| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHEM |
| Uniprot No | Q99969 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-157aa |
| 氨基酸序列 | MELTEAQRRG LQVALEEFHK HPPVQWAFQE TSVESAAVDTP FPAGIFVRLE FKLQQTSRK RDWKKPECKV RPNGRKRKCL ACIKLGSEDK VLGRLVHCPI ETQVLREAEE HQETQCLRVQ RAGEDPHSFY FPGQFAFS |
| 预测分子量 | 16 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3条关于重组蛋白研究的代表性参考文献示例(注：内容为虚构，仅作格式参考)：
1. **文献名称**：Optimization of Recombinant Protein Expression in E. coli Using Chemical Chaperones
**作者**：Zhang, L., et al. (2021)
**摘要**：本研究通过添加化学伴侣分子(如L-精氨酸)优化大肠杆菌表达系统，显著提高重组蛋白溶解性和产量，为工业规模生产提供新策略。
2. **文献名称**：Site-Specific Chemical Modification of Recombinant Antibodies for Enhanced Tumor Targeting
**作者**：Smith, J.R., & Lee, H. (2019)
**摘要**：开发了一种基于点击化学的定点修饰技术，改善重组抗体-药物偶联物(ADC)的肿瘤靶向性，体外实验显示细胞毒性提升3倍。
3. **文献名称**：Chemically Defined Mammalian Cell Culture System for Recombinant Glycoprotein Production
**作者**：Tanaka, K., et al. (2020)
**摘要**：设计无动物源成分的化学成分限定培养基，在CHO细胞中实现重组糖蛋白的高效表达，糖基化一致性达到>95%，满足治疗性蛋白生产标准。
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如需真实文献推荐，可提供具体研究方向(如表达系统/修饰技术/应用领域)，我将协助筛选相关领域的高影响力论文。
**Background of CHEM Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are pivotal in modern biotechnology and biomedical research. The development of CHEM (a hypothetical designation for illustrative purposes) recombinant proteins stems from advancements in molecular cloning, expression systems, and protein purification techniques. These proteins are synthesized by inserting target gene sequences into host organisms (e.g., bacteria, yeast, or mammalian cells), enabling large-scale production of functional proteins that mimic natural counterparts.
The rise of CHEM recombinant proteins addresses limitations in traditional protein extraction methods, such as low yield, contamination risks, and ethical concerns. By leveraging recombinant DNA technology, CHEM proteins are designed with high purity, specificity, and scalability. Common host systems include *E. coli* for cost-effective production and mammalian cells for post-translational modifications (e.g., glycosylation), ensuring biological activity in therapeutic applications.
Applications span therapeutics (e.g., monoclonal antibodies, vaccines), diagnostics (e.g., enzyme-linked immunosorbent assays), and basic research (e.g., structural studies). For instance, CHEM-engineered cytokines or growth factors are utilized in cancer immunotherapy, while insulin and clotting factors exemplify life-saving recombinant therapeutics.
Innovations in CRISPR, synthetic biology, and AI-driven protein design further enhance CHEM platforms, enabling customization for complex proteins, improved stability, and reduced immunogenicity. Challenges persist, such as optimizing expression yields and ensuring consistent post-translational modifications, yet ongoing research aims to refine these processes.
Overall, CHEM recombinant proteins exemplify the synergy between genetic engineering and industrial biotechnology, driving progress in precision medicine, industrial enzymology, and beyond. Their development underscores a transformative shift toward tailored, sustainable protein production to meet global health and scientific demands.
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