| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | yciK |
| Uniprot No | P31808 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-252aa |
| 氨基酸序列 | MHYQPKQDLLNDRIILVTGASDGIGREAAMTYARYGATVILLGRNEEKLRQVASHINEETGRQPQWFILDLLTCTSENCQQLAQRIAVNYPRLDGVLHNAGLLGDVCPMSEQNPQVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAASKFATEGMMQVLADEYQQRLRVNCINPGGTRTAMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTGMTFDAQPGRKPGISQ |
| 预测分子量 | 35.4 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. |
以下是基于常见研究方向构建的关于YciK重组蛋白的示例参考文献(注：文献为模拟示例，建议通过学术数据库检索真实研究)：
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1. **文献名称**: *Characterization of YciK as a metalloprotease in Escherichia coli: Cloning, expression, and enzymatic activity analysis*
**作者**: Smith A, et al.
**摘要**: 本研究报道了yciK基因在大肠杆菌中的重组表达与纯化，证实YciK是一种依赖锌离子的金属蛋白酶，并解析了其底物特异性及最适反应条件，提示其在细菌胞内蛋白降解中的潜在作用。
2. **文献名称**: *Structural insights into the YciK protein from Salmonella typhimurium: Crystallization and X-ray analysis*
**作者**: Tanaka K, et al.
**摘要**: 通过重组表达沙门氏菌YciK蛋白并解析其晶体结构(分辨率2.1 Å)，揭示了其独特的α/β折叠结构及金属结合位点，为理解其催化机制及设计抑制剂奠定基础。
3. **文献名称**: *Functional role of YciK in oxidative stress resistance of Pseudomonas aeruginosa*
**作者**: Lee H, et al.
**摘要**: 本研究利用重组YciK蛋白进行体外实验，发现其通过清除活性氧(ROS)增强铜绿假单胞菌的氧化应激耐受性，表明YciK在细菌环境适应中起关键作用。
4. **文献名称**: *High-yield production of recombinant YciK in Pichia pastoris and its application in industrial biocatalysis*
**作者**: Zhang L, et al.
**摘要**: 报道了在毕赤酵母中高效表达YciK重组蛋白的优化策略，纯化蛋白展示出高效酯酶活性，并验证其在有机合成中催化酯键水解的应用潜力。
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建议通过 **PubMed** 或 **Web of Science** 以“yciK recombinant protein”、“yciK gene function”为关键词检索最新文献。
The yciK gene, primarily studied in *Escherichia coli* and related bacteria, encodes a conserved hypothetical protein with unclear physiological roles. Initially annotated as a putative hydrolase or regulatory factor, YciK has attracted attention due to its widespread presence in Gram-negative bacteria and structural homology to stress-responsive proteins. Its genomic context often places it near genes involved in fatty acid metabolism or redox balance, suggesting potential links to cellular homeostasis.
Recombinant YciK protein production typically involves cloning the yciK gene into expression vectors (e.g., pET or pGEX systems) followed by heterologous expression in *E. coli* hosts. Purification methods commonly employ affinity tags (His-tag, GST) with subsequent chromatography steps. Studies reveal YciK forms homodimers and binds divalent metal ions, hinting at enzymatic or structural functions. Its conserved C-terminal domain shares weak similarity to metallo-β-lactamase superfamily motifs, though direct enzymatic activity remains unconfirmed.
Research focuses on elucidating YciK's role in bacterial stress adaptation. Knockout strains show increased sensitivity to oxidative stressors (e.g., H₂O₂) and membrane-disrupting agents, implying involvement in envelope integrity or detoxification pathways. Structural analyses using recombinant protein have identified potential substrate-binding pockets, yet endogenous ligands remain unknown. Recent interest stems from its upregulation during biofilm formation and antibiotic persistence states, positioning YciK as a potential target for antimicrobial adjuvants. Challenges persist in characterizing its precise biochemical function, driving continued use of recombinant variants for crystallography, interaction studies, and phenotypic complementation assays.
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