| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | lprG |
| Uniprot No | P9WK44 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-236aa |
| 氨基酸序列 | CSSGSKPSGGPLPDAKPLVEEATAQTKALKSAHMVLTVNGKIPGLSLKTLSGDLTTNPTAATGNVKLTLGGSDIDADFVVFDGILYATLTPNQWSDFGPAADIYDPAQVLNPDTGLANVLANFADAKAEGRDTINGQNTIRISGKVSAQAVNQIAPPFNATQPVPATVWIQETGDHQLAQAQLDRGSGNSVQMTLSKWGEKVQVTKPPVS |
| 预测分子量 | 29.2 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 **lprG重组蛋白** 的3篇参考文献的简要总结(基于公开研究数据，部分信息需结合具体文献验证)：
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1. **文献名称**: *"Mycobacterium tuberculosis LprG (Rv1411c): A Novel TLR2 Ligand That Inhibits Human Macrophage Class II MHC Antigen Processing"*
**作者**: Drage MG, et al.
**摘要**: 研究揭示了结核分枝杆菌LprG蛋白通过与宿主TLR2受体相互作用，抑制巨噬细胞MHC II类抗原呈递通路，从而帮助病原体逃避免疫清除的机制。重组LprG蛋白的纯化与功能分析表明其具有免疫调节特性。
2. **文献名称**: *"Structure of Rv1411c (LprG) from Mycobacterium tuberculosis: A Small Protein with a Fold Unique to Pathogenic Mycobacteria"*
**作者**: Sulzenbacher G, et al.
**摘要**: 通过X射线晶体学解析了LprG蛋白的三维结构，发现其具有独特的α-螺旋折叠模式，并推测其与病原菌脂质代谢相关。重组蛋白的表达与结构分析为研究其在结核病发病机制中的作用提供了基础。
3. **文献名称**: *"LprG-Mediated Surface Expression of Lipoarabinomannan in Mycobacterium tuberculosis"*
**作者**: Sani M, et al.
**摘要**: 研究表明，LprG重组蛋白通过与脂阿拉伯甘露聚糖(LAM)结合，促进其在细菌表面的定位，进而影响宿主免疫识别。该研究利用重组蛋白技术揭示了LprG在结核分枝杆菌细胞壁组装中的关键作用。
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如需获取全文或更多文献，建议通过 **PubMed/Google Scholar** 搜索关键词：**"LprG recombinant protein Mycobacterium"** 或 **"Rv1411c tuberculosis"**。
**Background of LprG Recombinant Protein**
LprG is a lipoprotein encoded by the *lprG* gene in *Mycobacterium tuberculosis* (Mtb), the causative agent of tuberculosis (TB). It belongs to the Proline-Glutamate (PE)/Proline-Proline-Glutamate (PPE) protein family, a group of mycobacteria-specific proteins associated with host-pathogen interactions, immune modulation, and virulence. LprG shares homology with LprA, another Mtb lipoprotein, and both are implicated in lipid transport and immune evasion.
Structurally, LprG contains a lipid anchor and a conserved N-terminal domain, enabling interactions with host cell receptors like Toll-like receptor 2 (TLR2). Studies suggest LprG acts as a chaperone for mycobacterial cell wall components, particularly trehalose dimycolate (TDM) and mycolic acids, facilitating their transport to the outer membrane. This interaction is critical for Mtb’s cell envelope integrity and pathogenicity.
Recombinant LprG protein is produced via heterologous expression systems (e.g., *E. coli*) for functional and immunological studies. Its recombinant form allows researchers to dissect its role in Mtb’s immune evasion mechanisms, such as suppressing pro-inflammatory cytokine production or modulating macrophage apoptosis. Additionally, LprG recombinant protein serves as a tool for diagnostic antigen screening or vaccine development, given its immunogenicity in host immune responses.
Recent research highlights LprG’s potential as a therapeutic target, as inhibitors disrupting LprG-lipid interactions could impair Mtb survival. However, its exact mechanisms and interplay with other virulence factors remain under investigation. Understanding LprG’s biology through recombinant protein studies is vital for advancing TB diagnostics, vaccines, and targeted therapies against drug-resistant strains.
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