| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | pyrG |
| Uniprot No | P65925 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-267aa |
| 氨基酸序列 | MTKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINIDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFIDINLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITDALKEKIKRAASTTDSDVIITEVGGTVGDIESLPFLEALRQMKADVGSENVMYIHTTLLPYLKAAGEMKTKPTQHSVKELRGLGIQPNMLVIRTEEPVEQGIKNKLAQFCDVNSEAVIESRDVEHLYQIPLNLQAQSMDQIVCDHLKL |
| 预测分子量 | 49.6 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pyrG重组蛋白的3篇参考文献概览：
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1. **文献名称**: *Expression and characterization of recombinant pyrG-encoded CTP synthase from Escherichia coli*
**作者**: Smith, J.R., et al.
**摘要**: 该研究在大肠杆菌中成功表达并纯化了重组pyrG编码的CTP合成酶，通过酶动力学分析揭示了其催化特性及对底物UTP和ATP的依赖性，为后续代谢工程研究奠定基础。
2. **文献名称**: *Crystal structure of pyrG-encoded CTP synthase in complex with substrate analogs*
**作者**: Tanaka, M., et al.
**摘要**: 作者解析了重组pyrG蛋白的X射线晶体结构，揭示了其与UTP和谷氨酰胺结合的活性位点构象，为靶向酶活性调控的抑制剂设计提供了结构依据。
3. **文献名称**: *Metabolic engineering of Aspergillus niger by overexpression of pyrG for enhanced citric acid production*
**作者**: Zhang, L., et al.
**摘要**: 研究通过重组表达黑曲霉pyrG基因，显著提高了胞内CTP水平，进而优化了菌株的嘧啶代谢通量，使柠檬酸产量提升约40%，展示了其在工业发酵中的应用潜力。
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注：以上文献为示例性概括，实际引用需根据具体研究内容检索PubMed、Web of Science等数据库获取。
**Background of pyrG Recombinant Protein**
The *pyrG* gene encodes cytidine triphosphate (CTP) synthase, an essential enzyme in the *de novo* biosynthesis of pyrimidines. This enzyme catalyzes the ATP-dependent conversion of uridine triphosphate (UTP) to CTP, a critical step in nucleotide metabolism. In microorganisms such as bacteria and fungi, *pyrG* is a key metabolic gene, and its deletion often results in auxotrophy for cytidine or uridine, making it a common selectable marker in genetic engineering.
Recombinant pyrG protein is produced through heterologous expression systems, such as *Escherichia coli* or yeast, to study its enzymatic properties, structure, or regulatory mechanisms. Its recombinant form enables precise control over production, purification, and functional analysis, bypassing challenges associated with native expression levels or interference from cellular metabolites.
In biotechnology, pyrG recombinant protein has applications in metabolic engineering, particularly in optimizing nucleotide biosynthesis pathways in industrial strains. For example, in *Bacillus* or *Aspergillus* species, engineered pyrG variants can enhance CTP production or improve strain fitness under nutrient-limited conditions. Additionally, pyrG is utilized as a selection marker in fungal transformation systems, where complementation of a *pyrG* deficiency allows for efficient screening of genetically modified organisms.
Recent studies also explore pyrG's role in microbial stress responses, as CTP levels influence nucleic acid synthesis and membrane lipid homeostasis. Structural analyses of recombinant pyrG have revealed insights into its allosteric regulation, aiding the design of inhibitors for antimicrobial development.
Overall, pyrG recombinant protein serves as a versatile tool in both basic research and applied microbiology, bridging gaps between nucleotide metabolism, genetic engineering, and bioproduction strategies.
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