纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MEC |
Uniprot No | Q9NRJ3-1 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 20-127aa |
氨基酸序列 | SEAILPIASSCCTEVSHHISRRLLERVNMCRIQRADGDCDLAAVILHVKR RRICVSPHNHTVKQWMKVQAAKKNGKGNVC HRKKHHGKRNSNRAHQGKHETYGHKTPY |
预测分子量 | 12 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MEC重组蛋白的3篇文献参考(注:MEC重组蛋白的语境可能存在多义性,以下为模拟示例):
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1. **文献名称**:*Expression and Functional Analysis of Recombinant MEC Protein in Mammary Epithelial Cells*
**作者**:Smith A, et al. (2020)
**摘要**:本研究通过基因工程技术在大肠杆菌中高效表达MEC重组蛋白,并验证其在乳腺上皮细胞中的生物学功能。实验表明该蛋白能调控细胞增殖和分化,为乳腺疾病机制研究提供新工具。
2. **文献名称**:*Structural Characterization of MEC Recombinant Protein for Vaccine Development*
**作者**:Zhang L, et al. (2018)
**摘要**:通过X射线晶体学解析MEC重组蛋白的三维结构,揭示其抗原表位区域。动物实验表明,该蛋白可诱导特异性抗体反应,为开发针对乳腺相关病原体的疫苗奠定基础。
3. **文献名称**:*Optimization of MEC Recombinant Protein Production in Yeast Expression Systems*
**作者**:Kim S, et al. (2021)
**摘要**:系统优化毕赤酵母系统中MEC重组蛋白的表达条件,显著提高产量和稳定性。纯化后的蛋白在体外实验中表现出优异的酶活性,适用于工业化生产。
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**注意**:以上内容为模拟生成,实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“MEC recombinant protein”或结合具体研究背景调整检索策略。若MEC指代特定蛋白(如甲基化酶或病原体相关蛋白),需补充全称以精准查询。
**Background of MEC Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biomedical research and therapeutic development. Among these, MEC (Multiepitope-Engineered Chimeric) recombinant proteins represent a specialized class designed to enhance immune targeting and functionality. These proteins are constructed by combining multiple antigenic epitopes—distinct regions of pathogens or disease-associated molecules—into a single chimeric structure. This design leverages epitope synergy to improve immunogenicity, stability, and specificity compared to single-epitope formulations.
The development of MEC recombinant proteins is driven by the need for advanced vaccines and diagnostics. Traditional approaches often focus on isolated antigens, which may fail to elicit broad or durable immune responses. By integrating epitopes from diverse pathogens or tumor-associated antigens, MEC proteins aim to trigger cross-reactive immunity, addressing challenges like pathogen variability (e.g., influenza, HIV) or cancer heterogeneity. Additionally, their modular architecture allows customization for specific applications, such as incorporating adjuvants or fusion tags for purification.
Production typically involves recombinant DNA technology, where target epitope sequences are cloned into expression vectors and expressed in host systems (e.g., *E. coli*, yeast, or mammalian cells). Advances in bioinformatics and structural biology have streamlined epitope selection and chimeric design, ensuring proper folding and functional presentation.
MEC recombinant proteins hold promise in vaccine development, particularly for complex diseases requiring multi-target immunity. They are also explored in antibody production, immunotherapy, and diagnostic assays. Challenges remain in optimizing epitope compatibility, minimizing off-target effects, and scaling manufacturing. Ongoing research focuses on improving delivery systems (e.g., nanoparticle carriers) and leveraging AI-driven design to refine efficacy.
In summary, MEC recombinant proteins exemplify the convergence of immunology, genetic engineering, and computational design, offering tailored solutions for next-generation biomedical interventions. Their versatility and precision position them as critical tools in combating evolving global health threats.
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