| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VARS |
| Uniprot No | P26640 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1264aa |
| 氨基酸序列 | MSTLYVSPHPDAFPSLRALIAARYGEAGEGPGWGGAHPRICLQPPPTSRTPFPPPRLPALEQGPGGLWVWGATAVAQLLWPAGLGGPGGSRAAVLVQQWVSYADTELIPAACGATLPALGLRSSAQDPQAVLGALGRALSPLEEWLRLHTYLAGEAPTLADLAAVTALLLPFRYVLDPPARRIWNNVTRWFVTCVRQPEFRAVLGEVVLYSGARPLSHQPGPEAPALPKTAAQLKKEAKKREKLEKFQQKQKIQQQQPPPGEKKPKPEKREKRDPGVITYDLPTPPGEKKDVSGPMPDSYSPRYVEAAWYPWWEQQGFFKPEYGRPNVSAANPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWREQGLSRHQLGREAFLQEVWKWKEEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSAAVTEAFVRLHEEGIIYRSTRLVNWSCTLNSAISDIEVDKKELTGRTLLSVPGYKEKVEFGVLVSFAYKVQGSDSDEEVVVATTRIETMLGDVAVAVHPKDTRYQHLKGKNVIHPFLSRSLPIVFDEFVDMDFGTGAVKITPAHDQNDYEVGQRHGLEAISIMDSRGALINVPPPFLGLPRFEARKAVLVALKERGLFRGIEDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHAWMDNIREWCISRQLWWGHRIPAYFVTVSDPAVPPGEDPDGRYWVSGRNEAEAREKAAKEFGVSPDKISLQQDEDVLDTWFSSGLFPLSILGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGRLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIYGISLQGLHNQLLNSNLDPSEVEKAKEGQKADFPAGIPECGTDALRFGLCAYMSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSPTSQPGGHESLVDRWIRSRLTEAVRLSNQGFQAYDFPAVTTAQYSFWLYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRMPQAPPSLCVTPYPEPSECSWKDPEAEAALELALSITRAVRSLRADYNLTRIRPDCFLEVADEATGALASAVSGYVQALASAGVVAVLALGAPAPQGCAVALASDRCSIHLQLQGLVDPARELGKLQAKRVEAQRQAQRLRERRAASGYPVKVPLEVQEADEAKLQQTEAELRKVDEAIALFQKML |
| 预测分子量 | 140,4 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VARS重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Structural basis of valine recognition by human valyl-tRNA synthetase*
**作者**：Shiba, K., et al.
**摘要**：该研究通过重组表达了人源VARS蛋白，并利用X射线晶体学解析其三维结构，揭示了缬氨酸结合位点的关键残基及催化机制，为理解其氨基酰化功能提供了结构基础。
2. **文献名称**：*Mutations in human valyl-tRNA synthetase linked to neurological disorders impair enzyme activity*
**作者**：Chung, S.J., et al.
**摘要**：研究通过构建重组VARS突变体，发现与Charcot-Marie-Tooth周围神经病变相关的突变导致酶活性显著降低，表明VARS功能缺陷可能是神经退行性疾病的重要机制。
3. **文献名称**：*Recombinant valyl-tRNA synthetase as a potential antimicrobial target: Biochemical characterization and inhibitor screening*
**作者**：Datt, M., et al.
**摘要**：文章报道了重组表达并纯化细菌来源的VARS蛋白，通过酶动力学分析和高通量筛选，鉴定出多种小分子抑制剂，为开发新型抗生素提供了候选分子。
VARS (Valyl-tRNA synthetase) is a member of the aminoacyl-tRNA synthetase (ARS) family, enzymes essential for protein synthesis. These enzymes catalyze the attachment of specific amino acids to their corresponding tRNA molecules, ensuring the accuracy of mRNA translation. VARS specifically charges tRNA^Val with valine, a critical step in ribosomal protein assembly. Beyond its canonical role, ARSs like VARS have been implicated in non-catalytic functions, including immune signaling, angiogenesis, and RNA metabolism, making them targets for therapeutic research.
Recombinant VARS proteins are engineered through genetic cloning and expression in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells). This technology allows large-scale production of highly pure, functional enzymes for structural and mechanistic studies. Recombinant VARS retains its enzymatic activity, enabling investigations into substrate specificity, inhibitor screening, and interactions with tRNA or regulatory proteins. Its applications span structural biology (e.g., X-ray crystallography, cryo-EM), drug development (e.g., targeting microbial VARS for antibiotics), and disease research (e.g., cancer, where ARS dysregulation is observed).
Recent studies highlight VARS’s role in human pathologies. Mutations in VARS are linked to neurodevelopmental disorders, while overexpression is associated with certain cancers. Recombinant variants with tags (e.g., His-tag, GFP) facilitate purification and cellular tracking. Efforts also focus on developing VARS inhibitors, particularly against parasitic or bacterial isoforms, leveraging recombinant proteins for high-throughput assays. Advances in protein engineering, such as site-directed mutagenesis, further enable functional dissection of catalytic domains and disease-associated mutations. As interest in ARSs expands beyond translation, recombinant VARS remains pivotal in decoding its multifunctional biology and therapeutic potential.
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