| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | cysK |
| Uniprot No | P0A535 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-310aa |
| 氨基酸序列 | MSIAEDITQLIGRTPLVRLRRVTDGAVADIVAKLEFFNPANSVKDRIGVAMLQAAEQAGLIKPDTIILEPTSGNTGIALAMVCAARGYRCVLTMPETMSLERRMLLRAYGAELILTPGADGMSGAIAKAEELAKTDQRYFVPQQFENPANPAIHRVTTAEEVWRDTDGKVDIVVAGVGTGGTITGVAQVIKERKPSARFVAVEPAASPVLSGGQKGPHPIQGIGAGFVPPVLDQDLVDEIITVGNEDALNVARRLAREEGLLVGISSGAATVAALQVARRPENAGKLIVVVLPDFGERYLSTPLFADVAD |
| 预测分子量 | 40.2 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cysK重组蛋白的3篇文献示例(内容为虚构，仅作参考)：
1. **《重组大肠杆菌中cysK的高效表达及酶学性质分析》**
- 作者：Zhang et al.
- 摘要：研究利用原核表达系统成功表达并纯化了cysK重组蛋白，通过酶活性实验证实其催化半胱氨酸合成的功能，并优化了反应条件。
2. **《Structural insights into the catalytic mechanism of cysK from Salmonella typhimurium》**
- 作者：Wang & Smith
- 摘要：通过X射线晶体学解析了沙门氏菌cysK蛋白的三维结构，揭示了其底物结合位点及催化机制，为抗菌药物设计提供依据。
3. **《Functional characterization of cysK in Pseudomonas aeruginosa biofilm formation》**
- 作者：Lee et al.
- 摘要：发现铜绿假单胞菌中cysK基因缺失导致生物被膜形成能力下降，表明cysK在细菌致病性中的潜在作用。
4. **《A novel purification strategy for recombinant cysK with high stability and activity》**
- 作者：Gupta et al.
- 摘要：开发了一种新型亲和层析法纯化cysK重组蛋白，显著提高了蛋白稳定性和体外半衰期，适用于工业化酶制剂生产。
(注：以上文献为模拟内容，实际引用需查询PubMed、Google Scholar等数据库获取真实文献。)
**Background of cysK Recombinant Protein**
CysK, or cysteine synthase A, is a key enzyme in the cysteine biosynthesis pathway, primarily found in bacteria, plants, and some archaea. It catalyzes the final step of cysteine production by converting *O*-acetyl-L-serine (OAS) and sulfide into L-cysteine, a sulfur-containing amino acid critical for protein synthesis, redox homeostasis, and antioxidant defense. In bacteria, cysteine biosynthesis is essential for survival, particularly under oxidative stress or nutrient-limited conditions, making CysK a potential target for antimicrobial drug development.
Structurally, CysK belongs to the pyridoxal 5'-phosphate (PLP)-dependent enzyme family. It typically functions as a homodimer, with each subunit containing a PLP-binding domain that facilitates the condensation reaction. The enzyme’s activity is tightly regulated; for instance, in *Escherichia coli*, CysK expression is controlled by the cysteine-responsive transcriptional regulator CysB, ensuring metabolic balance.
Recombinant CysK is produced via heterologous expression in bacterial hosts like *E. coli*, enabling large-scale purification for biochemical and structural studies. Researchers often clone the *cysK* gene into expression vectors with affinity tags (e.g., His-tag) to simplify isolation. Studies using recombinant CysK have elucidated its catalytic mechanism, substrate specificity, and interaction with inhibitors.
Beyond basic research, CysK has biotechnological relevance. Its role in cysteine synthesis is leveraged in metabolic engineering to enhance cysteine production in industrial microbes. Additionally, targeting CysK with small-molecule inhibitors is explored as a strategy to combat pathogenic bacteria, including antibiotic-resistant strains. However, challenges remain in achieving selectivity over human homologs, such as cystathionine β-synthase.
Overall, CysK recombinant protein serves as a vital tool for understanding microbial sulfur metabolism and developing antimicrobial agents, bridging fundamental biochemistry with applied biotechnology.
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