| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ITPA |
| Uniprot No | Q9BY32 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 3-180aa |
| 氨基酸序列 | ASLVGKKI VFVTGNAKKL EEVVQILGDK FPCTLVAQKI DLPEYQGEPD EISIQKCQEA VRQVQGPVLV EDTCLCFNAL GGLPGPYIKW FLEKLKPEGL HQLLAGFEDK SAYALCTFAL STGDPSQPVR LFRGRTSGRI VAPRGCQDFG WDPCFQPDGY EQTYAEMPKA EKNAVSHRFR |
| 预测分子量 | 21 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于ITPA重组蛋白的3篇参考文献的简要信息：
1. **文献名称**: *"Cloning and Expression of Human Inosine Triphosphate Pyrophosphatase and Characterization of the Recombinant Protein"*
**作者**: Ota, I., et al.
**摘要**: 该研究报道了人源ITPA基因的克隆及其在大肠杆菌中的重组表达。通过酶活性实验，证实重组蛋白具有水解异常核苷酸(如ITP和dITP)的功能，为后续研究ITPA在核苷酸代谢中的作用提供了基础。
2. **文献名称**: *"Functional Analysis of Recombinant ITPA Variants Associated with Neurological Disorders"*
**作者**: Lin, S., et al.
**摘要**: 本文通过体外重组表达ITPA突变体(如p.Pro32Thr和p.Arg178Cys)，发现部分突变导致酶活性和热稳定性显著下降，提示其与婴儿期神经发育障碍的致病机制相关。
3. **文献名称**: *"Crystal Structure of Recombinant Human ITPA and Mechanistic Insights into Substrate Recognition"*
**作者**: Smith, J.L., et al.
**摘要**: 利用X射线晶体学解析了重组人源ITPA的三维结构，揭示了其底物结合口袋的关键氨基酸残基，阐明了ITPA选择性识别ITP/dITP而非ATP的分子机制。
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**备注**：以上文献信息为示例，实际引用时需核实具体文献来源及发表年份。若需扩展，可关注ITPA重组蛋白在药物筛选或基因治疗中的应用研究。
**Background of Recombinant ITPA Protein**
Inosine triphosphatase (ITPA) is a conserved enzyme critical for maintaining nucleotide pool homeostasis by hydrolyzing inosine triphosphate (ITP) and other deaminated purine nucleotides to their monophosphate forms. This activity prevents the incorporation of non-canonical nucleotides into DNA and RNA, thereby safeguarding genomic stability and ensuring accurate nucleic acid synthesis. ITPA deficiency, caused by genetic mutations, is linked to adverse drug responses and diseases. For instance, reduced ITPA activity correlates with hemolytic anemia in patients treated with thiopurine drugs and increased toxicity from antiviral therapies like ribavirin.
Recombinant ITPA protein, produced via genetic engineering in systems such as *E. coli*, yeast, or mammalian cells, enables detailed study of its enzymatic mechanisms, structure-function relationships, and interactions with substrates or inhibitors. Its production involves cloning the *ITPA* gene into expression vectors, followed by purification using affinity chromatography. Researchers employ recombinant ITPA to investigate its role in nucleotide metabolism, DNA repair, and disease pathogenesis. It also serves as a tool for diagnostic assays, predicting patient susceptibility to drug-induced toxicity, and guiding personalized treatment strategies. Structural analyses (e.g., X-ray crystallography) of recombinant ITPA have revealed key residues involved in substrate binding and catalysis, offering insights for therapeutic targeting. Overall, recombinant ITPA is vital for advancing both basic research and clinical applications in pharmacogenomics and molecular medicine.
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