binding. As a result, dUTPase continues to be a focal point in molecular biology, pharmacology, and biotechnology research, with implications spanning from basic science to clinical applications.
