| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MIg |
| Uniprot No | P83881 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-106aa |
| 氨基酸序列 | MVNVPKTRRT FCKKCGKHQP HKVTQYKKGK DSLYAQGKRR YDRKQSGYGG QTKPIFRKKA KTTKKIVLRL ECVEPNCRSK RMLAIKRCKH FELGGDKKRK GQVIQF |
| 预测分子量 | 12,4 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MIg(膜免疫球蛋白)重组蛋白的3篇模拟参考文献，涵盖结构、表达及应用方向：
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1. **文献名称**：*Expression and Functional Analysis of Recombinant Membrane Immunoglobulin in B Cell Signaling*
**作者**：Smith, J., et al.
**摘要**：该研究通过哺乳动物细胞系统成功表达重组MIg蛋白，并验证其作为B细胞受体(BCR)的信号传导功能，证实重组MIg可激活下游酪氨酸激酶通路，为研究BCR相关疾病提供工具。
2. **文献名称**：*Engineering scFv-Based Recombinant MIg Mimetics for Targeted Therapy*
**作者**：Chen, L., & Wang, H.
**摘要**：作者设计了一种基于单链抗体(scFv)的重组MIg模拟蛋白，能够特异性结合肿瘤抗原。体外实验显示其可诱导癌细胞凋亡，为开发新型靶向免疫疗法奠定基础。
3. **文献名称**：*Cryo-EM Structure Determination of Recombinant MIg Complexes*
**作者**：Kumar, R., et al.
**摘要**：利用冷冻电镜技术解析了重组MIg与抗原结合的高分辨率三维结构，揭示了其跨膜区与胞内信号分子的相互作用机制，为优化重组MIg的稳定性提供结构依据。
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**注**：以上文献为模拟示例，实际研究中建议通过PubMed、Google Scholar等平台检索最新论文。若需具体领域文献，可提供更详细的关键词或研究方向。
**Background of Recombinant MIg Proteins**
Recombinant proteins, including monoclonal immunoglobulins (MIg), are engineered through genetic modification to mimic natural proteins, offering precise control over structure and function. The development of recombinant MIg traces back to advancements in molecular biology in the late 20th century, particularly the advent of recombinant DNA technology. This innovation enabled the insertion of immunoglobulin genes into expression systems like bacteria, yeast, or mammalian cells, bypassing traditional hybridoma methods and improving scalability, consistency, and customization.
MIg proteins typically consist of antibody fragments (e.g., Fab, scFv) or full-length immunoglobulins designed for therapeutic, diagnostic, or research applications. Their engineering allows for tailored antigen-binding sites, reduced immunogenicity (e.g., humanized or chimeric designs), and enhanced functional properties (e.g., increased stability or binding affinity). For example, therapeutic MIgs are pivotal in oncology, autoimmune diseases, and infectious diseases, targeting specific biomarkers with high precision.
The production process involves cloning antibody genes into expression vectors, transfecting host cells, and purifying the expressed proteins. Mammalian systems (e.g., CHO cells) are preferred for post-translational modifications, ensuring proper folding and glycosylation. Recent innovations, such as CRISPR-based editing and transient expression systems, have accelerated development cycles and improved yields.
Recombinant MIgs also address limitations of conventional antibodies, such as batch-to-batch variability and ethical concerns in animal-derived production. They underpin cutting-edge therapies like bispecific antibodies and antibody-drug conjugates (ADCs), expanding treatment modalities. Additionally, diagnostic applications leverage their specificity in assays like ELISA or flow cytometry.
Current research focuses on optimizing expression platforms, enhancing pharmacokinetics, and exploring novel formats (e.g., nanobodies). As personalized medicine grows, recombinant MIgs represent a cornerstone of targeted therapies, driving innovation in biologics and precision healthcare.
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