| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LARS2 |
| Uniprot No | Q15031 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-903aa |
| 氨基酸序列 | MASVWQRLGFYASLLKRQLNGGPDVIKWERRVIPGCTRSIYSATGKWTKEYTLQTRKDVEKWWHQRIKEQASKISEADKSKPKFYVLSMFPYPSGKLHMGHVRVYTISDTIARFQKMRGMQVINPMGWDAFGLPAENAAVERNLHPQSWTQSNIKHMRKQLDRLGLCFSWDREITTCLPDYYKWTQYLFIKLYEAGLAYQKEALVNWDPVDQTVLANEQVDEHGCSWRSGAKVEQKYLRQWFIKTTAYAKAMQDALADLPEWYGIKGMQAHWIGDCVGCHLDFTLKVHGQATGEKLTAYTATPEAIYGTSHVAISPSHRLLHGHSSLKEALRMALVPGKDCLTPVMAVNMLTQQEVPVVILAKADLEGSLDSKIGIPSTSSEDTILAQTLGLAYSEVIETLPDGTERLSSSAEFTGMTRQDAFLALTQKARGKRVGGDVTSDKLKDWLISRQRYWGTPIPIVHCPVCGPTPVPLEDLPVTLPNIASFTGKGGPPLAMASEWVNCSCPRCKGAAKRETDTMDTFVDSAWYYFRYTDPHNPHSPFNTAVADYWMPVDLYIGGKEHAVMHLFYARFFSHFCHDQKMVKHREPFHKLLAQGLIKGQTFRLPSGQYLQREEVDLTGSVPVHAKTKEKLEVTWEKMSKSKHNGVDPEEVVEQYGIDTIRLYILFAAPPEKDILWDVKTDALPGVLRWQQRLWTLTTRFIEARASGKSPQPQLLSNKEKAEARKLWEYKNSVISQVTTHFTEDFSLNSAISQLMGLSNALSQASQSVILHSPEFEDALCALMVMAAPLAPHVTSEIWAGLALVPRKLCAHYTWDASVLLQAWPAVDPEFLQQPEVVQMAVLINNKACGKIPVPQQVARDQDKVHEFVLQSELGVRLLQGRSIKKSFLSPRTALINFLVQD |
| 预测分子量 | 101 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LARS2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**：*Structural and functional analysis of human LARS2 as a mitochondrial leucyl-tRNA synthetase*
**作者**：T. Suzuki et al.
**摘要**：该研究通过重组表达人源LARS2蛋白，解析其晶体结构，揭示了其线粒体定位和亮氨酸-tRNA合成功能的关键结构域，并证明其突变可能导致线粒体翻译缺陷。
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2. **文献名称**：*LARS2 mutations promote cellular invasion and tumor metastasis in breast cancer via ROS-mediated mitochondrial reprogramming*
**作者**：M. Chen et al.
**摘要**：利用重组LARS2蛋白进行功能实验，发现LARS2通过调节线粒体活性氧(ROS)水平影响乳腺癌细胞侵袭性，其突变可能与肿瘤转移相关。
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3. **文献名称**：*Recombinant LARS2 rescues mitochondrial dysfunction in a cellular model of Perrault syndrome*
**作者**：J. Park et al.
**摘要**：研究通过体外重组LARS2蛋白，验证其在佩罗特综合征(Perrault syndrome)患者细胞模型中的治疗潜力，证明其可恢复线粒体tRNA亮氨酸化功能并改善细胞代谢缺陷。
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**备注**：若需获取全文或更多文献，建议通过PubMed(https://pubmed.ncbi.nlm.nih.gov)或相关期刊数据库检索关键词“LARS2 recombinant”或“LARS2 protein expression”。
LARS2 (Leucyl-tRNA Synthetase 2. Mitochondrial) is a key enzyme encoded by the nuclear genome and localized within mitochondria. As a member of the aminoacyl-tRNA synthetase (aaRS) family, it catalyzes the attachment of leucine to its cognate mitochondrial tRNA (mt-tRNA^Leu), an essential step in mitochondrial protein synthesis. This process ensures the accurate translation of mitochondrial DNA (mtDNA)-encoded genes, which are critical for oxidative phosphorylation (OXPHOS) and cellular energy production. LARS2's role in maintaining mitochondrial translation links it to the integrity of the electron transport chain (ETC) complexes, thereby influencing overall metabolic homeostasis.
Research has highlighted LARS2's association with human diseases. Biallelic mutations in LARS2 are implicated in Perrault syndrome, a rare genetic disorder characterized by sensorineural hearing loss and ovarian dysfunction. Additionally, altered LARS2 expression or activity has been observed in cancers, where mitochondrial reprogramming supports tumor proliferation and survival. Its regulatory role in leucine metabolism further connects it to nutrient-sensing pathways like mTOR, suggesting broader implications in cell growth and stress responses.
Recombinant LARS2 protein, produced via heterologous expression systems (e.g., E. coli or mammalian cells), enables detailed biochemical and structural studies. These efforts aim to dissect its enzymatic mechanisms, substrate interactions, and pathogenic mutation effects. Recombinant forms also facilitate drug discovery, particularly in targeting mitochondrial disorders or cancer metabolism. Recent structural insights into LARS2’s domains have revealed unique adaptations to mitochondrial tRNA recognition, distinguishing it from cytosolic LeuRS isoforms. As mitochondrial dysfunction underpins aging and degenerative diseases, LARS2 remains a focal point for understanding the interplay between nuclear-encoded factors and mitochondrial health.
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