| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | nanE |
| Uniprot No | Q8XNZ3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-221aa |
| 氨基酸序列 | MLDVVKGNLIVSCQALSDEPLHSSFIMGRMAIAAKQGGAAAIRAQGVNDINEIKEVTKLPIIGIIKRNYDDSEIYITPTMKEVDELLKTDCEMIALDATKRKRPNGENVKDLVDAIHAKGRLAMADISTLEEGIEAEKLGFDCVSTTLSGYTPYSKQSNSVDFELLEELVKTVKIPVICEGRINTPEELKKALDLGAYSAVVGGAITRPQQITKRFTDILK |
| 预测分子量 | 30.1 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. |
以下是关于nanE重组蛋白的3-4篇文献示例(注：文献为虚构示例，仅用于演示格式)：
1. **文献名称**：*Crystal Structure and Substrate Specificity of Recombinant NanE from Neisseria meningitidis*
**作者**：Smith A, et al.
**摘要**：解析了脑膜炎奈瑟菌来源的nanE重组蛋白的晶体结构，揭示了其底物结合位点的关键氨基酸残基，为靶向抑制剂设计提供了依据。
2. **文献名称**：*Recombinant NanE as a Novel Vaccine Candidate against Streptococcal Infections*
**作者**：Johnson B, et al.
**摘要**：评估了重组NanE蛋白在链球菌感染小鼠模型中的免疫原性，结果显示其可诱导特异性抗体反应并降低细菌定植率，具有疫苗开发潜力。
3. **文献名称**：*Enzymatic Characterization of Recombinant NanE in Sialic Acid Metabolism*
**作者**：Lee C, et al.
**摘要**：通过体外酶活实验验证了重组NanE的N-乙酰神经氨酸裂解酶活性，并发现其催化效率受pH和金属离子调控，为唾液酸代谢研究提供数据支持。
4. **文献名称**：*Development of a NanE-based Diagnostic Antigen for Bacterial Pathogen Detection*
**作者**：Martinez D, et al.
**摘要**：利用重组NanE蛋白作为诊断抗原，建立了一种高灵敏度的ELISA检测方法，可特异性识别多种致病菌感染患者血清中的抗体。
(注：以上文献及作者为模拟内容，实际研究中请参考真实数据库如PubMed。)
NanE, also known as N-acetylneuraminate lyase, is a key enzyme in the sialic acid metabolic pathway, catalyzing the reversible cleavage of N-acetylneuraminic acid (Neu5Ac) into N-acetylmannosamine (ManNAc) and pyruvate. This enzyme plays a critical role in bacterial pathogenesis and host-pathogen interactions, particularly in species like *Streptococcus pneumoniae*, where it contributes to nutrient acquisition, immune evasion, and biofilm formation. In humans, the homologous enzyme is involved in sialic acid recycling, making it relevant to cellular signaling and glycoconjugate synthesis.
The recombinant NanE protein is produced via genetic engineering, typically by cloning the *nanE* gene into expression vectors (e.g., *E. coli* or yeast systems) to enable large-scale production. Its recombinant form retains the enzymatic activity of the native protein, allowing researchers to study its structure-function relationships, substrate specificity, and regulatory mechanisms. Structural studies using X-ray crystallography have revealed its conserved (β/α)₈ TIM barrel fold and active-site residues critical for catalysis.
Interest in recombinant NanE spans multiple fields. In infectious disease research, it serves as a potential antimicrobial target due to its role in bacterial survival. In biotechnology, it is explored for enzymatic synthesis of sialic acid derivatives used in glycobiology and therapeutic development. Additionally, NanE variants engineered for enhanced stability or altered substrate preferences hold promise for industrial biocatalysis. Recent studies also investigate its involvement in metabolic disorders, as dysregulated sialic acid metabolism is linked to certain diseases. The development of recombinant NanE tools continues to advance both basic science and applied research, bridging microbiology, enzymology, and biomedical engineering.
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