| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IARS |
| Uniprot No | P41252 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 693-852aa |
| 氨基酸序列 | DRWILSFMQSLIGFFETEMAAYRLYTVVPRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELMYQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKTIPIKYPLKEIVV |
| 预测分子量 | 26.3 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IARS重组蛋白的参考文献示例(注：以下内容为基于学术文献常见主题的模拟描述，实际文献需通过数据库验证):
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1. **标题**: *Heterologous Expression and Characterization of Recombinant Isoleucyl-tRNA Synthetase from Escherichia coli*
**作者**: Smith J, et al.
**摘要**: 该研究报道了大肠杆菌IARS基因的克隆及在原核表达系统中的重组表达，通过亲和层析纯化获得高纯度蛋白，并验证了其催化异亮氨酸与tRNA结合的酶活性，为后续酶学机制研究奠定基础。
2. **标题**: *Crystal Structure Analysis of Human IARS Reveals Conformational Changes During Catalysis*
**作者**: Lee S, et al.
**摘要**: 作者利用重组表达的人源IARS蛋白进行结晶，通过X射线衍射解析其三维结构，揭示了ATP结合域和底物识别区的构象变化，阐明了IARS在蛋白质合成中的动态调控机制。
3. **标题**: *Functional Role of IARS in Inflammatory Signaling Pathways*
**作者**: Zhang Y, et al.
**摘要**: 研究通过体外重组IARS蛋白与免疫细胞共培养实验，发现IARS可通过调控NF-κB通路增强炎症因子释放，提示其在自身免疫疾病中的潜在治疗靶点价值。
4. **标题**: *Development of an IARS Inhibitor Screening Platform Using Purified Recombinant Protein*
**作者**: Tanaka K, et al.
**摘要**: 构建基于重组IARS蛋白的高通量药物筛选体系，鉴定出多个小分子抑制剂，为针对耐药菌的氨基酰-tRNA合成酶靶向抗生素开发提供新策略。
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**建议**：实际文献检索可通过PubMed或SciHub输入关键词“IARS recombinant”“Isoleucyl-tRNA Synthetase expression”获取。部分相关真实文献可能包括：
- Park SG et al. (2005) *Human IARS as a potential biomarker...*
- Kim JY et al. (2012) *Crystallographic analysis of bacterial IARS...*
IARS (Isoleucyl-tRNA synthetase) is a member of the aminoacyl-tRNA synthetase (AaRS) family, enzymes essential for protein synthesis. It catalyzes the attachment of isoleucine to its cognate tRNA, ensuring fidelity in the genetic code translation process. Beyond its canonical role, IARS has been implicated in non-canonical functions, including signaling pathways, inflammation regulation, and immune responses. Dysregulation of IARS is linked to human diseases, such as mitochondrial disorders, neurological pathologies, and certain cancers.
Recombinant IARS proteins are engineered using expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to study its structure, function, and interactions. These proteins retain enzymatic activity and structural integrity, enabling research into post-translational modifications, substrate binding mechanisms, and inhibitor screening. Recombinant technology allows site-directed mutagenesis to explore disease-associated variants or engineer thermostable/active mutants for industrial applications.
In therapeutic contexts, recombinant IARS serves as a target for drug development. For example, inhibitors of bacterial IARS are explored as antibiotics, leveraging species-specific structural differences. In autoimmune diseases, autoantibodies against IARS (e.g., anti-Jo-1 in antisynthetase syndrome) highlight its immunogenic potential, driving biomarker discovery. Additionally, mitochondrial IARS variants are studied for roles in tissue-specific metabolic disorders.
Advances in structural biology (e.g., cryo-EM, X-ray crystallography) using recombinant IARS have resolved conformational dynamics, aiding rational drug design. Challenges include maintaining solubility and post-translational modifications in heterologous systems. Overall, recombinant IARS bridges basic science and translational applications, offering insights into both fundamental biology and therapeutic innovation.
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