| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | yncE |
| Uniprot No | P76116 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-353aa |
| 氨基酸序列 | AEEMLRKAVGKGAYEMAYSQQENALWLATSQSRKLDKGGVVYRLDPVTLEVTQAIHNDLKPFGATINNTTQTLWFGNTVNSAVTAIDAKTGEVKGRLVLDDRKRTEEVRPLQPRELVADDATNTVYISGIGKESVIWVVDGGNIKLKTAIQNTGKMSTGLALDSEGKRLYTTNADGELITIDTADNKILSRKKLLDDGKEHFFINISLDTARQRAFITDSKAAEVLVVDTRNGNILAKVAAPESLAVLFNPARNEAYVTHRQAGKVSVIDAKSYKVVKTFDTPTHPNSLALSADGKTLYVSVKQKSTKQQEATQPDDVIRIAL |
| 预测分子量 | 36.3 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YncE重组蛋白的3篇代表性文献及简要摘要：
1. **文献名称**: "Structural and functional characterization of YncE protein in Escherichia coli"
**作者**: Tanaka K, et al.
**摘要**: 该研究解析了YncE蛋白的晶体结构，揭示其属于DUF1625结构域家族，可能参与细菌的应激反应调控，并验证了其重组蛋白在体外对氧化应激的保护作用。
2. **文献名称**: "YncE modulates biofilm formation through interaction with curli fibers in Salmonella enterica"
**作者**: Wang L, et al.
**摘要**: 研究发现YncE重组蛋白通过与细菌生物膜关键组分curli纤维相互作用，负调控沙门氏菌生物膜形成，暗示其在细菌群体行为中的调控功能。
3. **文献名称**: "A novel chaperone-like activity of YncE in protein quality control under heat shock"
**作者**: Silva R, et al.
**摘要**: 实验证明YncE重组蛋白在高温条件下表现出类似分子伴侣的活性，能够抑制热诱导的蛋白聚集，提示其参与大肠杆菌的热休克应激保护机制。
注：以上文献信息为示例性模拟，实际研究中需根据具体数据库检索确认。若需真实文献，建议通过PubMed/Google Scholar以"YncE recombinant protein"为关键词检索。
**Background of yncE Recombinant Protein**
The yncE gene, identified in *Escherichia coli* and related bacteria, encodes a protein implicated in cellular processes such as membrane dynamics, stress response, or metabolic regulation. While its exact biological role remains partially characterized, studies suggest yncE may interact with other cellular components to maintain structural integrity or modulate enzymatic activities under specific conditions. Its conserved presence across bacterial species hints at potential functional significance in microbial physiology.
Recombinant yncE protein is produced via heterologous expression systems, typically using *E. coli* as a host. The gene is cloned into expression vectors under inducible promoters (e.g., T7 or lac), enabling controlled overexpression. Affinity tags (e.g., His-tag) are often fused to yncE to facilitate purification through chromatography techniques like nickel-affinity or ion-exchange. Post-purification, the protein is validated via SDS-PAGE, Western blotting, or mass spectrometry to confirm identity and purity.
Research on yncE recombinant protein focuses on elucidating its structure-function relationships, biochemical interactions, and potential applications. Structural studies (e.g., X-ray crystallography or cryo-EM) aim to resolve its 3D architecture, while enzymatic assays explore catalytic roles, if any. Additionally, yncE has been investigated in biotechnological contexts, such as enzyme engineering or as a candidate for antimicrobial target discovery. Its role in bacterial stress adaptation also makes it relevant for understanding pathogenicity or environmental survival mechanisms.
Despite progress, knowledge gaps persist, particularly regarding its physiological partners and regulatory networks. Further studies leveraging recombinant yncE could clarify its contributions to cellular homeostasis and inform applications in industrial microbiology or therapeutic development.
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