| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DPYS |
| Uniprot No | Q14117 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-519aa |
| 氨基酸序列 | MAAPSRLLIR GGRVVNDDFS EVADVLVEDG VVRALGHDLL PPGGAPAGLR VLDAAGKLVL PGGIDTHTHM QFPFMGSRSI DDFHQGTKAA LSGGTTMIID FAIPQKGGSL IEAFETWRSW ADPKVCCDYS LHVAVTWWSD QVKEEMKILV QDKGVNSFKM FMAYKDLYMV TDLELYEAFS RCKEIGAIAQ VHAENGDLIA EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV NCPLYIVHVM SKSAAKVIAD ARRDGKVVYG EPIAASLGTD GTHYWNKEWH HAAHHVMGPP LRPDPSTPDF LMNLLANDDL TTTGTDNCTF NTCQKALGKD DFTKIPNGVN GVEDRMSVIW EKGVHSGKMD ENRFVAVTST NAAKIFNLYP RKGRIAVGSD ADIVIWDPKG TRTISAKTHH QAVNFNIFEG MVCHGVPLVT ISRGKVVYEA GVFSVTAGDG KFIPRKPFAE YIYKRIKQRD RTCTPTPVER APYKGEVATL KSRVTKEDAT AGTRKQAHP |
| 预测分子量 | 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DPYS重组蛋白的3篇文献摘要概述：
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1. **文献名称**: "Molecular cloning and characterization of human dihydropyrimidinase"
**作者**: Jansen, G., et al.
**摘要**: 该研究报道了人类DPYS基因的克隆及其在大肠杆菌中的重组表达。通过纯化重组DPYS蛋白，分析了其催化二氢尿嘧啶水解的酶动力学特性，并探讨了金属离子对酶活性的调控作用。
2. **文献名称**: "Crystal structure of dihydropyrimidinase from Thermus sp. at 1.3 Å resolution"
**作者**: Nishiyama, T., et al.
**摘要**: 研究利用重组DPYS蛋白(来源于嗜热菌)进行结晶和X射线结构解析，揭示了其四聚体结构及活性位点的金属结合特征，为理解DPYS催化机制提供了结构基础。
3. **文献名称**: "Functional analysis of disease-causing mutations in human dihydropyrimidinase"
**作者**: van Kuilenburg, A.B.P., et al.
**摘要**: 通过体外表达携带突变的重组人DPYS蛋白，评估了遗传性DPYS缺陷症相关突变对酶活性和稳定性的影响，发现部分突变导致蛋白错误折叠及催化功能丧失。
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这些文献涵盖了DPYS重组蛋白的基因克隆、结构解析及疾病相关突变的功能研究，均为该领域的代表性工作。
**Background of DPYS Recombinant Protein**
Dihydropyrimidinase (DPYS), also known as dihydropyrimidine amidohydrolase, is a key enzyme in the pyrimidine degradation pathway. It catalyzes the hydrolysis of 5.6-dihydrouracil and 5.6-dihydrothymine into β-ureidopropionate and β-ureidoisobutyrate, respectively, facilitating nitrogen excretion and nucleotide metabolism. Dysfunction in DPYS is linked to the rare autosomal recessive disorder β-ureidopropionase deficiency, characterized by neurological abnormalities and elevated levels of dihydropyrimidines in bodily fluids.
Recombinant DPYS protein is produced using genetic engineering techniques, often expressed in bacterial (e.g., *E. coli*), yeast, or mammalian cell systems. This allows large-scale production of the enzyme for functional and structural studies. Researchers utilize recombinant DPYS to investigate its catalytic mechanisms, substrate specificity, and role in drug metabolism, particularly in the breakdown of chemotherapeutic agents like 5-fluorouracil (5-FU). Variations in DPYS activity can influence drug efficacy and toxicity, making it a focus in pharmacogenomics.
Structural studies of recombinant DPYS have revealed its tetrameric organization and dependence on zinc ions for enzymatic activity. Mutational analyses using recombinant protein have identified residues critical for substrate binding and catalysis, enhancing understanding of genotype-phenotype correlations in genetic disorders. Additionally, recombinant DPYS serves as a tool for developing diagnostic assays and enzyme replacement therapies.
Overall, DPYS recombinant protein bridges biochemical research, clinical diagnostics, and therapeutic innovation, offering insights into metabolic disorders and personalized medicine strategies.
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