纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | TLF1 |
Uniprot No | P05620 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 25-260aa |
氨基酸序列 | VIGGDECNINEHPFLVALYDAWSGRFLCGGTLINPEWVLTAAHCDSKNFKMKLGAHSKKVLNEDEQIRNPKEKFICPNKKNDEVLDKDIMLIKLDSPVSYSEHIAPLSLPSSPPSVGSVCRIMGWGSITPVEETFPDVPHCANINLLDDVECKPGYPELLPEYRTLCAGVLQGGIDTCGFDSGTPLICNGQFQGIVSYGGHPCGQSRKPGIYTKVFDYNAWIQSIIAGNTAATCLP |
预测分子量 | 33.1 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TLF1(Trypanosome Lytic Factor-1)重组蛋白研究的示例参考文献(注:部分内容为示例性概括,实际文献需通过学术数据库查询):
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1. **标题**:*Recombinant TLF1 as a potential therapeutic agent against African trypanosomiasis*
**作者**:Smith J, Doe R, et al.
**摘要**:本研究成功在大肠杆菌中表达并纯化了重组TLF1蛋白,证实其具有体外裂解布氏锥虫(Trypanosoma brucei)的活性,为开发抗锥虫病药物提供了实验基础。
2. **标题**:*Structural and functional characterization of the TLF1 recombinant protein*
**作者**:Zhang Y, Wang L, et al.
**摘要**:通过X射线晶体学解析了重组TLF1的三维结构,揭示了其与锥虫细胞表面受体结合的特定结构域,并验证了其溶虫活性依赖pH环境。
3. **标题**:*TLF1-mediated oxidative stress pathways in trypanosome killing*
**作者**:Johnson M, Brown K, et al.
**摘要**:研究发现重组TLF1通过诱导锥虫细胞内活性氧(ROS)积累触发程序性细胞死亡,阐明了其分子作用机制。
4. **标题**:*Expression optimization and delivery challenges of recombinant TLF1 in vivo*
**作者**:Lee S, Martinez P, et al.
**摘要**:评估了不同表达系统(哺乳动物细胞、昆虫细胞)生产重组TLF1的效率,并探讨了其在小鼠模型中的药代动力学特性及递送障碍。
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**注意**:以上为模拟示例,实际文献需通过PubMed、Google Scholar等平台以关键词“TLF1 recombinant protein”或“Trypanosome Lytic Factor-1”检索。TLF1相关研究多集中于抗寄生虫机制,重组蛋白的应用常涉及表达优化、结构功能分析及治疗潜力探索。
**Background of TLF1 Recombinant Protein**
TLF1 (TATA-box-binding protein-like factor 1), also known as TBPL1. is a member of the TBP (TATA-box-binding protein) family of transcription factors. Unlike canonical TBP, which is essential for RNA polymerase II-mediated transcription initiation at TATA-containing promoters, TLF1 lacks the ability to bind TATA boxes. Instead, it plays distinct roles in transcriptional regulation, particularly in TATA-less promoters and during specific developmental stages. TLF1 is evolutionarily conserved and has been implicated in embryogenesis, germ cell development, and cellular differentiation. Studies in model organisms, such as zebrafish and mice, reveal its critical function in early embryonic development, where its depletion leads to developmental arrest or lethality.
Structurally, TLF1 shares homology with TBP in its core domain but diverges in regions responsible for DNA binding and protein interactions. This divergence underlies its unique regulatory mechanisms. Recombinant TLF1 protein is typically produced using expression systems like *E. coli* or mammalian cell cultures, followed by purification via affinity tags. Its recombinant form enables biochemical studies, including protein-DNA/RNA interaction assays, structural analyses, and exploration of its role in chromatin remodeling or transcriptional complexes.
Research on TLF1 has expanded into disease contexts, particularly cancer, where aberrant transcriptional regulation is common. Its involvement in stem cell maintenance and differentiation also links it to regenerative medicine. However, challenges remain in fully elucidating its interaction partners, regulatory networks, and tissue-specific functions. TLF1 recombinant protein thus serves as a vital tool for dissecting the complexity of eukaryotic transcription and developmental biology.
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