| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | dcyD |
| Uniprot No | P76316 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-328aa |
| 氨基酸序列 | PLHNLTRFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPNAQLEELATRVEAQGFRPYVIPVGGSNALGALGYVESALEIAQQCEGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKELELTASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGGAPALFAYHPHV |
| 预测分子量 | 39.0 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dcyD重组蛋白的3篇代表性文献示例(注：部分信息为模拟概括，具体文献需根据实际数据库检索确认)：
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1. **文献名称**: *Functional Characterization of the dcyD Gene Product in Escherichia coli Cell Division*
**作者**: Tanaka K, et al.
**摘要**: 本研究通过克隆并表达dcyD重组蛋白，证实其参与大肠杆菌细胞分裂的调控。实验表明，dcyD缺失导致细胞分裂异常，重组蛋白的体外纯化进一步揭示其与FtsZ蛋白的相互作用，提示其在分裂环组装中的潜在功能。
2. **文献名称**: *Expression and Purification of Recombinant dcyD Protein for Structural Studies*
**作者**: Müller S, et al.
**摘要**: 报道了一种高效表达和纯化dcyD重组蛋白的方法，采用大肠杆菌表达系统优化条件，获得高纯度蛋白用于结晶分析。初步X射线衍射数据表明dcyD具有独特的α/β折叠结构，为后续功能机制研究奠定基础。
3. **文献名称**: *The Role of dcyD in Bacterial Osmoadaptation: Insights from Recombinant Protein Analysis*
**作者**: Chen L, Wang H.
**摘要**: 通过构建dcyD重组蛋白突变体，研究发现其在渗透压应激响应中调控相容性溶质合成通路的关键作用。酶活实验表明重组dcyD具有依赖于NADPH的脱氢酶活性，可能参与细胞内的氧化还原平衡。
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**注**：以上文献信息为模拟示例，实际研究中建议通过PubMed、Web of Science等数据库以“dcyD recombinant protein”或“dcyD gene function”为关键词检索最新文献。若需具体文献指引，可进一步提供研究方向(如结构、功能或应用)。
**Background of dcyD Recombinant Protein**
The dcyD gene encodes a critical enzyme involved in bacterial cell wall biosynthesis, particularly within the D-alanine metabolism pathway. This pathway is essential for synthesizing peptidoglycan, a key structural component of bacterial cell walls. The dcyD protein, often identified as a D-alanine dehydrogenase or a related enzyme, catalyzes the oxidation of D-alanine to pyruvate and ammonia, contributing to the recycling of D-alanine or its utilization in metabolic processes. Dysregulation of this enzyme can impair cell wall integrity, making it a potential target for antibacterial drug development, especially against pathogens like *Mycobacterium tuberculosis*, where D-cycloserine (a structural analog of D-alanine) is used as a second-line antibiotic.
Recombinant dcyD protein is typically produced using heterologous expression systems, such as *Escherichia coli*, to enable large-scale purification and functional studies. The gene is cloned into expression vectors under inducible promoters, and the resulting protein is often tagged with histidine or other affinity tags for simplified purification via chromatography. Structural and biochemical characterization of recombinant dcyD has provided insights into its catalytic mechanism, substrate specificity, and interaction with inhibitors.
Research on dcyD recombinant protein is particularly relevant in addressing antibiotic resistance. Overexpression or mutations in dcyD have been linked to bacterial resistance against D-cycloserine, highlighting the need to study its structure-activity relationships. Additionally, this protein serves as a tool for screening novel antimicrobial compounds or optimizing existing drugs. Beyond therapeutic applications, studies on dcyD contribute to understanding bacterial physiology and evolution, offering broader implications for microbiology and synthetic biology. Its recombinant form thus bridges fundamental research and translational drug discovery efforts.
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