| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | Neu4 |
| Uniprot No | Q8BZL1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-478aa |
| 氨基酸序列 | MGPTRVPRRTVLFQRERTGLTYRVPALLCVPPRPTLLAFAEQRLSPDDSHAHRLVLRRGTLTRGSVRWGTLSVLETAVLEEHRSMNPCPVLDEHSGTIFLFFIAVLGHTPEAVQIATGKNAARLCCVTSCDAGLTWGSVRDLTEEAIGAALQDWATFAVGPGHGVQLRSGRLLVPAYTYHVDRRECFGKICWTSPHSLAFYSDDHGISWHCGGLVPNLRSGECQLAAVDGDFLYCNARSPLGNRVQALSADEGTSFLPGELVPTLAETARGCQGSIVGFLAPPSIEPQDDRWTGSPRNTPHSPCFNLRVQESSGEGARGLLERWMPRLPLCYPQSRSPENHGLEPGSDGDKTSWTPECPMSSDSMLQSPTWLLYSHPAGRRARLHMGIYLSRSPLDPHSWTEPWVIYEGPSGYSDLAFLGPMPGASLVFACLFESGTRTSYEDISFCLFSLADVLENVPTGLEMLSLRDKAQGHCWPS |
| 预测分子量 | 52,4 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Neu4重组蛋白的参考文献示例(注：文献为虚构，仅作格式参考)：
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1. **文献名称**：Expression and Functional Characterization of Recombinant Human Neu4 Sialidase in E. coli
**作者**：T. Suzuki et al.
**摘要**：研究通过大肠杆菌表达系统成功制备重组人源Neu4唾液酸酶，优化纯化流程并验证其酶活性。结果显示重组Neu4对神经节苷脂底物具有特异性水解能力，为研究其在代谢疾病中的作用提供工具。
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2. **文献名称**：Structural Insights into Neu4 Recombinant Protein: Implications for Substrate Binding
**作者**：M. Tanaka & K. Yamamoto
**摘要**：通过X射线晶体学解析Neu4重组蛋白的三维结构，揭示其活性位点关键氨基酸残基与底物结合机制，为开发靶向Neu4的抑制剂奠定结构基础。
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3. **文献名称**：Role of Recombinant Neu4 in Cancer Cell Migration and Metastasis
**作者**：L. Zhang et al.
**摘要**：体外实验表明，重组Neu4蛋白通过调控细胞表面唾液酸化水平抑制结肠癌细胞迁移，提示其可能作为肿瘤转移的潜在治疗靶点。
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**备注**：实际文献需通过PubMed/Google Scholar检索关键词(如 "Neu4 sialidase recombinant")获取。若需真实文献，建议查阅《Journal of Biological Chemistry》或《Glycobiology》等期刊近年发表的研究。
Neu4 recombinant protein, typically derived from the neuraminidase-4 (NEU4) gene, is a genetically engineered protein involved in sialic acid metabolism. Neuraminidases, also called sialidases, are enzymes that catalyze the removal of sialic acid residues from glycoproteins, glycolipids, and oligosaccharides, playing critical roles in cellular communication, pathogen-host interactions, and metabolic regulation. Among the four human neuraminidases (NEU1-NEU4), NEU4 exhibits unique substrate specificity and subcellular localization, primarily localizing to lysosomes and mitochondria. It is implicated in modulating neuronal function, cancer progression, and lysosomal storage disorders.
The recombinant NEU4 protein is produced using expression systems like bacterial (E. coli) or mammalian cells, enabling large-scale purification for research and therapeutic applications. Its recombinant form retains enzymatic activity, allowing studies on sialylation-dependent processes, such as cell adhesion, signaling, and immune evasion. NEU4’s role in diseases like Alzheimer’s, where altered sialylation affects amyloid-beta aggregation, and in cancers, where it influences metastasis, has driven interest in its recombinant production.
Research utilizing Neu4 recombinant protein focuses on elucidating its structural-functional relationships, substrate preferences, and interactions with inhibitors. It also serves as a tool for developing enzyme replacement therapies for sialidase deficiencies. Despite progress, challenges remain in optimizing its stability and activity in vitro. Overall, Neu4 recombinant protein is a valuable resource for exploring sialic acid biology and its implications in health and disease.
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