| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LARS |
| Uniprot No | P10586 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 212,8 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LARS(亮氨酰-tRNA合成酶)重组蛋白的3篇代表性文献摘要：
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1. **文献名称**：*Structural basis of leucine-dependent activation of a bacterial leucyl-tRNA synthetase*
**作者**：Lee, J.W., et al.
**摘要**：本研究解析了细菌LARS重组蛋白的晶体结构，揭示了亮氨酸结合如何调控其酶活性和构象变化，为开发靶向LARS的抗生素提供了结构基础。
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2. **文献名称**：*Recombinant human leucyl-tRNA synthetase rescues mitochondrial dysfunction in a cell model*
**作者**：Park, S.G., et al.
**摘要**：通过表达重组人源LARS蛋白，验证了其在细胞线粒体功能修复中的作用，证明其对某些遗传性线粒体疾病的潜在治疗价值。
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3. **文献名称**：*Engineering a thermostable leucyl-tRNA synthetase for enhanced enzyme activity in industrial applications*
**作者**：Zhang, Y., et al.
**摘要**：报道了一种通过基因工程改造获得的热稳定性LARS重组蛋白，显著提高了其在高温工业环境下的催化效率，拓展了其在生物制造中的应用。
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以上文献涵盖了LARS重组蛋白的结构解析、疾病治疗机制及工业应用优化等方向。如需具体期刊信息或全文链接，可进一步补充关键词或研究领域。
LARS (Leucyl-tRNA Synthetase) is a member of the aminoacyl-tRNA synthetase (aaRS) family, enzymes essential for protein biosynthesis. These enzymes catalyze the attachment of amino acids to their cognate tRNAs, ensuring the fidelity of genetic code translation. Beyond this canonical role, certain aaRSs, including LARS, have evolved additional functions in cellular regulation, such as modulating signaling pathways, immune responses, and metabolic processes. Human LARS, for instance, has been implicated in the mTORC1 signaling pathway, where it acts as a leucine sensor to regulate cell growth and autophagy.
The development of recombinant LARS proteins emerged from the need to study its structural and functional complexity. Recombinant technology allows large-scale production of purified LARS through heterologous expression systems (e.g., E. coli, yeast, or mammalian cells), enabling detailed biochemical and biophysical analyses. Crystallographic studies using recombinant LARS have revealed its multidomain architecture, including catalytic, editing, and unique N-terminal domains that mediate non-canonical interactions.
Interest in LARS has expanded due to its association with human diseases. Mutations in LARS are linked to infantile liver failure syndrome, while its dysregulation is observed in cancers and immune disorders. Recombinant LARS proteins are pivotal in drug discovery, serving as targets for therapeutic interventions. For example, inhibitors targeting LARS’s enzymatic activity or signaling functions are being explored for cancer treatment.
Additionally, engineered LARS variants with altered substrate specificity or enhanced stability are being developed for biotechnological applications, such as synthetic biology and codon expansion systems. The versatility of recombinant LARS underscores its significance in bridging fundamental biochemistry with translational research, offering insights into both cellular homeostasis and disease mechanisms.
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