| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Aars1 |
| Uniprot No | Q8BGQ7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-968aa |
| 氨基酸序列 | MDATLTAREIRERFINFFRRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPSHPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALELLTQEFGIPVERLYVTYFGGDEAAGLEPDLECRQIWQNLGLDEARILPGNMKDNFWEMGDTGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNRESDGVLKPLPKKSIDTGMGLERLVSVLQNKMSNYDTDLFMPYFEAIQKGTGARPYTGKVGAEDADGIDMAYRVLADHARTITVALADGGRPDNTGRGYVLRRILRRAVRYSHEKLNASRGFFATLVDVVVQSLGDAFPELKKDPEMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDCKTIPGDTAWLLYDTYGFPVDLTGLIAEEKGLVVDMNGFEEERRLAQLKSQGKGAGDEDLIMLDIYAIEELRAKGLEATDDSPKYNYQSDSSGSYVFECTVATVLALRREKMFVDEVVTGQECGVVLDKTCFYAEQGGQIYDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGNLKVGDQVRLFIDEPRRRPVMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIVNGMIEAAKPVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPCGPAGSLTSVEFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKSETLKKSLSAMEAKVKAQTAPNKDVQREIADLGEALATAVIPQWQKDEQRETLKSLKKVMDDLDRASKADVQKRVLEKTKQLIDSNPNQPLVILEMESGASAKALNEALKLFKTHSPQTSAMLFTVDNEAGKITCLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDMSAQATGKNVGCLQEALQLATSFAQLRLGDVKN |
| 预测分子量 | 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Aars1重组蛋白的参考文献示例(注：以下内容为模拟示例，文献信息非真实存在)：
1. **《重组Aars1蛋白在大肠杆菌中的高效表达与功能鉴定》**
*作者：Smith J, et al.*
摘要：本研究成功在大肠杆菌中表达了重组Aars1蛋白，通过优化诱导条件提高了可溶性表达水平，并利用镍柱亲和层析纯化获得高纯度蛋白。酶活性实验证实重组Aars1具有丙氨酰-tRNA合成活性，为后续功能研究奠定了基础。
2. **《AARS1突变体的重组表达及其在Charcot-Marie-Tooth病中的致病机制分析》**
*作者：Lee S, et al.*
摘要：通过构建AARS1致病突变体的重组蛋白，发现部分突变导致酶催化活性显著下降，并影响tRNA结合能力。该研究揭示了AARS1突变通过干扰蛋白质合成导致周围神经病变的分子机制。
3. **《人源Aars1的晶体结构解析及其底物识别机制》**
*作者：Zhang Y, et al.*
摘要：利用重组表达的人源Aars1蛋白进行结晶和X射线衍射分析，首次报道了其全长三维结构，明确了ATP和丙氨酸结合的关键结构域，为设计靶向抑制剂提供了结构依据。
4. **《基于重组Aars1蛋白的抗真菌药物筛选平台开发》**
*作者：Johnson R, et al.*
摘要：建立了一种以重组真菌Aars1蛋白为靶点的高通量筛选体系，成功鉴定出多个抑制酶活性的小分子化合物，为抗真菌药物研发提供了新策略。
(注：如需真实文献，建议通过PubMed或Web of Science以“Alanyl-tRNA synthetase recombinant”或“AARS1 recombinant protein”为关键词检索。)
**Background of Aars1 Recombinant Protein**
Aars1 (Alanyl-tRNA Synthetase 1) is a member of the aminoacyl-tRNA synthetase (aaRS) family, enzymes essential for protein synthesis. It catalyzes the attachment of alanine to its cognate tRNA (tRNA^Ala) during translation, ensuring the accurate incorporation of amino acids into growing polypeptide chains. As a class II aaRS, Aars1 possesses a conserved catalytic domain for adenylate formation and tRNA recognition, along with unique structural motifs that contribute to substrate specificity and editing functions.
Recombinant Aars1 protein is produced through heterologous expression systems (e.g., *E. coli* or mammalian cell lines), enabling high-purity, functional studies. Its recombinant form retains enzymatic activity, making it valuable for *in vitro* assays, structural biology (e.g., X-ray crystallography), and drug discovery targeting translational machinery.
Beyond its canonical role, Aars1 has been implicated in non-canonical pathways, including inflammation, angiogenesis, and cellular stress responses. Mutations in the *AARS1* gene are linked to rare neurological disorders, such as Charcot-Marie-Tooth disease, highlighting its importance in neuronal health. Dysregulation of Aars1 is also observed in cancers, where altered tRNA synthetase activity may drive tumor progression.
Research on recombinant Aars1 aids in understanding disease mechanisms, developing therapeutic inhibitors, and exploring tRNA synthetases as biomarkers. Its versatility as a tool continues to advance both basic and applied biomedical research.
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