| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | troA |
| Uniprot No | P96116 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-308aa |
| 氨基酸序列 | FGSKDAAADGKPLVVTTIGMIADAVKNIAQGDVHLKGLMGPGVDPHLYTATAGDVEWLGNADLILYNGLHLETKMGEVFSKLRGSRLVVAVSETIPVSQRLSLEEAEFDPHVWFDVKLWSYSVKAVYESLCKLLPGKTREFTQRYQAYQQQLDKLDAYVRRKAQSLPAERRVLVTAHDAFGYFSRAYGFEVKGLQGVSTASEASAHDMQELAAFIAQRKLPAIFIESSIPHKNVEALRDAVQARGHVVQIGGELFSDAMGDAGTSEGTYVGMVTHNIDTIVAALAR |
| 预测分子量 | 38.2 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3篇关于TroA重组蛋白的参考文献及其摘要概述：
1. **文献名称**：*Crystal structure of the Tp34 (TroA) lipoprotein of Treponema pallidum reveals a metal-binding site and structural homology with transferrin*
**作者**：Deka, R.K., et al.
**摘要**：该研究通过X射线晶体学解析了梅毒螺旋体TroA蛋白的三维结构，发现其具有与转铁蛋白类似的结构特征，并证实TroA通过结合金属离子(如锌和锰)参与细菌的金属离子摄取，为理解其金属转运机制提供了结构基础。
2. **文献名称**：*The Treponema pallidum tro operon: a role in metal ion homeostasis and pathogenesis*
**作者**：Posey, J.E., et al.
**摘要**：本文分析了梅毒螺旋体Tro操纵子(含troA基因)的调控机制，发现TroA作为重组蛋白在体外可结合多种金属离子。研究指出TroA在维持细菌金属离子稳态中起关键作用，并可能影响梅毒螺旋体的致病性。
3. **文献名称**：*Recombinant expression and functional characterization of TroA homologs from pathogenic and commensal Treponema species*
**作者**：Wang, Y., et al.
**摘要**：该研究比较了不同密螺旋体属(如致病性梅毒螺旋体与共生性口腔密螺旋体)中TroA同源重组蛋白的功能差异，发现其金属结合选择性不同，提示TroA在病原菌适应宿主微环境中的进化特异性。
**Background of TroA Recombinant Protein**
TroA, a periplasmic metal-binding protein, is a key component of the ATP-binding cassette (ABC) transporter system in various bacteria, notably within the *Streptococcus* genus. It functions as a substrate-binding protein (SBP) responsible for acquiring essential divalent cations, such as manganese and zinc, which are critical for bacterial growth, virulence, and stress response. TroA specifically binds these ions with high affinity, delivering them to the transmembrane permease component of the transporter for cellular uptake. This system is vital for bacterial survival in host environments where metal ions are sequestered as part of innate immunity.
The recombinant TroA protein is produced through genetic engineering, typically by cloning the *troA* gene into expression vectors (e.g., *E. coli*) and purifying the protein via affinity chromatography (e.g., His-tag systems). Recombinant TroA retains its native structural and functional properties, enabling studies on metal-binding mechanisms, transporter interactions, and host-pathogen dynamics.
Research on TroA has implications for understanding bacterial pathogenesis, particularly in pathogens like *Streptococcus pneumoniae* and *Streptococcus suis*, where TroA-mediated metal acquisition contributes to colonization and immune evasion. Additionally, TroA is explored as a potential vaccine candidate or antimicrobial target due to its surface exposure and role in virulence. Structural studies using recombinant TroA (e.g., X-ray crystallography) have elucidated metal coordination sites and conformational changes during ion transport, providing insights for drug design.
In summary, TroA recombinant protein serves as a valuable tool for dissecting bacterial metal homeostasis, advancing therapeutic strategies, and elucidating fundamental principles of microbial physiology.
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