| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Cps1 |
| Uniprot No | P31327 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1400-1500aa |
| 氨基酸序列 | ANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDN YVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKA A |
| 预测分子量 | 37 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CPS1重组蛋白的3篇代表性文献摘要示例(注：文献信息为虚构，仅供格式参考)：
1. **文献名称**: *Heterologous Expression and Purification of Functional Carbamoyl Phosphate Synthetase 1 (CPS1) in E. coli*
**作者**: Noguchi T. et al.
**摘要**: 本研究成功在大肠杆菌中表达了重组人源CPS1蛋白，并通过优化诱导条件和纯化步骤获得高活性酶。重组CPS1在体外尿素合成体系中表现出与天然酶相似的动力学特性，为后续代谢疾病研究提供工具。
2. **文献名称**: *Structural Insights into CPS1 Deficiency Mutations via Recombinant Protein Analysis*
**作者**: Ahmed S. et al.
**摘要**: 通过构建CPS1常见致病突变体的重组蛋白，发现R453W突变导致酶活性显著下降，并利用晶体学分析揭示其破坏ATP结合域结构的分子机制，为遗传性尿素循环障碍提供病理依据。
3. **文献名称**: *Mammalian Cell-Expressed Recombinant CPS1 Corrects Metabolic Dysfunction in a Mouse Model*
**作者**: Habib R. et al.
**摘要**: 在HEK293细胞中表达并纯化具有正确翻译后修饰的重组CPS1.通过小鼠模型验证其可有效恢复尿素循环功能，降低血氨水平，证明其在酶替代疗法中的潜在应用价值。
(注：以上文献及作者为模拟内容，实际引用请通过PubMed或学术数据库检索。)
Carbamoyl phosphate synthetase 1 (CPS1) is a mitochondrial enzyme critical to the urea cycle, the primary metabolic pathway for detoxifying ammonia in humans. As the first and rate-limiting enzyme in this cycle, CPS1 catalyzes the ATP-dependent conversion of ammonia, bicarbonate, and glutamine into carbamoyl phosphate. This reaction is essential for nitrogen disposal, with deficiencies in CPS1 activity leading to hyperammonemia, a life-threatening condition characterized by toxic ammonia accumulation, particularly in newborns.
The CPS1 protein consists of two major domains: a glutaminase domain for ammonia generation and a synthetase domain for carbamoyl phosphate production. Its activity depends on the allosteric activator N-acetylglutamate (NAG), linking urea cycle function to cellular energy status. Genetic mutations in CPS1 are associated with rare autosomal recessive disorders, driving interest in recombinant CPS1 protein for research and therapeutic development.
Recombinant CPS1 is produced using expression systems like bacterial (E. coli) or mammalian cell cultures, though challenges persist due to its large size (~1.500 amino acids) and mitochondrial localization requirements. Researchers employ this engineered protein to study enzyme kinetics, mutation effects, and potential gene therapies. Recent applications extend beyond urea cycle research, including investigations into CPS1's role as a metabolic biomarker in liver diseases and cancers, where altered expression correlates with disease progression.
Current efforts focus on improving recombinant CPS1 stability and delivery for enzyme replacement strategies, while structural studies using the recombinant protein aim to identify drug targets for ammonia metabolism disorders. Its dual role in nitrogen metabolism and cellular energy regulation continues to make CPS1 a focal point in both clinical biochemistry and molecular medicine research.
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