| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | nanA |
| Uniprot No | Q0SWI8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-288aa |
| 氨基酸序列 | MKGIYSALLVSFDKDGNINEKGLREIIRHNIDVCKIDGLYVGGSTGENFMLSTDEKKRIFEIAMDEAKGQVKLIAQVGSVNLKEAVELAKFTTDLGYDAISAVTPFYYKFDFNEIKHYYETIINSVDNKLIIYSIPFLTGVNMSIEQFAELFENDKIIGVKFTAADFYLLERMRKAFPDKLIFAGFDEMMLPATVLGVDGAIGSTFNVNGIRARQIFEAAQKGDIETALEVQHVTNDLITDILNNGLYQTIKLILQEQGVDAGYCRQPMKEATEEMIEKAKEINKKYF |
| 预测分子量 | 34.0 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nanA重组蛋白的3篇代表性文献示例(注：文献信息为虚拟模拟，仅供格式参考)：
1. **《Cloning and enzymatic characterization of recombinant NanA neuraminidase from Streptococcus pneumoniae》**
- 作者：Smith, J. et al.
- 摘要：研究通过大肠杆菌系统成功表达并纯化了重组NanA蛋白，证实其具有唾液酸酶活性，并发现其对宿主细胞黏附的关键作用，为抗感染治疗提供靶点。
2. **《Structural analysis of NanA protein reveals potential epitopes for vaccine development》**
- 作者：Li, X. et al.
- 摘要：利用X射线晶体学解析了肺炎链球菌NanA蛋白的三维结构，筛选出高免疫原性区域，动物实验显示重组NanA可诱导中和抗体，提示其作为疫苗候选的潜力。
3. **《Heterologous expression of nanA in Lactococcus lactis and functional evaluation in vitro》**
- 作者：García, R. et al.
- 摘要：在乳酸乳球菌中异源表达NanA蛋白，验证其酶活性和稳定性，证明其在降解呼吸道黏液层的功能，为构建递送系统提供实验基础。
**Background of NanA Recombinant Protein**
The *nanA* gene encodes neuraminidase (sialidase) A, a key virulence factor produced by *Streptococcus pneumoniae*, a bacterial pathogen responsible for pneumonia, meningitis, and other invasive diseases. Neuraminidase enzymes, including NanA, cleave terminal sialic acid residues from glycoconjugates on host cell surfaces, facilitating bacterial adherence, colonization, and immune evasion. NanA specifically contributes to pneumococcal pathogenesis by exposing host cell receptors, disrupting mucosal barriers, and enhancing biofilm formation. Its role in cleaving sialic acids also promotes secondary bacterial infections by damaging epithelial tissues and modulating host inflammatory responses.
Recombinant NanA protein is engineered through molecular cloning, where the *nanA* gene is expressed in heterologous systems like *E. coli* or yeast. This allows large-scale production of purified NanA for functional and structural studies. Researchers utilize recombinant NanA to investigate its enzymatic mechanisms, substrate specificity, and interactions with host molecules. Such studies have highlighted its potential as a therapeutic target; inhibiting NanA activity could reduce pneumococcal virulence.
Additionally, NanA recombinant protein is employed in vaccine development. Including NanA in multicomponent vaccines aims to induce protective immunity against pneumococcal infections. Structural analyses (e.g., X-ray crystallography) of recombinant NanA have revealed critical domains for enzyme activity and inhibitor binding, guiding rational drug design. Beyond therapeutics, NanA serves as a tool in glycobiology research to study sialylation patterns in cellular processes.
Overall, NanA recombinant protein is vital for understanding pneumococcal pathogenicity and advancing strategies to combat related diseases. Its applications span basic science, drug discovery, and vaccine development, underscoring its significance in both biomedical research and clinical innovation.
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