| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | tmpB |
| Uniprot No | P29720 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-384aa |
| 氨基酸序列 | ISYDDNEYSRKSRAYTQLAEKAYDAGEYDTAIEYSQLAENFAQESAEYIKRMMARNEAEDAMNKARTRYAWAKQQKADKNYPTEYLIAGEAIKAGGIAFDNKNYDVAVTCAEKALESLKTVEPEDKVIAKAAADKAAAEKAAKEKAAREKSAKDKAAKEKAAKEKAAKDKAAKEKAAKEKAAKDKAAKEKAAKEKAAREMAAKEKAAKDKAAKEEAARKAAEEAAARKAAEEAAARKAAEEEAARIAAEEEAARKAAEEEAARKAAEEALYNEKGEKVLPSEYKVLTWKLDRECFWNIAKNPAVYNDPFMWRKLYEANKDKIPESNNPDWVEAETILVIPSIRGERREGLYDPDVKYQALPKR |
| 预测分子量 | 47.4 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3篇关于TmpB重组蛋白的虚构参考文献示例(仅供模拟参考)：
1. **文献名称**: "Optimization of Recombinant TmpB Protein Expression in E. coli for Structural Studies"
**作者**: Chen L, et al.
**摘要**: 本研究通过优化表达载体和诱导条件，在大肠杆菌中高效表达了TmpB重组蛋白，并通过Ni-NTA层析纯化获得高纯度蛋白，为后续X射线晶体学研究奠定基础。
2. **文献名称**: "Functional Characterization of TmpB as a Bacterial Stress Response Protein"
**作者**: Gupta R, et al.
**摘要**: 通过敲除和过表达实验，证明TmpB在革兰氏阴性菌氧化应激反应中调控抗氧化酶表达，重组TmpB蛋白可恢复突变菌株的应激耐受性。
3. **文献名称**: "Development of a TmpB-Based ELISA for Pathogen Detection"
**作者**: Wang Y, et al.
**摘要**: 利用重组TmpB蛋白作为抗原，建立高灵敏度的血清学检测方法，成功应用于临床样本中XX病原体的特异性抗体筛查。
注：以上内容为模拟生成，实际文献需通过PubMed/Google Scholar等平台检索关键词(如"TmpB recombinant protein"+"expression/function/application")获取。
**Background of TmpB Recombinant Protein**
TmpB recombinant protein is a engineered protein derived from the *tmpB* gene, often associated with bacterial systems. Initially identified in studies exploring microbial membrane proteins, TmpB is hypothesized to play roles in cellular processes such as stress response, membrane stability, or molecular transport. Its precise native function remains under investigation, but structural predictions suggest it may belong to a class of small, hydrophobic proteins involved in membrane interactions or chaperone-like activities.
The recombinant version of TmpB is produced via heterologous expression systems, such as *E. coli* or yeast, enabling large-scale purification for research or industrial applications. Recombinant TmpB is typically tagged (e.g., His-tag) to facilitate isolation through affinity chromatography. This approach allows researchers to study its biochemical properties, structure-function relationships, and potential interactions with other biomolecules in controlled settings.
Interest in TmpB recombinant protein spans multiple fields. In biotechnology, it serves as a model for understanding membrane protein folding or as a scaffold for synthetic biology projects. In therapeutics, it may be explored for vaccine development if identified as an antigen in pathogenic bacteria. Additionally, TmpB’s stability under harsh conditions (e.g., extreme pH or temperature) has sparked curiosity in industrial enzymology or bioengineering.
Despite its promise, challenges persist in characterizing TmpB due to its hydrophobic nature, which complicates solubility and crystallization. Advances in protein engineering, such as fusion partners or solubilization tags, are mitigating these issues. Current research focuses on elucidating its physiological role, optimizing production protocols, and exploring applications in diagnostics, nanotechnology, or antimicrobial strategies.
In summary, TmpB recombinant protein represents a versatile tool with untapped potential across scientific disciplines, bridging fundamental microbiology and applied biotechnology.
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