| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NEU2 |
| Uniprot No | Q9Y3R4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 180-268aa |
| 氨基酸序列 | AYRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQ RVVTLNARSHLRARVQAQSTNDGLDFQESQLVKKLVEPP |
| 预测分子量 | 35 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NEU2重组蛋白的3篇参考文献示例(注：文献为模拟示例，实际引用请核实原文)：
1. **"Expression and characterization of recombinant human NEU2 sialidase in mammalian cells"**
- **作者**: Monti E., et al.
- **摘要**: 研究通过哺乳动物表达系统(COS-7细胞)成功表达重组人NEU2蛋白，并分析其酶学特性，发现其对神经节苷脂底物具有特异性水解活性，提示其在糖代谢中的潜在作用。
2. **"NEU2 sialidase downregulation promotes colon cancer cell migration via modulation of ganglioside expression"**
- **作者**: Miyagi T., et al.
- **摘要**: 通过重组NEU2蛋白实验，揭示NEU2在结肠癌细胞中通过调控神经节苷脂的唾液酸化水平抑制细胞迁移，其表达下调可能导致肿瘤转移增强。
3. **"Structural insights into the catalytic mechanism of NEU2 sialidase through X-ray crystallography"**
- **作者**: Chichili G.R., et al.
- **摘要**: 利用重组NEU2蛋白的晶体结构解析，阐明其活性位点及催化机制，为设计特异性抑制剂提供结构基础。
建议通过PubMed或Google Scholar以关键词“NEU2 recombinant protein”、“sialidase NEU2”进一步检索最新文献。
NEU2. also known as sialidase-2. is a member of the neuraminidase enzyme family that catalyzes the hydrolysis of terminal sialic acid residues from glycoproteins, glycolipids, and oligosaccharides. This lysosomal enzyme plays a critical role in cellular metabolism by regulating the degradation and recycling of sialoglycoconjugates. Unlike other mammalian sialidases (NEU1. NEU3. NEU4), NEU2 is uniquely cytosolic in localization, suggesting distinct biological functions. Its activity influences cellular processes such as cell signaling, apoptosis, and immune response modulation.
Recombinant NEU2 protein is engineered through molecular cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems to achieve proper folding and enzymatic activity. This engineered version retains the native enzyme's ability to cleave α2-3. α2-6. and α2-8 glycosidic linkages of sialic acids, making it valuable for studying glycan remodeling and sialylation patterns in biological systems. Researchers utilize recombinant NEU2 to investigate its role in diseases associated with abnormal sialylation, including cancer metastasis, viral infection mechanisms, and neurodegenerative disorders like Alzheimer's disease.
In therapeutic contexts, NEU2 has gained attention for its potential in cancer treatment. Elevated sialylation on tumor cell surfaces often correlates with immune evasion and metastasis, and NEU2-mediated desialylation may reverse these effects. Additionally, recombinant NEU2 serves as a tool enzyme in glycobiology research for modifying therapeutic proteins, enhancing their efficacy through controlled desialylation. Ongoing studies focus on optimizing its stability, substrate specificity, and delivery mechanisms for biomedical applications, bridging fundamental glycobiology with translational medicine.
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