| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NANS |
| Uniprot No | Q9NR45 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-359aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMPLELELCPGRWVGGQHPCFIIAEIGQNHQ GDLDVAKRMIRMAKECGADCAKFQKSELEFKFNRKALERPYTSKHSWGKT YGEHKRHLEFSHDQYRELQRYAEEVGIFFTASGMDEMAVEFLHELNVPFF KVGSGDTNNFPYLEKTAKKGRPMVISSGMQSMDTMKQVYQIVKPLNPNFC FLQCTSAYPLQPEDVNLRVISEYQKLFPDIPIGYSGHETGIAISVAAVAL GAKVLERHITLDKTWKGSDHSASLEPGELAELVRSVRLVERALGSPTKQL LPCEMACNEKLGKSVVAKVKIPEGTILTMDMLTVKVGEPKGYPPEDIFNL VGKKVLVTVEEDDTIMEELVDNHGKKIKS |
| 预测分子量 | 42 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NANS(N-乙酰神经氨酸合成酶)重组蛋白研究的模拟参考文献(注：部分信息为示例性质，具体文献请通过学术数据库核实)：
1. **文献名称**: "Heterologous Expression and Characterization of Recombinant NANS in Escherichia coli"
**作者**: Zhang L, et al.
**摘要**: 本研究通过构建pET载体在大肠杆菌中高效表达重组NANS蛋白，优化表达条件后获得可溶性蛋白，并通过酶活实验验证其催化神经氨酸合成的功能，为唾液酸生物合成机制研究提供基础。
2. **文献名称**: "Structural Insights into Human N-Acetylneuraminic Acid Synthase (NANS) via Crystallography"
**作者**: Thompson R, et al.
**摘要**: 首次解析了人源NANS重组蛋白的晶体结构(分辨率2.1Å)，揭示了其底物结合域的关键氨基酸残基，为开发针对遗传性唾液酸代谢疾病的药物提供了结构基础。
3. **文献名称**: "Functional Analysis of NANS Mutants in a Zebrafish Disease Model"
**作者**: Chen H, et al.
**摘要**: 通过杆状病毒系统表达野生型及突变型NANS重组蛋白，结合斑马鱼模型证实NANS基因突变导致骨骼发育异常，提示其在脊椎动物发育中的关键作用。
建议通过PubMed、Web of Science或Google Scholar搜索关键词："N-acetylneuraminic acid synthase recombinant" 或 "NANS protein expression" 获取最新文献。实际研究中需注意文献的发表年份(推荐优先选择近5年研究)及期刊影响力(如JBC、Protein Expr Purif等生物化学领域期刊)。
**Background of NANS Recombinant Protein**
N-acetylneuraminic acid synthase (NANS) is a key enzyme in the sialic acid biosynthesis pathway, catalyzing the conversion of N-acetylmannosamine (ManNAc) and phosphoenolpyruvate (PEP) to N-acetylneuraminic acid (Neu5Ac), a predominant sialic acid in vertebrates. Sialic acids are critical components of glycoconjugates on cell surfaces, playing roles in cell-cell recognition, immune modulation, and pathogen-host interactions. Dysregulation of sialylation is linked to developmental disorders, cancer metastasis, and infectious diseases.
Recombinant NANS protein is engineered using biotechnological platforms (e.g., *E. coli* or mammalian expression systems) to produce high-purity, functional enzyme for research and therapeutic applications. Its production enables detailed structural and functional studies, aiding in understanding congenital disorders like NANS-related developmental syndromes, characterized by skeletal abnormalities and neurological deficits. Mutations in the *NANS* gene disrupt sialic acid synthesis, underscoring the enzyme’s role in embryonic development and homeostasis.
In biomedicine, recombinant NANS serves as a tool to explore sialylation mechanisms in diseases, screen enzyme inhibitors for therapeutic targeting, and support glycobiology research. It also holds potential in biomanufacturing sialylated molecules, such as vaccines or synthetic human milk oligosaccharides. Overall, NANS recombinant protein bridges fundamental glycobiology with translational applications, offering insights into disease mechanisms and innovative biotechnological solutions.
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