| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | hspX |
| Uniprot No | P0A5B8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-144aa |
| 氨基酸序列 | ATTLPVQRHPRSLFPEFSELFAAFPSFAGLRPTFDTRLMRLEDEMKEGRYEVRAELPGVDPDKDVDIMVRDGQLTIKAERTEQKDFDGRSEFAYGSFVRTVSLPVGADEDDIKATYDKGILTVSVAVSEGKPTEKHIQIRSTN |
| 预测分子量 | 18.1 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3篇关于 **hspX(Rv2031c)重组蛋白** 的参考文献及简要摘要：
1. **文献名称**：*"Cloning and expression of the Mycobacterium tuberculosis gene encoding latent-form immunodominant antigen HSPX"*
**作者**：Yuan Y, Crane D.D., Simpson R.M., et al.
**摘要**：该研究成功克隆并表达了结核分枝杆菌的hspX基因(Rv2031c)，发现其编码的HSPX蛋白在细菌潜伏感染阶段高表达，可作为潜伏性结核感染的潜在诊断标志物。
2. **文献名称**：*"Recombinant HSPX protein of Mycobacterium tuberculosis induces protective immunity against tuberculosis in mice"*
**作者**：Hickey T.B., Zvi A.B., Sherman D.R., et al.
**摘要**：研究通过动物实验证明，重组HSPX蛋白能显著激活小鼠的Th1型免疫反应，降低结核分枝杆菌的肺部载菌量，提示其作为结核亚单位疫苗的潜力。
3. **文献名称**：*"Evaluation of recombinant HSPX for serodiagnosis of tuberculosis in clinical samples"*
**作者**：Shi C., Wang Y., Chen M., et al.
**摘要**：该文献评估了重组HSPX蛋白在结核血清学诊断中的价值，发现其与活动性结核患者血清的抗体结合特异性显著高于传统抗原(如ESAT-6/CFP-10)。
4. **文献名称**：*"Structure and function of the HSPX protein from Mycobacterium tuberculosis: Role in dormancy and stress adaptation"*
**作者**：Cunningham A.F., Spreadbury C.L.
**摘要**：通过结构生物学分析，揭示了HSPX蛋白的α-晶状体结构域在低温或缺氧条件下的稳定表达特性，表明其可能通过分子伴侣功能帮助细菌适应休眠状态。
如需具体文献来源(期刊、年份)，可进一步提供数据库(如PubMed)检索关键词!
HspX, also known as the 16-kDa α-crystallin homolog, is a member of the small heat shock protein (sHSP) family and plays a critical role in bacterial stress adaptation, particularly in Mycobacterium tuberculosis (Mtb). This protein is highly expressed under hypoxic or nutrient-deprived conditions, which mimic the hostile microenvironment encountered during latent tuberculosis infection. HspX contributes to Mtb's ability to enter a dormant state, enabling long-term persistence within host macrophages and evading immune detection. Its structural stability, conferred by α-crystallin domains, allows it to act as a molecular chaperone, preventing protein aggregation under stress.
Recombinant HspX (rHspX) is produced through genetic engineering, typically by cloning the hspX gene into expression vectors (e.g., E. coli systems) followed by purification using chromatography. Its recombinant form retains immunogenic properties, making it valuable for tuberculosis research. Studies highlight its potential as a diagnostic marker for latent TB, as it elicits strong antibody and T-cell responses in infected individuals. Additionally, rHspX is explored as a vaccine candidate, either alone or in combination with other antigens, to enhance protective immunity against active and latent TB.
Research also focuses on its role in bacterial pathogenesis and host-pathogen interactions. Structural analyses of rHspX provide insights into its chaperone-like mechanisms, while knockout models demonstrate its necessity for Mtb's stress tolerance. Despite progress, challenges remain in optimizing its diagnostic specificity and vaccine efficacy across diverse populations. Overall, rHspX serves as a pivotal tool for understanding TB latency and developing targeted therapeutic strategies.
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