| 纯度 | >90%SDS-PAGE. |
| 种属 | Bacillus |
| 靶点 | tcyA |
| Uniprot No | P42199 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-268aa |
| 氨基酸序列 | CGAGNDNQSKDNAKDGDLWASIKKKGVLTVGTEGTYEPFTYHDKDTDKLTGYDVEVITEVAKRLGLKVDFKETQWDSMFAGLNSKRFDVVANQVGKTDREDKYDFSDKYTTSRAVVVTKKDNNDIKSEADVKGKTSAQSLTSNYNKLATNAGAKVEGVEGMAQALQMIQQGRVDMTYNDKLAVLNYLKTSGNKNVKIAFETGEPQSTYFTFRKGSGEVVDQVNKALKEMKEDGTLSKISKKWFGEDVSK |
| 预测分子量 | 29.6 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tcyA重组蛋白的3篇参考文献，信息整理自相关研究领域：
1. **标题**：Functional characterization of the Staphylococcus aureus cysteine transporter TcyA
**作者**：J. M. Fessler, et al.
**摘要**：研究利用重组表达的TcyA蛋白分析其在金黄色葡萄球菌中的半胱氨酸转运功能，证实其依赖ATP的转运机制及在细菌硫代谢中的关键作用。
2. **标题**：Expression and purification of recombinant TcyA protein from Escherichia coli for structural studies
**作者**：K. L. Anderson & R. G. Brennan
**摘要**：报道了在大肠杆菌中高效表达并纯化TcyA重组蛋白的方法，通过X射线晶体学解析其三维结构，揭示了底物结合域特征。
3. **标题**：Role of the tcyABC operon in Staphylococcus aureus virulence and antibiotic resistance
**作者**：S. P. Nair, et al.
**摘要**：通过构建tcyA基因缺失突变体，结合重组蛋白回补实验，证明TcyA通过调控半胱氨酸摄取影响细菌生物膜形成及甲氧西林耐药性。
注：以上文献为领域代表性方向模拟，具体研究请以实际发表的论文为准。建议在PubMed或Web of Science中以“tcyA recombinant protein”“Staphylococcus aureus cysteine transporter”为关键词检索最新文献。
**Background of TcyA Recombinant Protein**
TcyA is a bacterial L-cysteine transporter belonging to the ATP-binding cassette (ABC) transporter superfamily, which plays a critical role in nutrient uptake and cellular homeostasis. Initially identified in *Bacillus subtilis* and other Gram-positive bacteria, TcyA is part of the TcyABC system, responsible for high-affinity cysteine uptake. Its function is tightly linked to sulfur metabolism, supporting bacterial survival under sulfur-limited conditions. Structural studies reveal that TcyA contains transmembrane domains for substrate recognition and cytoplasmic ATP-binding domains to energize transport.
Recombinant TcyA protein is produced using heterologous expression systems (e.g., *E. coli* or yeast) to enable large-scale purification and functional characterization. The recombinant form retains native structural and transport properties, making it a valuable tool for studying substrate specificity, transport mechanisms, and interactions with regulatory proteins. Researchers employ techniques like site-directed mutagenesis, cryo-EM, or X-ray crystallography to dissect its molecular architecture.
Interest in TcyA stems from its potential applications in antimicrobial development, as cysteine transport is vital for bacterial pathogenesis. Inhibiting TcyA could disrupt pathogen viability, offering a novel therapeutic strategy. Additionally, engineered TcyA variants are explored in biotechnology for biosensing or sulfur-containing compound production. Challenges include optimizing recombinant expression for solubility and stability, as well as elucidating its regulation in diverse bacterial species. Current research focuses on structure-function relationships, inhibitor screening, and ecological roles in microbial communities.
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