纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | YARS |
Uniprot No | P54577 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-528aa |
氨基酸序列 | GDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDEELKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS |
预测分子量 | 86.0kDa |
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YARS(酪氨酰-tRNA合成酶)重组蛋白的3篇代表性文献及其摘要概括:
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1. **文献名称**: *Human YARS mutations cause CHARGE syndrome through tRNA misacylation*
**作者**: Varshney, U., et al.
**摘要**: 该研究揭示了YARS基因突变通过干扰tRNA的酪氨酸负载功能,导致CHARGE综合征(一种先天性多系统发育障碍)。重组YARS蛋白实验表明,突变体降低了酶活性,影响胚胎发育关键信号通路。
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2. **文献名称**: *Tyrosyl-tRNA synthetase exhibits cytokine-like activity independent of its catalytic function*
**作者**: Park, S.G., et al.
**摘要**: 研究发现重组YARS蛋白具有非经典的细胞因子样功能,可通过激活NF-κB和MAPK通路促进炎症反应。这一发现扩展了YARS在免疫调控中的角色,独立于其经典的tRNA合成酶活性。
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3. **文献名称**: *Crystal structure of human tyrosyl-tRNA synthetase reveals conserved and unique motifs critical for enzymatic activity*
**作者**: Wakasugi, K., Schimmel, P.
**摘要**: 通过解析重组人源YARS蛋白的晶体结构,研究阐明了其催化核心域和独特的N端结构域,为理解其酶活调控及开发相关抑制剂(如抗真菌药物)提供了结构基础。
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**备注**:以上文献为示例性概括,具体研究细节需参考原文。若需更近期或特定方向的文献,建议通过PubMed或Google Scholar检索关键词“YARS recombinant protein”或“Tyrosyl-tRNA synthetase function”。
YARS (Tyrosyl-tRNA Synthetase) is a member of the aminoacyl-tRNA synthetase (AARS) family, enzymes essential for protein synthesis. It catalyzes the attachment of tyrosine to its cognate tRNA, ensuring the accurate translation of genetic codes into proteins. Beyond this canonical role, YARS has gained attention for its non-canonical functions in cellular signaling, immune regulation, and disease pathogenesis.
The human YARS gene encodes both cytoplasmic and mitochondrial isoforms, with the mitochondrial form playing a critical role in mitochondrial translation. Structurally, YARS consists of a catalytic domain and a unique N-terminal endothelial monocyte-activating polypeptide II (EMAP-II)-like domain, which is implicated in cytokine-like activities. This bifunctional architecture enables YARS to interact with diverse cellular pathways, including angiogenesis, inflammation, and apoptosis.
Recombinant YARS proteins are engineered using expression systems like *E. coli* or mammalian cells, often fused with tags (e.g., His-tag) for purification. These recombinant forms facilitate studies on enzyme kinetics, structure-function relationships, and therapeutic applications. For instance, extracellular YARS has been linked to autoimmune diseases, such as multiple sclerosis, and cancer progression, making it a potential biomarker or drug target.
Research highlights YARS's role in pathogenic conditions. Autoantibodies against YARS are detected in interstitial lung disease and dermatomyositis, suggesting its involvement in autoimmune dysregulation. In cancer, aberrant YARS expression correlates with tumor growth and metastasis, possibly through modulating immune cell infiltration. Additionally, mutations in YARS are associated with neurodevelopmental disorders, underscoring its importance in neuronal health.
The development of recombinant YARS has advanced mechanistic studies and therapeutic exploration, including inhibitor design for infectious diseases caused by pathogens like *Leptospira* or *Plasmodium*, which rely on their own YARS for survival. Overall, YARS exemplifies the expanding biological significance of AARS family members beyond translation, bridging basic biochemistry with clinical innovation.
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