| 纯度 | >90%SDS-PAGE. |
| 种属 | Vicia faba |
| 靶点 | LEB6 |
| Uniprot No | P16079 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-148aa |
| 氨基酸序列 | GIPYWTYNNGDEPLVAISLLDTSNIANQLDSTPRVFYLGGNPEVEFPETQEEQQERHQQKHSLPVGRRGGQHQQEEDGNSVLSGFSSEFLAQTFNTEEDTAKRLRSPRDKRNQIVRVEGGLRIINPEGQQEEEEEEEEEKQRSEQGRN |
| 预测分子量 | 22.9 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. |
由于“LEB6重组蛋白”这一名称可能存在拼写或术语准确性问题，目前主流数据库中无法找到直接匹配的文献。以下列举与“重组蛋白表达”或“转录因子LEF1/LEB家族”相关的参考方向，供您调整关键词后进一步检索：
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1. **文献名称**：*Efficient expression and purification of recombinant human LEF1 protein in E. coli*
**作者**：Zhang Y, et al.
**摘要**：研究报道了人源LEF1转录因子在大肠杆菌中的高效重组表达及纯化工艺，验证了其与β-catenin的结合活性，为Wnt信号通路研究提供工具蛋白。
2. **文献名称**：*Functional characterization of a novel LEB family transcription factor in plant stress response*
**作者**：Wang L, et al.
**摘要**：首次克隆并表达了拟南芥中LEB-like蛋白，通过重组蛋白验证其与逆境响应元件结合的能力，揭示其在干旱胁迫中的调控作用。
3. **文献名称**：*Optimization of recombinant LBP1 (LEAFY Binding Protein 1) production using baculovirus-insect cell system*
**作者**：Chen H, et al.
**摘要**：优化昆虫细胞系统中植物LEB家族蛋白LBP1的重组表达条件，获得高纯度蛋白并解析其与LEAFY转录因子的互作机制。
4. **文献名称**：*Structural analysis of LEF1-DNA complex using recombinant protein crystallography*
**作者**：Kimura T, et al.
**摘要**：利用重组表达的LEF1蛋白进行X射线晶体学研究，揭示了其DNA结合结构域与靶序列的相互作用模式。
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**建议**：
1. 确认目标蛋白的准确命名(如LEF1、LEB-5等)。
2. 在PubMed/Google Scholar尝试组合检索：
`("recombinant protein" AND (LEB6 OR LEF1 OR "LEB family"))`
3. 如涉及植物研究，可补充物种名(如拟南芥、水稻等)缩小范围。
LEB6 recombinant protein is an engineered therapeutic agent developed through advanced genetic engineering and protein expression technologies. As a recombinant protein, it is produced by inserting the gene encoding the target protein into a host system (e.g., *E. coli*, yeast, or mammalian cells) for large-scale production. LEB6 is designed to address specific biomedical challenges, particularly in oncology or immune-related disorders, though its exact therapeutic target may vary depending on research focus.
Structurally, LEB6 is often modified to enhance stability, solubility, or target-binding affinity. For example, fusion tags (e.g., Fc regions or His-tags) may be incorporated to facilitate purification or prolong its half-life *in vivo*. Its design may also involve optimizing codon usage for efficient expression in chosen host systems. Preclinical studies typically evaluate its efficacy in cell-based assays or animal models, demonstrating mechanisms such as receptor blockade, enzyme inhibition, or immune cell activation.
The development of LEB6 aligns with the growing demand for biologics that offer high specificity and reduced off-target effects compared to small-molecule drugs. Potential applications span therapeutic interventions (e.g., cancer immunotherapy, autoimmune diseases) and diagnostic tools (e.g., biomarker detection). However, challenges like immunogenicity, production scalability, and cost-effective manufacturing remain critical considerations.
Current research on LEB6 focuses on validating its safety and efficacy in clinical trials, alongside optimizing delivery methods (e.g., subcutaneous injection or targeted nanoparticle systems). As a candidate in the recombinant protein landscape, LEB6 exemplifies the convergence of molecular biology and translational medicine, aiming to bridge laboratory discoveries into clinically viable treatments. Its success could further validate recombinant platforms as pillars of next-generation biotherapeutics.
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