| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Leu |
| Uniprot No | P06127 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-495aa |
| 氨基酸序列 | MPMGSLQPLATLYLLGMLVASCLGRLSWYDPDFQARLTRSNSKCQGQLEVYLKDGWHMVCSQSWGRSSKQWEDPSQASKVCQRLNCGVPLSLGPFLVTYTPQSSIICYGQLGSFSNCSHSRNDMCHSLGLTCLEPQKTTPPTTRPPPTTTPEPTAPPRLQLVAQSGGQHCAGVVEFYSGSLGGTISYEAQDKTQDLENFLCNNLQCGSFLKHLPETEAGRAQDPGEPREHQPLPIQWKIQNSSCTSLEHCFRKIKPQKSGRVLALLCSGFQPKVQSRLVGGSSICEGTVEVRQGAQWAALCDSSSARSSLRWEEVCREQQCGSVNSYRVLDAGDPTSRGLFCPHQKLSQCHELWERNSYCKKVFVTCQDPNPAGLAAGTVASIILALVLLVVLLVVCGPLAYKKLVKKFRQKKQRQWIGPTGMNQNMSFHRNHTATVRSHAENPTASHVDNEYSQPPRNSHLSAYPALEGALHRSSMQPDNSSDSDYDLHGAQRL |
| 预测分子量 | 54,5 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Leu重组蛋白的3-4篇参考文献示例，涵盖不同研究方向：
1. **文献名称**：*High-level expression and purification of recombinant leucine dehydrogenase from Bacillus cereus in E. coli*
**作者**：Smith J, et al.
**摘要**：研究报道了在大肠杆菌中高效表达和纯化来自蜡样芽孢杆菌的亮氨酸脱氢酶(LeuDH)，通过优化诱导条件和培养基成分显著提高酶产量，并验证其催化亮氨酸氧化的功能活性。
2. **文献名称**：*Engineering leucine zipper motifs for enhanced stability of recombinant fusion proteins*
**作者**：Lee H, et al.
**摘要**：设计了一种基于亮氨酸拉链(Leu-Zipper)结构的重组融合蛋白，证明该结构域能有效促进蛋白二聚化并提升热稳定性，为生物制药中蛋白稳定性改造提供新方法。
3. **文献名称**：*Functional analysis of a leucine-rich repeat receptor-like kinase in plant immunity*
**作者**：Zhang Y, et al.
**摘要**：通过重组表达植物源富含亮氨酸重复序列(LRR)的受体蛋白，揭示其通过识别病原体相关分子模式(PAMPs)激活免疫信号通路的分子机制。
4. **文献名称**：*Targeting LeuB for antimicrobial drug discovery against Staphylococcus aureus*
**作者**：Patel R, et al.
**摘要**：研究利用重组表达的葡萄球菌LeuB酶(3-异丙基苹果酸脱氢酶)筛选小分子抑制剂，发现多个化合物可阻断细菌亮氨酸生物合成途径，抑制病原体生长。
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以上示例覆盖重组蛋白的表达优化、结构工程、功能研究及药物开发应用，可根据实际研究方向进一步调整关键词和内容。
Leu recombinant proteins, often associated with leucine-rich motifs or leucine biosynthesis pathways, are engineered proteins produced using recombinant DNA technology. Leucine (Leu), an essential amino acid, plays critical roles in protein structure, metabolic regulation, and cellular signaling. Recombinant proteins incorporating leucine-rich domains, such as leucine zippers or leucine-rich repeats (LRRs), are widely studied for their ability to mediate protein-protein interactions, stabilize tertiary structures, or participate in molecular recognition processes (e.g., immune response or signal transduction).
The production of Leu recombinant proteins typically involves cloning target genes into expression vectors, followed by expression in host systems like *E. coli*, yeast, or mammalian cells. Optimization of codon usage or leucine supplementation may enhance yield, particularly for proteins requiring high leucine content. Such proteins are pivotal in structural biology for studying folding mechanisms and in drug development, where leucine-rich regions are targeted for therapeutic interventions (e.g., antibodies or enzyme inhibitors).
Additionally, Leu recombinant proteins are tools in metabolic engineering, especially in modifying microbial strains for leucine overproduction, which has industrial applications in food additives or bioplastics. Their role in mTOR signaling—a pathway regulated by leucine to modulate cell growth and autophagy—further highlights their biomedical relevance. Challenges include ensuring proper post-translational modifications in heterologous systems and minimizing aggregation in leucine-rich sequences. Overall, these proteins bridge fundamental research and biotechnological applications, underscoring the versatility of recombinant technology in addressing health and industrial needs.
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