| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Iars1 |
| Uniprot No | P41252 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1262aa |
| 氨基酸序列 | MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHILAGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQCRAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMPFSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNPEMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCKENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTTEVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVENMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVCIGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHYPFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQKMSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAYRFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVVPRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELMYQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKTIPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMVLGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQFEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGTYLNSVIESHTEFIFTTIKAPLKPYPVSPSDKVLIQEKTQLKGSELEITLTRGSSLPGPACAYVNLNICANGSEQGGVLLLENPKGDNRLDLLKLKSVVTSIFGVKNTELAVFHDETEIQNQTDLLSLSGKTLCVTAGSAPSLINSSSTLLCQYINLQLLNAKPQECLMGTVGTLLLENPLGQNGLTHQGLLYEAAKVFGLRSRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTADF |
| 预测分子量 | 145kDa |
| 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IARS1重组蛋白的3篇文献示例(内容基于公开研究趋势，建议通过学术数据库验证原文)：
---
1. **文献名称**：*Crystal structure of human cytosolic isoleucyl-tRNA synthetase (IARS1) in complex with isoleucyl-adenylate*
**作者**：Park SG, et al.
**摘要**：解析了人源IARS1重组蛋白的晶体结构，揭示了其催化结构域与异亮氨酰-腺苷酸复合物的结合模式，为研究氨酰-tRNA合成酶的催化机制提供结构基础。
2. **文献名称**：*IARS1 regulates cell proliferation through mTORC1 signaling in response to amino acid availability*
**作者**：Kim JH, et al.
**摘要**：研究证明重组IARS1蛋白可通过感知氨基酸水平调控mTORC1信号通路，影响细胞增殖，提示其在代谢应激中的生物学功能。
3. **文献名称**：*Recombinant IARS1 promotes tumorigenesis in colorectal cancer via modulating Wnt/β-catenin pathway*
**作者**：Zhang Y, et al.
**摘要**：通过体外重组IARS1蛋白实验，发现其过表达激活Wnt/β-catenin通路，促进结直肠癌细胞侵袭，表明其作为潜在肿瘤治疗靶点。
---
**备注**：以上文献信息为示例性质，实际研究中需通过PubMed、Web of Science等平台检索具体论文。IARS1研究多聚焦于其在翻译调控、代谢疾病及癌症中的作用，重组蛋白技术常用于其功能与机制解析。
IARS1 (Isoleucyl-tRNA Synthetase 1) is a mitochondrial enzyme belonging to the class I aminoacyl-tRNA synthetase (aaRS) family. It catalyzes the attachment of isoleucine to its cognate tRNA (tRNA^Ile) during mitochondrial protein synthesis, a critical step in maintaining translational fidelity and supporting oxidative phosphorylation. Unlike its cytosolic counterpart (IARS2), IARS1 is nuclear-encoded but functions exclusively in mitochondria, reflecting the evolutionary origin of mitochondrial translation machinery.
Mutations in IARS1 have been linked to mitochondrial disorders, particularly those affecting energy-demanding tissues like the nervous system and muscles. Studies suggest that impaired IARS1 activity disrupts mitochondrial translation, leading to defective electron transport chain complexes and cellular energy deficits. Its role in metabolic homeostasis has also drawn attention in cancer research, as some tumors exhibit altered IARS1 expression to adapt to metabolic reprogramming.
Recombinant IARS1 protein is typically produced in bacterial (e.g., E. coli) or eukaryotic expression systems for structural and functional studies. Structural analyses using recombinant IARS1 have revealed conserved catalytic domains and unique mitochondrial-targeting sequences. Researchers employ it to investigate enzyme kinetics, substrate specificity, and interactions with tRNA or regulatory proteins. Therapeutic applications are being explored, including high-throughput screening for small-molecule modulators to correct pathogenic mutations or target cancer-specific isoforms.
Challenges in working with recombinant IARS1 include maintaining proper post-translational modifications and solubility due to its large size (>1.000 amino acids). Recent advances in cryo-EM and gene-editing tools have accelerated mechanistic studies, positioning IARS1 as a focal point for understanding mitochondrial pathologies and developing precision therapies.
×
