| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MG |
| Uniprot No | P29372 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-298aa |
| 氨基酸序列 | MVTPALQMKKPKQFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSD AAQAPCPRERCLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLAR AFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMF MKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTL RKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLE PSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQALE HHHHHH |
| 预测分子量 | 34 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MG重组蛋白研究的示例参考文献(注：以下为模拟示例，非真实文献)：
---
1. **标题**：Optimization of Mycoplasma genitalium Recombinant Protein Expression in E. coli
**作者**：Zhang, L. et al.
**摘要**：本研究通过优化大肠杆菌BL21(DE3)中的诱导条件(温度、IPTG浓度)，成功提高了MG重组蛋白(假设为MG_ribosomal蛋白)的可溶性表达。结果表明，20°C诱导显著减少包涵体形成，为后续功能研究奠定基础。
2. **标题**：Functional Characterization of a Novel MG Membrane Glycoprotein Expressed in HEK293 Cells
**作者**：Smith, J.R. & Patel, A.
**摘要**：利用哺乳动物HEK293细胞系统表达MG膜糖蛋白(MG-MP)，证实其正确糖基化及细胞膜定位。通过表面等离子共振技术(SPR)揭示了该蛋白与宿主细胞受体的相互作用机制。
3. **标题**：A Rapid Purification Strategy for MG Recombinant Antigen Using Tag-free Chromatography
**作者**：Kim, S. et al.
**摘要**：开发了一种新型无标签纯化方法，通过离子交换层析结合尺寸排阻色谱，从毕赤酵母表达系统中高效纯化MG重组抗原，纯度达95%，适用于诊断试剂开发。
4. **标题**：Evaluation of MG Recombinant Protein as a Vaccine Candidate in Murine Models
**作者**：García, M. et al.
**摘要**：在小鼠模型中评估了MG重组蛋白(假设为黏附素蛋白)的免疫原性，显示其可诱导特异性抗体及Th1型细胞免疫应答，提示其作为疫苗候选的潜力。
---
以上示例涵盖表达优化、功能研究、纯化策略及应用探索，供参考学习重组蛋白研究框架。实际研究中请查询具体数据库(如PubMed)获取真实文献。
**Background of MG Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biomedical research and therapeutic development. MG recombinant proteins, a representative category in this field, are typically produced using advanced expression systems (e.g., mammalian cells, bacteria, or yeast) to ensure proper folding, post-translational modifications, and bioactivity. These proteins are designed to mimic naturally occurring molecules, enabling their use in drug discovery, diagnostics, and functional studies of disease mechanisms.
The development of MG recombinant proteins often leverages mammalian expression platforms, such as CHO (Chinese Hamster Ovary) or HEK293 cells, to achieve human-like glycosylation and structural accuracy. This is critical for therapeutic applications, where protein stability, immunogenicity, and receptor interactions must closely resemble native human proteins. For research, MG recombinant proteins serve as standardized tools to study signaling pathways, protein-protein interactions, and cellular responses, reducing variability compared to animal-derived or tissue-extracted proteins.
In therapeutics, MG recombinant proteins have enabled breakthroughs in treating cancers, autoimmune disorders, and infectious diseases. Examples include monoclonal antibodies, cytokines, and fusion proteins targeting specific molecular pathways. For instance, MG-engineered checkpoint inhibitors (e.g., anti-PD-1/PD-L1) are widely used in oncology, while recombinant cytokines like interferons or interleukins modulate immune responses.
Quality control remains a cornerstone of MG recombinant protein production. Rigorous testing ensures endotoxin-free products, high purity (>95%), and batch-to-batch consistency, meeting regulatory standards for clinical and research use. Innovations in protein engineering, such as site-specific mutagenesis or Fc-fusion technologies, further enhance their functionality and half-life.
Despite advancements, challenges persist in scaling production, optimizing yield, and minimizing costs. MG recombinant proteins continue to evolve with emerging technologies like CRISPR-based editing and AI-driven protein design, promising faster development of tailored therapies. Their versatility and precision underscore their pivotal role in advancing precision medicine and understanding human biology.
×
