| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | mipA |
| Uniprot No | P0A908 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-248aa |
| 氨基酸序列 | EGKFSLGAGVGVVEHPYKDYDTDVYPVPVINYEGDNFWFRGLGGGYYLWNDATDKLSITAYWSPLYFKAKDSGDHQMRHLDDRKSTMMAGLSYAHFTQYGYLRTTLAGDTLDNSNGIVWDMAWLYRYTNGGLTVTPGIGVQWNSENQNEYYYGVSRKESARSGLRGYNPNDSWSPYLELSASYNFLGDWSVYGTARYTRLSDEVTDSPMVDKSWTGLISTGITYKF |
| 预测分子量 | 33.1 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mipA重组蛋白的3篇参考文献示例(注：内容为假设性概括，实际文献需根据具体研究验证)：
1. **文献名称**: "Cloning, Expression, and Purification of the mipA Gene from *Legionella pneumophila*"
**作者**: Smith J, et al.
**摘要**: 该研究成功克隆了嗜肺军团菌的*mi*pA基因，并在大肠杆菌中表达重组MipA蛋白。通过亲和层析纯化后，证实该蛋白具有脯氨酰异构酶活性，可能增强细菌在巨噬细胞内的存活能力。
2. **文献名称**: "Structural Insights into the Virulence-associated MipA Protein of *Pseudomonas aeruginosa*"
**作者**: Zhang L, et al.
**摘要**: 通过X射线晶体学解析了铜绿假单胞菌MipA重组蛋白的三维结构，揭示其FK506结合蛋白结构域，并证明其通过调控宿主细胞信号通路促进细菌感染。
3. **文献名称**: "Recombinant MipA as a Potential Vaccine Candidate Against *Burkholderia pseudomallei*"
**作者**: Patel R, et al.
**摘要**: 研究利用重组MipA蛋白免疫小鼠，发现其可诱导高滴度抗体反应，并在攻毒实验中显著降低类鼻疽杆菌的肺部定植，提示其疫苗开发潜力。
4. **文献名称**: "Functional Characterization of mipA in *Salmonella Typhimurium* Pathogenesis"
**作者**: Kim H, et al.
**摘要**: 通过敲除和回补实验证实，重组表达的MipA蛋白在鼠伤寒沙门氏菌侵染上皮细胞过程中起关键作用，可能通过调节宿主细胞骨架重组促进细菌侵袭。
(注：以上内容为示例，实际文献需根据具体研究检索确认。)
**Background of MipA Recombinant Protein**
MipA (Macrophage infectivity potentiator A) is a virulence-associated protein initially identified in pathogenic bacteria such as *Legionella pneumophila* and *Pseudomonas aeruginosa*. It belongs to the immunophilin family, characterized by peptidyl-prolyl cis-trans isomerase (PPIase) activity, which facilitates protein folding and conformational changes by catalyzing the isomerization of peptide bonds. This enzymatic function is critical for bacterial survival within host cells, particularly in evading immune responses and promoting intracellular replication.
In *L. pneumophila*, MipA enhances the bacterium's ability to infect and proliferate within macrophages, a key step in Legionnaires' disease pathogenesis. Structural studies reveal that MipA contains a conserved FK506-binding protein (FKBP)-like domain, which mediates interactions with host cell components. Its role in bacterial virulence has made it a target for therapeutic interventions, including small-molecule inhibitors.
Recombinant MipA protein is produced via genetic engineering, typically using *Escherichia coli* expression systems. The gene encoding MipA is cloned into expression vectors, allowing large-scale production of the protein for functional and structural studies. Recombinant versions retain enzymatic activity and are utilized to investigate host-pathogen interactions, screen inhibitory compounds, or develop diagnostic tools.
Research on MipA also extends to vaccine development, as antibodies against MipA can neutralize bacterial infectivity in experimental models. Additionally, its conserved nature across bacterial species suggests potential as a broad-spectrum target. Studies on recombinant MipA continue to advance understanding of bacterial pathogenesis and inform strategies for combating infections caused by opportunistic pathogens.
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