| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MPL |
| Uniprot No | P40238 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-491aa |
| 氨基酸序列 | QDVSLLASDSEPLKCFSRTFEDLTCFWDEEEAAPSGTYQLLYAYPREKPRACPLSSQSMPHFGTRYVCQFPDQEEVRLFFPLHLWVKNVFLNQTRTQRVLFVDSVGLPAPPSIIKAMGGSQPGELQISWEEPAPEISDFLRYELRYGPRDPKNSTGPTVIQLIATETCCPALQRPHSASALDQSPCAQPTMPWQDGPKQTSPSREASALTAEGGSCLISGLQPGNSYWLQLRSEPDGISLGGSWGSWSLPVTVDLPGDAVALGLQCFTLDLKNVTCQWQQQDHASSQGFFYHSRARCCPRDRYPIWENCEEEEKTNPGLQTPQFSRCHFKSRNDSIIHILVEVTTAPGTVHSYLGSPFWIHQAVRLPTPNLHWREISSGHLELEWQHPSSWAAQETCYQLRYTGEGHQDWKVLEPPLGARGGTLELRPRSRYRLQLRARLNGPTYQGPWSSWSDPTRVETATETAW |
| 预测分子量 | 56.5 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MPL重组蛋白的3篇代表性文献示例(注：文献信息为示例性质，实际引用需核实原文)：
1. **文献名称**：*Recombinant human thrombopoietin: basic biology and evaluation of clinical studies*
**作者**：Kaushansky K.
**摘要**：探讨重组人促血小板生成素(rhTPO)与MPL受体结合的分子机制，总结其在治疗化疗引起的血小板减少症的临床试验结果，证明其安全性和促进血小板再生的有效性。
2. **文献名称**：*Structural and functional analysis of the MPL receptor using recombinant protein expression*
**作者**：Staerk J. et al.
**摘要**：通过重组表达技术解析MPL受体胞外域的三维结构，揭示其与TPO结合的关键表位，为开发靶向MPL的激动剂类药物提供结构基础。
3. **文献名称**：*A novel MPL agonist peptide mimicking thrombopoietin improves megakaryocyte proliferation in vitro*
**作者**：Li J. et al.
**摘要**：设计了一种重组MPL激动剂多肽，体外实验显示其可激活JAK-STAT信号通路，显著促进巨核细胞增殖，为小分子TPO模拟物的开发提供新策略。
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**提示**：实际研究中建议通过PubMed或Web of Science以关键词“MPL recombinant protein”、“thrombopoietin receptor therapeutic”检索最新文献，重点关注高被引论文及权威期刊(如*Blood*、*Nature Biotechnology*)。
**Background of MPL Recombinant Proteins**
MPL (Mycoplasma pneumoniae lysate) recombinant proteins are derived from *Mycoplasma pneumoniae*, a pathogenic bacterium responsible for respiratory infections, including atypical pneumonia. *M. pneumoniae* lacks a cell wall and exhibits antigenic variability, complicating diagnostic and therapeutic strategies. Traditional approaches to study or target this pathogen often rely on whole-cell lysates or inactivated strains, which may pose safety risks or lack specificity.
Recombinant protein technology has emerged as a pivotal tool to address these challenges. MPL recombinant proteins are engineered by cloning and expressing specific antigenic genes of *M. pneumoniae* in heterologous systems, such as *E. coli* or yeast. This allows large-scale production of purified antigens, enabling precise immunological studies and vaccine development. Key targets include the P1 adhesin, CARDS toxin, and other surface proteins critical for bacterial adhesion and virulence.
The development of MPL recombinant proteins has advanced diagnostics by improving serological assays (e.g., ELISA) through standardized antigens, reducing cross-reactivity. In vaccine research, these proteins offer safer alternatives to live-attenuated or whole-cell vaccines, focusing immune responses on protective epitopes. However, challenges remain, such as ensuring conformational fidelity of recombinant antigens and addressing the pathogen’s genetic diversity.
Recent studies explore fusion proteins or multi-epitope constructs to enhance immunogenicity. Additionally, adjuvants or delivery systems (e.g., nanoparticles) are being tested to boost efficacy. Beyond medical applications, MPL recombinant proteins are used in basic research to dissect host-pathogen interactions and immune evasion mechanisms.
Overall, MPL recombinant proteins represent a convergence of molecular biology and immunology, offering targeted solutions for combating *M. pneumoniae* infections while providing a framework for addressing similar intracellular pathogens.
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