| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TM |
| Uniprot No | O75204 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-238aa |
| 氨基酸序列 | MYAPGGAGLPGGRRRRSPGGSALPKQPERSLASALPGALSITALCTALAEPAWLHIHGGTCSRQELGVSDVLGYVHPDLLKDFCMNPQTVLLLRVIAAFCFLGILCSLSAFLLDVFGPKHPALKITRRYAFAHILTVLQCATVIGFSYWASELILAQQQQHKKYHGSQVYVTFAVSFYLVAGAGGASILATAANLLRHYPTEEEEQALELLSEMEENEPYPAEYEVINQFQPPPAYTP |
| 预测分子量 | 25,8 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TM(跨膜)重组蛋白的3篇参考文献示例，涵盖表达技术、结构解析及应用方向：
1. **《Strategies for the recombinant expression of transmembrane proteins in Escherichia coli》**
- 作者：M. Overton 等
- 摘要：探讨在大肠杆菌中表达跨膜蛋白的技术挑战，提出通过融合标签、膜定位优化及宿主改造提升表达效率，为大规模生产提供方案。
2. **《Baculovirus-mediated expression of G protein-coupled receptors in insect cells for structural studies》**
- 作者：A. Akermann 等
- 摘要：利用杆状病毒-昆虫细胞系统高效表达GPCRs(跨膜蛋白家族)，结合纯化技术获得高纯度蛋白，支持晶体学和冷冻电镜结构解析。
3. **《Single-particle cryo-EM analysis of membrane proteins: From structure to drug discovery》**
- 作者：Y. Cheng 等
- 摘要：综述冷冻电镜技术在跨膜蛋白结构解析中的应用，以实例展示其如何推动针对离子通道和受体的药物设计。
4. **《Targeting transmembrane proteins in cancer therapy: Insights from recombinant antibody engineering》**
- 作者：S. Zhang 等
- 摘要：研究基于重组跨膜蛋白(如HER2)开发单克隆抗体及抗体-药物偶联物，验证其在癌症靶向治疗中的潜力。
(注：以上文献为示例性质，实际引用时需核实作者、标题及内容准确性。)
**Background of TM Recombinant Proteins**
Transmembrane (TM) recombinant proteins are engineered molecules designed to mimic the structure and function of natural membrane-spanning proteins, which play critical roles in cellular signaling, transport, and adhesion. These proteins typically contain one or more hydrophobic α-helical domains that anchor them within lipid bilayers, enabling interactions with both extracellular and intracellular environments. Their complexity arises from challenges in maintaining structural integrity outside native membranes, limiting traditional study methods.
The advent of recombinant DNA technology revolutionized TM protein research by enabling their production in heterologous systems (e.g., *E. coli*, yeast, mammalian cells*). Key strategies include codon optimization, fusion tags (e.g., His-tags, GFP), and modified expression vectors to enhance solubility and stability. Despite progress, producing functional TM proteins remains challenging due to hydrophobicity-driven aggregation and incomplete post-translational modifications in prokaryotic systems. Mammalian or insect cell systems are often preferred for complex folding and glycosylation.
Applications span drug discovery (e.g., targeting G protein-coupled receptors), structural biology (via cryo-EM or X-ray crystallography), and synthetic biology (designing artificial membrane systems). For instance, recombinant TM proteins like ion channels or transporters are pivotal in screening therapeutics for neurological or metabolic disorders.
Recent advances in detergent screening, lipid nanodiscs, and cell-free expression systems have improved yield and functionality. Additionally, computational modeling aids in predicting TM domain interactions, guiding rational design. Ongoing research focuses on optimizing transmembrane segment folding and developing high-throughput purification methods.
In summary, TM recombinant proteins bridge gaps in understanding membrane protein dynamics, offering tools for biomedical innovation. Their continued development relies on interdisciplinary approaches combining genetic engineering, biophysics, and bioinformatics.
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