| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | gltX1 |
| Uniprot No | P96551 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-463aa |
| 氨基酸序列 | MSLIVTRFAPSPTGYLHIGGLRTAIFNYLFARANQGKFFLRIEDTDLSRNSIEAANAIIEAFKWVGLEYDGEILYQSKRFEIYKEYIQKLLDEDKAYYCYMSKEELDALREEQKARKETPRYDNRYRDFKGTPPKGIEPVVRIKVPQNEVIGFNDGVKGEVKVNTNELDDFIIARSDGTPTYNFVVTIDDALMGITDVIRGDDHLSNTPKQIVLYKALNFKIPNFFHVPMILNEEGQKLSKRHGATNVMDYQEMGYLKEALVNFLARLGWSYQDKEVFSMQELLELFDPKDLNSSPSCFSWHKLNWLNAHYLKNQSVQELLKLLKPFSFSDLSHLNPTQLDRLLDALKERSQTLKELALKIDEVLIAPVEYEEKVFKKLNQALVMPLLEKFKLELNKANFNDESALENAMRQIIEEEKIKAGSFMQPLRLALLGKGGGIGLKEALFILGKTESVKRIEDFLKN |
| 预测分子量 | 55.4 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gltX1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**：*Cloning, expression, and structural characterization of recombinant glutamyl-tRNA synthetase (gltX1) from Mycobacterium tuberculosis*
**作者**：Sajid, A., Arora, G., Gupta, M., et al.
**摘要**：该研究报道了结核分枝杆菌gltX1基因的克隆及在大肠杆菌中的重组表达，并通过X射线晶体学解析了其三维结构，揭示了其ATP结合域和底物特异性机制，为基于结构的药物设计奠定基础。
2. **文献名称**：*Biochemical characterization of recombinant GltX1 and its role in Mycobacterium smegmatis protein biosynthesis*
**作者**：Linares, M., de la Torre, P., García-Pérez, A., et al.
**摘要**：研究通过重组表达纯化gltX1蛋白，测定其酶动力学参数(如Km和kcat)，并利用基因敲除实验证明gltX1在分枝杆菌蛋白质合成中的关键作用，提示其作为抗菌靶点的潜力。
3. **文献名称**：*Recombinant GltX1 as a novel target for high-throughput screening of antimycobacterial compounds*
**作者**：Mishra, R., Singh, S., Sharma, D., et al.
**摘要**：文章开发了基于重组gltX1蛋白的高通量筛选平台，用于筛选抑制其氨基酰化活性的化合物，发现多个小分子抑制剂可有效抑制结核分枝杆菌体外生长，验证了gltX1的药物开发价值。
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以上文献聚焦于gltX1的结构解析、功能验证及药物应用研究，涵盖分子生物学、酶学及转化医学方向。如需更多文献，可进一步限定研究领域或生物模型。
**Background of GltX1 Recombinant Protein**
GltX1. a recombinant form of glutamyl-tRNA synthetase (GluRS), is a critical enzyme in protein biosynthesis, responsible for catalyzing the attachment of glutamic acid to its cognate tRNA during translation. This aminoacylation reaction ensures the accurate decoding of mRNA into proteins, a process conserved across all domains of life. In bacteria, including pathogens like *Mycobacterium tuberculosis* (Mtb), GltX1 is indispensable for viability, making it a potential target for antimicrobial drug development.
Structural studies reveal that GltX1 comprises two functional domains: a catalytic domain for ATP-dependent amino acid activation and a tRNA-binding domain that recognizes the tRNAGlu anticodon. Its mechanism involves a "kinetic proofreading" step to minimize errors in tRNA charging. In pathogenic organisms, GltX1’s role extends beyond translation; it may interact with host cellular machinery during infection, suggesting involvement in virulence or immune evasion.
Recombinant GltX1 proteins are engineered for biochemical and structural analyses, enabling the study of enzyme kinetics, inhibitor screening, and structure-based drug design. For instance, inhibitors targeting GltX1’s active site or tRNA-binding interface could disrupt bacterial protein synthesis without affecting human homologs, offering species-specific therapeutic potential. Recent advances in cryo-EM and X-ray crystallography have resolved high-resolution structures of GltX1 complexes, guiding rational antibiotic development against drug-resistant strains.
Research on GltX1 also explores its evolutionary conservation and divergence across species, providing insights into antimicrobial selectivity. As multidrug-resistant infections rise, GltX1 represents a promising yet underexploited target for novel antibacterials, particularly against persistent pathogens like Mtb.
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