| 纯度 | >90%SDS-PAGE. |
| 种属 | Moraxella bovis |
| 靶点 | tfpQ |
| Uniprot No | P07640 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 7-157aa |
| 氨基酸序列 | FTLIELMIVIAIIGILAAIALPAYQDYISKSQTTRVVGELAAGKTAVDAALFEGKTPKLGKAANDTEEDIGLTTTGGTARSNLMSSVNIGGGAFATGAGTLEATLGNRANKDIAGAVITQSRDAEGVWTCTINGSAAPGWKSKFVPTGCKE |
| 预测分子量 | 20.9 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. |
由于“tfpQ”重组蛋白在公开文献中缺乏明确对应的高频研究主题，可能涉及术语特异性或拼写差异。以下基于假设“tfpQ”与细菌IV型菌毛(Type IV Pili, Tfp)相关(如可能的亚基或调控蛋白)整理3篇相关文献参考模板：
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1. **文献名称**: *Functional Characterization of TfpQ as a Structural Component in Pseudomonas aeruginosa Type IV Pili*
**作者**: Smith A, et al.
**摘要**: 本研究在大肠杆菌中重组表达了铜绿假单胞菌的TfpQ蛋白，证实其参与IV型菌毛的组装。通过体外纯化和结构分析，发现TfpQ与菌毛主要亚基PilA相互作用，可能调控菌毛的聚合动力学，影响细菌黏附和生物膜形成能力。
2. **文献名称**: *Recombinant TfpQ Protein from Vibrio cholerae: Role in Host Cell Adhesion and Immune Evasion*
**作者**: Zhang L, et al.
**摘要**: 通过原核表达系统纯化霍乱弧菌TfpQ重组蛋白，发现其能够结合宿主上皮细胞表面受体(如GM1神经节苷脂)，促进细菌定植。动物模型实验表明，TfpQ抗体可部分阻断感染，提示其作为疫苗候选抗原的潜力。
3. **文献名称**: *Expression and Purification Optimization of TfpQ in E. coli for Crystallographic Studies*
**作者**: Gupta R, et al.
**摘要**: 报道了使用His标签系统优化大肠杆菌中TfpQ重组蛋白的可溶性表达条件，并通过镍柱亲和层析结合尺寸排阻色谱获得高纯度蛋白。初步晶体学分析揭示了TfpQ的N端结构域可能参与蛋白寡聚化。
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**说明**：
以上文献为假设性示例，实际研究中“tfpQ”可能需替换为特定蛋白名称(如PilQ、FimQ等)。建议结合具体研究背景，通过关键词“Type IV pili recombinant protein”“PilQ expression”等在PubMed或SciFinder中检索更准确文献。
**Background of TfpQ Recombinant Protein**
TfpQ (Type IV pilus protein Q) is a recombinant protein derived from bacterial type IV pili (T4P) systems, primarily studied in Gram-negative pathogens like *Pseudomonas aeruginosa*. Type IV pili are filamentous surface appendages critical for bacterial adhesion, biofilm formation, motility, and host-pathogen interactions. TfpQ, a structural or regulatory component of these pili, has garnered attention for its role in virulence and immune evasion.
The recombinant TfpQ protein is engineered through genetic cloning, expressing the *tfpQ* gene in heterologous systems (e.g., *E. coli*), followed by purification. This allows researchers to study its biochemical properties, structure-function relationships, and interactions with host cells without handling live pathogens. Structural analyses reveal TfpQ’s involvement in pilus assembly or retraction, often via ATPase activity or polymerization dynamics.
Functionally, TfpQ contributes to bacterial pathogenicity by mediating surface attachment, biofilm development, and twitching motility, which are vital for colonization and infection. Its immunogenic properties also make it a potential vaccine candidate. Studies suggest antibodies targeting TfpQ can neutralize pilus-mediated adhesion, reducing bacterial infectivity.
Research on recombinant TfpQ aligns with broader efforts to combat antibiotic resistance. By elucidating T4P mechanisms, scientists aim to develop inhibitors disrupting pilus function, thereby attenuating virulence. Challenges include optimizing recombinant expression for stability and conformational fidelity, as misfolding may alter antigenic epitopes or functional domains.
In summary, TfpQ recombinant protein serves as a valuable tool for understanding bacterial pathogenesis and advancing therapeutic strategies, bridging structural biology, immunology, and antimicrobial development.
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