| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | uox |
| Uniprot No | P25688 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-303aa |
| 氨基酸序列 | AHYHDNYGKNDEVEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLRSKKDYLHGDNSDIIPTDTIKNTVHVLAKLRGIRNIETFAMNICEHFLSSFNHVTRAHVYVEEVPWKRFEKNGIKHVHAFIHTPTGTHFCEVEQMRNGPPVIHSGIKDLKVLKTTQSGFEGFLKDQFTTLPEVKDRCFATQVYCKWRYQRRDVDFEAIWGAVRDIVLQKFAGPYDKGEYSPSVQKTLYDIQVLSLSQLPEIEDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGKITGTVKRKLPSRL |
| 预测分子量 | 41.8 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. |
以下是关于重组尿酸氧化酶(UOX)的3篇代表性文献示例(仅供参考，建议通过学术数据库核实完整信息)：
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1. **标题**: *"Recombinant Urate Oxidase (Rasburicase) for the Management of Hyperuricemia in Patients with Hematologic Malignancies"*
**作者**: Pui CH, et al.
**摘要**: 该研究评估了重组尿酸氧化酶(rasburicase)在血液肿瘤患者中的疗效，证明其能快速降低血清尿酸水平，预防肿瘤溶解综合征(TLS)相关肾损伤，比传统别嘌呤醇更有效。
2. **标题**: *"Expression and Characterization of Recombinant Candida utilis Urate Oxidase in Pichia pastoris"*
**作者**: Zhang Y, et al.
**摘要**: 研究通过毕赤酵母表达系统高效生产来源于假丝酵母的重组UOX，优化发酵条件后酶活性显著提高，为大规模生产提供可行方案，并验证其体外催化尿酸降解的能力。
3. **标题**: *"Comparative Stability of Recombinant Urate Oxidases from Different Species"*
**作者**: Legoux R, et al.
**摘要**: 比较了猪、灵杆菌等不同来源的重组UOX的热稳定性和pH耐受性，发现灵杆菌来源的酶在生理环境下稳定性更佳，为药物开发中的酶源选择提供依据。
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**提示**：实际文献可通过PubMed、Google Scholar等平台，以关键词“recombinant urate oxidase”、“rasburicase”、“UOX expression”检索，并优先选择高被引或近五年研究。
Urate oxidase (UOX), also known as uricase, is a peroxisomal enzyme that catalyzes the oxidation of uric acid into allantoin, a more water-soluble compound easily excreted by the kidneys. While present in most mammals, humans and higher primates lack functional UOX due to evolutionary mutations, making them susceptible to hyperuricemia—a condition linked to gout, kidney stones, and tumor lysis syndrome. This biological gap spurred interest in recombinant UOX as a therapeutic agent.
Recombinant UOX proteins are produced using genetic engineering techniques, typically by expressing the enzyme in microbial systems like *E. coli* or yeast. The first FDA-approved recombinant UOX, rasburicase (derived from *Aspergillus flavus*), revolutionized the management of hyperuricemia in chemotherapy patients by rapidly reducing serum uric acid levels. However, its immunogenicity and short half-life limited long-term use. To address this, pegylated versions (e.g., pegloticase) were developed, enhancing stability and reducing immune reactions.
Beyond clinical applications, UOX serves as a model protein for studying enzyme kinetics, stability, and protein engineering. Its role in purine metabolism pathways also makes it valuable for biochemical research and industrial processes, such as尿酸检测试剂盒. Ongoing research focuses on optimizing expression systems, improving catalytic efficiency, and exploring novel formulations for chronic gout therapy. Despite challenges like antigenicity, recombinant UOX remains a cornerstone in both therapeutic and biotechnological fields, bridging a critical metabolic deficiency in humans.
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