| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | cysP |
| Uniprot No | P16700 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-338aa |
| 氨基酸序列 | TELLNSSYDVSRELFAALNPPFEQQWAKDNGGDKLTIKQSHAGSSKQALAILQGLKADVVTYNQVTDVQILHDKGKLIPADWQSRLPNNSSPFYSTMGFLVRKGNPKNIHDWNDLVRSDVKLIFPNPKTSGNARYTYLAAWGAADKADGGDKGKTEQFMTQFLKNVEVFDTGGRGATTTFAERGLGDVLISFESEVNNIRKQYEAQGFEVVIPKTNILAEFPVAWVDKNVQANGTEKAAKAYLNWLYSPQAQTIITDYYYRVNNPEVMDKLKDKFPQTELFRVEDKFGSWPEVMKTHFTSGGELDKLLAAGRN |
| 预测分子量 | 48.0 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cysP重组蛋白的模拟参考文献示例(仅供参考，非真实文献)：
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1. **文献名称**: "Cloning, Expression, and Purification of Recombinant cysP Phosphatase from *E. coli*"
**作者**: Smith A, et al.
**摘要**: 本研究报道了cysP基因在大肠杆菌中的重组表达及纯化。通过构建pET载体系统，利用镍柱亲和层析获得高纯度cysP蛋白，并验证其磷酸酶活性，为后续功能研究奠定基础。
2. **文献名称**: "Structural Insights into cysP Sulfate Transporter by X-ray Crystallography"
**作者**: Zhang L, et al.
**摘要**: 通过X射线晶体学解析了cysP蛋白的3D结构，揭示其硫酸盐结合位点及跨膜转运机制，为理解细菌硫代谢通路提供结构生物学依据。
3. **文献名称**: "Functional Characterization of Recombinant cysP in Antioxidant Defense"
**作者**: Tanaka K, et al.
**摘要**: 实验证明重组cysP蛋白通过调节半胱氨酸生物合成，增强宿主细胞抗氧化应激能力，提示其在氧化应激相关疾病中的潜在应用价值。
4. **文献名称**: "Optimization of cysP Expression in *Pichia pastoris* for Industrial Applications"
**作者**: Müller J, et al.
**摘要**: 在毕赤酵母中优化cysP重组蛋白的高效分泌表达，结合发酵工艺改进，显著提高产量，为大规模生产用于生物技术工业的cysP蛋白提供方案。
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**建议**：实际文献可通过PubMed/Google Scholar检索关键词如“cysP recombinant protein expression”、“cysP phosphatase structure”等获取。注意结合研究领域(如硫酸盐转运或磷酸酶活性)筛选文献。
CysP recombinant protein is a genetically engineered form of the CysP protein, originally identified as a sulfate/thiosulfate-binding component of the sulfate transport system in various bacteria. CysP belongs to the ABC (ATP-binding cassette) transporter family and plays a critical role in sulfur assimilation, a process essential for bacterial survival, particularly under sulfur-limiting conditions. It functions as a periplasmic binding protein that captures extracellular sulfate or thiosulfate ions and delivers them to transmembrane transporters for uptake into the cell. This pathway is vital for synthesizing sulfur-containing biomolecules like cysteine, methionine, and iron-sulfur clusters, which are fundamental for protein structure, redox balance, and metabolic activities.
The recombinant form of CysP is produced using heterologous expression systems, such as *E. coli*, enabling large-scale purification for structural and functional studies. Research on CysP has gained attention due to its potential as a therapeutic target. Pathogenic bacteria, including *Streptococcus pneumoniae* and *Salmonella enterica*, rely on sulfur acquisition during infection, making CysP critical for their virulence and survival in host environments. Inhibiting CysP could disrupt bacterial sulfur metabolism, offering a strategy for novel antimicrobial agents.
Additionally, CysP recombinant protein is utilized in structural biology to elucidate substrate-binding mechanisms and conformational changes during transport. Crystallographic studies have revealed its conserved ligand-binding domains and specificity for sulfur oxyanions. Beyond antimicrobial applications, CysP serves as a model for understanding ABC transporter dynamics and evolutionary adaptations in nutrient uptake systems. Its study also contributes to synthetic biology, where engineered sulfur pathways could optimize industrial microbial production of sulfur-containing compounds. Overall, CysP recombinant protein bridges fundamental microbiology with translational research in drug development and biotechnology.
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