纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | TARS |
Uniprot No | P26639 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-723aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW PEYIYTRLEM YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT TPYQIACGIS QGLADNTVIA KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE NGFYYDMYLE EGGVSSNDFS SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL NEKVNTPTTT VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP GSCFFLPKGA YIYNALIEFI RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE VEKELFALKP MNCPGHCLMF DHRPRSWREL PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL DFLRTVYSVF GFSFKLNLST RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI DLDPGCTLNK KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT ISETIERLQQ LKEFRSKQAE EEF |
预测分子量 | 86 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3篇与TARS(苏氨酰-tRNA合成酶)重组蛋白相关的研究文献摘要概括:
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1. **文献名称**:*Structural insights into the mechanism of human cytoplasmic threonyl-tRNA synthetase*
**作者**:Yang XL 等
**摘要内容**:该研究解析了人源TARS蛋白的晶体结构,并通过重组表达技术获得高纯度蛋白。研究发现其活性位点动态变化与底物识别相关,为设计靶向TARS的小分子抑制剂提供结构基础。
2. **文献名称**:*Autoantigen properties of human threonyl-tRNA synthetase in inflammatory arthritis*
**作者**:Howard OM 等
**摘要内容**:研究利用重组人源TARS蛋白,验证其在类风湿性关节炎患者血清中的自身抗体结合能力,揭示TARS可能通过激活炎性信号通路参与自身免疫疾病进展。
3. **文献名称**:*High-level expression and purification of recombinant human threonyl-tRNA synthetase for biochemical characterization*
**作者**:Guo M 等
**摘要内容**:文章优化了TARS在大肠杆菌中的重组表达与纯化条件,获得高活性蛋白,并分析其酶动力学参数,为后续功能研究和药物筛选提供可靠方法。
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以上文献涵盖TARS重组蛋白的结构解析、疾病关联机制及表达技术优化方向,均为领域内代表性研究。如需具体年份或期刊信息,可进一步补充关键词检索。
**Background of TARS Recombinant Protein**
TARS (Threonyl-tRNA Synthetase) is a critical enzyme in protein biosynthesis, responsible for catalyzing the attachment of threonine to its cognate tRNA during translation. Beyond its canonical role in maintaining translational fidelity, TARS has garnered attention for its non-canonical functions in various cellular processes, including immune regulation, angiogenesis, and apoptosis. Dysregulation of TARS has been implicated in diseases such as cancer, inflammatory disorders, and microbial infections, positioning it as a potential therapeutic target.
The development of recombinant TARS protein leverages genetic engineering to produce purified, functional enzyme in heterologous systems like *E. coli*, yeast, or mammalian cell cultures. Recombinant technology allows for scalable production, structural modifications, and enhanced stability, facilitating research into TARS’s mechanistic roles and interactions. For instance, studies using recombinant TARS have revealed its extracellular signaling capabilities in inflammation and its interaction with specific cytokines or cell-surface receptors.
In drug discovery, recombinant TARS serves as a tool for high-throughput screening of inhibitors, particularly for antimicrobial agents, as microbial TARS enzymes differ structurally from human counterparts. Additionally, engineered variants of TARS are explored for biocatalytic applications or as carriers for targeted drug delivery. Challenges remain in optimizing expression systems for proper post-translational modifications and minimizing immunogenicity in therapeutic contexts.
Overall, recombinant TARS exemplifies the convergence of structural biology, biotechnology, and translational medicine, offering insights into fundamental biological processes and paving the way for novel therapeutic strategies.
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