| 纯度 | >90%SDS-PAGE. |
| 种属 | E. coli |
| 靶点 | cysH |
| Uniprot No | P17854 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-244aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSKLDLNALNELPKVDRILALAETNAELEK LDAEGRVAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIRPDIPVILTDTG YLFPETYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGVEGIEK YNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQRGVFKVL PIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWEPGMAEEET RFFGLKRECGLHEG |
| 预测分子量 | 30 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3篇关于CysH重组蛋白研究的参考文献概述：
1. **《Cloning, expression and characterization of the cysH gene of Mycobacterium tuberculosis》**
- 作者：Williams, S.J. et al.
- 摘要：研究克隆并在大肠杆菌中表达了结核分枝杆菌CysH蛋白(磷酸腺苷磷酸硫酸还原酶)，分析了其酶活性及在硫代谢中的作用，为抗结核药物靶点研究提供基础。
2. **《Structural and functional analysis of the APS reductase from Arabidopsis thaliana》**
- 作者：Gutierrez-Marcos, J.F. et al.
- 摘要：解析拟南芥CysH同源蛋白的晶体结构，揭示其催化机制及辅因子结合位点，探讨其在植物硫同化途径中的功能。
3. **《Heterologous expression and purification of functional CysH enzyme from Pseudomonas aeruginosa》**
- 作者：Li, H. & Wang, Q.
- 摘要：报道铜绿假单胞菌CysH蛋白在毕赤酵母系统中的重组表达与纯化，验证其还原酶活性，并评估其在细菌抗氧化胁迫中的潜在作用。
注：以上文献名为示例性概括，实际研究需通过学术数据库(如PubMed/Web of Science)检索具体文章。
**Background of cysH Recombinant Protein**
The *cysH* gene encodes adenosine 5'-phosphosulfate reductase (APSR), a key enzyme in the sulfate assimilation pathway responsible for reducing adenosine 5'-phosphosulfate (APS) to sulfite. This reaction is critical for the biosynthesis of sulfur-containing compounds, such as cysteine, methionine, and iron-sulfur clusters, which are essential for cellular metabolism, redox balance, and protein function. The *cysH*-encoded APS reductase is conserved across bacteria, plants, and some archaea, playing a central role in assimilatory sulfate reduction. In pathogenic microorganisms, this enzyme is often linked to virulence and survival under sulfur-limited host environments, making it a potential target for antimicrobial drug development.
Recombinant cysH protein is produced through heterologous expression systems, such as *Escherichia coli* or yeast, enabling large-scale purification for functional and structural studies. Its recombinant form facilitates biochemical characterization, including substrate specificity, catalytic mechanisms, and inhibitor screening. Additionally, structural analyses (e.g., X-ray crystallography or cryo-EM) of the recombinant protein provide insights into active-site architecture and regulatory domains, aiding in rational drug design.
Research on cysH recombinant protein has applications in biotechnology and medicine. For instance, engineered APS reductases with enhanced activity could improve sulfur metabolism in industrial microbial strains for biofuel or amino acid production. In antimicrobial research, inhibitors targeting cysH could disrupt pathogen sulfur metabolism, offering novel therapeutic strategies. Furthermore, studies on plant APS reductase variants may contribute to developing crops with optimized sulfur utilization, enhancing stress resilience or nutrient efficiency. Overall, cysH recombinant protein serves as a versatile tool for advancing both basic science and applied biotechnologies.
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