| 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)：
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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。
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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.
在生物科技领域，蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者，凭借自身卓越的研发实力，每年能成功研发 1000 多种全新蛋白，在重组蛋白领域不断突破。 在重组蛋白生产过程中，艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白，到具有特定催化功能的酶、参与信号传导的激酶，再到用于免疫研究的病毒抗原，艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统，昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势，能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求，从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品，更是从源头到终端的一站式解决方案。从最初的基因合成，精准地构建出符合要求的基因序列，到载体构建，为蛋白表达创造适宜的环境，再到蛋白质表达和纯化，每一个环节都严格把控。我们充分尊重客户的个性化需求，在表达 / 纯化标签的选择、表达宿主的确定等方面，为客户量身定制专属方案。 同时，艾普蒂还配备了多种纯化体系，能够应对不同特性蛋白的纯化需求。这种灵活性和专业性，极大地提高了蛋白表达和纯化的成功率，让客户的研究项目得以顺利推进，在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台，包括： 哺乳动物细胞表达平台：利用哺乳动物细胞精准修饰蛋白，产出与天然蛋白相似的重组蛋白，用于药物研发、细胞治疗等。 杂交瘤开发平台：通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株，优化后的技术让抗体亲和力与特异性更高，应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台：FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞；Beacon® 基于微流控技术，单细胞水平捕获、分析 B 细胞，挖掘抗体多样性，缩短开发周期。 凭借这些平台，艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务，推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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