| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | TM1 |
| Uniprot No | A1KYZ2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-284aa |
| 氨基酸序列 | MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANNRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANIQLVEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSGY |
| 预测分子量 | 48.8 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TM1重组蛋白的3篇示例参考文献(注：内容为模拟虚构，仅供参考)：
---
1. **文献名称**: *Structural insights into TM1 domain of GPCRs through recombinant protein expression*
**作者**: Zhang L, et al.
**摘要**: 本研究成功表达并纯化了GPCR家族中TM1结构域的重组蛋白，通过X射线晶体学解析其三维结构，揭示了TM1在受体激活中的构象变化机制。
---
2. **文献名称**: *Functional characterization of recombinant TM1 protein in cancer cell signaling*
**作者**: Patel R, et al.
**摘要**: 利用哺乳动物细胞系统表达TM1重组蛋白，发现其通过调控EGFR信号通路抑制肿瘤细胞迁移，为靶向TM1的抗癌药物开发提供实验依据。
---
3. **文献名称**: *Optimization of TM1 recombinant protein production in E. coli for therapeutic applications*
**作者**: Müller S, et al.
**摘要**: 通过优化大肠杆菌表达系统的培养条件和密码子偏好性，大幅提升TM1重组蛋白的产量和稳定性，推动其在蛋白质药物领域的规模化制备。
---
如需真实文献，建议在PubMed或Web of Science中检索关键词“TM1 recombinant protein”或结合具体蛋白名称(如“GPCR TM1”)。
TM1 recombinant protein refers to a class of engineered transmembrane proteins or protein domains that play critical roles in cellular signaling, ion transport, or structural integrity. The "TM1" designation typically denotes the first transmembrane domain within multi-pass membrane proteins, such as G protein-coupled receptors (GPCRs), ion channels, or adhesion molecules. These proteins are characterized by their α-helical structures spanning the lipid bilayer, often serving as functional or regulatory units. Recombinant TM1 proteins are produced using biotechnological platforms (e.g., E. coli, yeast, or mammalian cell systems) to enable detailed study of membrane protein behavior, which is challenging in native environments due to their hydrophobicity and structural complexity.
Research on TM1 recombinant proteins has accelerated structural biology efforts, particularly in cryo-EM and X-ray crystallography, revealing mechanisms of ligand binding, conformational changes, and intermolecular interactions. They are pivotal in drug discovery, as approximately 40% of therapeutic targets are membrane proteins. For example, TM1 domains in GPCRs influence receptor activation states, making them targets for drugs treating neurological disorders or cardiovascular diseases. Challenges in production include maintaining proper folding and post-translational modifications, often addressed through codon optimization, lipid-based solubilization, or fusion tags.
Recent advancements in cell-free expression systems and nanodisc technologies have improved the yield and stability of TM1 recombinant proteins, facilitating high-throughput screening and personalized medicine applications. Their study also contributes to understanding diseases linked to membrane protein dysfunction, such as cystic fibrosis (CFTR channel) or cancer (integrin signaling). Ongoing research focuses on engineering TM1-containing chimeric proteins for biosensors or targeted therapies, highlighting their versatility in both basic science and translational applications.
×
