| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | XDH |
| Uniprot No | P47989 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1333aa |
| 氨基酸序列 | MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDRLQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCCMNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQASTLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFGAACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISDLNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSAFKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKEELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLDPTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRYENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDKVTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDLKKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKMLGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGRHPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGRLCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKLEGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGALLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAASVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLGYSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAVGEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVTGVPENCKPWSVRV |
| 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. |
以下为3篇与XDH重组蛋白相关的虚构参考文献示例(仅供格式参考，内容非真实文献)：
1. **文献名称**: "Expression and Purification of Recombinant Xanthine Dehydrogenase in E. coli"
**作者**: Zhang L., et al.
**摘要**: 本研究报道了利用大肠杆菌表达系统高效表达XDH重组蛋白的优化方法，通过His标签纯化获得高活性酶，并验证其在体外催化黄嘌呤转化为尿酸的功能。
2. **文献名称**: "Structural Insights into Human XDH by Cryo-EM Analysis"
**作者**: Tanaka K., et al.
**摘要**: 通过冷冻电镜解析了重组人源XDH蛋白的3.2Å分辨率结构，揭示了其底物结合位点及氧化还原辅酶结合域的特征，为痛风治疗药物设计提供结构基础。
3. **文献名称**: "Role of Recombinant XDH in Hyperuricemia Mouse Models"
**作者**: Wang Y., et al.
**摘要**: 利用重组XDH蛋白构建高尿酸血症小鼠模型，证明XDH过表达导致血清尿酸水平升高，并探讨了其与肾脏损伤的潜在关联。
(注：以上文献信息为模拟生成，实际引用时需查询真实数据库如PubMed、Web of Science等获取。)
Xanthine dehydrogenase (XDH) is a molybdoflavoprotein enzyme that plays a critical role in purine catabolism, catalyzing the oxidation of hypoxanthine to xanthine and xanthine to uric acid. Historically studied for its involvement in gout and oxidative stress-related pathologies, XDH exists in two interconvertible forms: a dehydrogenase (XDH, NAD⁺-dependent) and an oxidase (XO, O₂-dependent) that generates reactive oxygen species. Recombinant XDH technology emerged to overcome challenges in isolating native enzymes, such as low yield and instability. By cloning the XDH gene into expression systems (e.g., E. coli, yeast, or insect cells), researchers produce purified, functional XDH with controlled post-translational modifications. This approach enables scalable production for biomedical and industrial applications, including drug screening, mechanistic studies of hyperuricemia, and biosensor development. Recent advances in structural biology (e.g., cryo-EM) have refined understanding of XDH's catalytic mechanisms and allosteric regulation, driving rational engineering of recombinant variants with enhanced stability or altered substrate specificity. Challenges persist in maintaining enzymatic activity during heterologous expression, particularly in preserving the molybdenum cofactor and iron-sulfur clusters. Recombinant XDH also serves as a tool to study its pathological role in ischemia-reperfusion injury, cancer metastasis, and metabolic disorders, while engineered forms are explored for biocatalytic synthesis of pharmaceuticals. Ongoing research focuses on optimizing expression systems and developing XDH-targeted therapeutics, positioning recombinant XDH as a versatile asset in both basic science and translational medicine.
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