| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TARS2 |
| Uniprot No | Q9BW92 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 369-718aa |
| 氨基酸序列 | EHYQEDMFAVQPPGSDRPPSSQSDDSTRHITDTLALKPMNCPAHCLMFAHRPRSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLRSVYAVLGFSFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGQAGALERPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDADSGLTLSRRIRRAQLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTRVPNAEEIF |
| 预测分子量 | 55.3 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TARS2重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Recombinant expression and functional characterization of human mitochondrial threonyl-tRNA synthetase*
**作者**：Park, S. G., et al.
**摘要**：本研究报道了人源线粒体TARS2蛋白在大肠杆菌中的重组表达及纯化方法，并验证了其氨基酰化活性。通过体外实验证实重组TARS2对线粒体tRNA的识别特异性，为研究其突变相关神经疾病提供了工具。
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2. **文献名称**：*Structural insights into the pathogenicity of TARS2 mutations in mitochondrial encephalopathy*
**作者**：Zhang, Y., et al.
**摘要**：作者利用重组TARS2蛋白解析了其晶体结构，揭示了致病性突变(如p.Arg336Cys)对酶活性中心的影响，阐明了突变导致线粒体翻译缺陷的分子机制。
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3. **文献名称**：*A high-throughput screening assay for TARS2 inhibitors using recombinant protein-based fluorescence polarization*
**作者**：Kim, J., & Lee, C.
**摘要**：开发了一种基于重组TARS2蛋白的荧光偏振高通量筛选方法，用于发现靶向该酶的抑制剂，为治疗与TARS2过表达相关的癌症提供了潜在策略。
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4. **文献名称**：*Functional analysis of TARS2 variants associated with pontocerebellar hypoplasia using a recombinant yeast model*
**作者**：Gonzalez, M., et al.
**摘要**：通过酵母异源表达系统重组TARS2蛋白，验证了多个临床突变体(如p.Leu156Pro)对细胞生长的挽救能力，证明其功能丧失与神经发育障碍的直接关联。
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**注**：以上文献为示例性内容，实际文献需通过数据库(如PubMed、Web of Science)以关键词“TARS2 recombinant”“threonyl-tRNA synthetase expression”检索获取。若需具体文献，建议补充年份或研究领域进一步筛选。
**Background of TARS2 Recombinant Protein**
TARS2. or threonyl-tRNA synthetase 2. is a mitochondrial enzyme encoded by the nuclear *TARS2* gene. It belongs to the family of aminoacyl-tRNA synthetases (aaRSs), which play a critical role in protein synthesis by catalyzing the attachment of specific amino acids to their corresponding transfer RNAs (tRNAs). Specifically, TARS2 charges tRNA^Thr with threonine, ensuring the accurate incorporation of this amino acid into mitochondrial proteins during translation.
Mutations in *TARS2* have been linked to mitochondrial disorders, such as combined oxidative phosphorylation deficiency (COXPD21), characterized by neurological impairments, developmental delays, and metabolic dysfunction. This association highlights TARS2's essential role in mitochondrial function and energy production.
Recombinant TARS2 protein is engineered through genetic engineering techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic (e.g., mammalian or insect cell) systems. The recombinant form allows researchers to study the enzyme's structure, catalytic mechanisms, and interaction with substrates or inhibitors in controlled settings. It also serves as a tool for investigating disease-related mutations, enabling structure-function analyses to pinpoint molecular defects underlying mitochondrial pathologies.
Beyond basic research, TARS2 recombinant protein has potential therapeutic applications. For instance, it could support gene therapy strategies aimed at restoring enzyme activity in patients with *TARS2* mutations. Additionally, it may aid in high-throughput drug screening to identify compounds that modulate TARS2 activity or stabilize dysfunctional variants.
Despite its utility, challenges remain in producing stable, functional recombinant TARS2 due to its complex post-translational modifications and mitochondrial localization signals. Ongoing research focuses on optimizing expression systems and purification protocols to enhance yield and activity, paving the way for deeper insights into mitochondrial biology and novel treatment avenues.
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