| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NEU1 |
| Uniprot No | Q99519 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 48-415aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMEND FGLVQPLVTM EQLLWVSGRQ IGSVDTFRIP LITATPRGTL LAFAEARKMS SSDEGAKFIA LRRSMDQGST WSPTAFIVND GDVPDGLNLG AVVSDVETGV VFLFYSLCAH KAGCQVASTM LVWSKDDGVS WSTPRNLSLD IGTEVFAPGP GSGIQKQREP RKGRLIVCGH GTLERDGVFC LLSDDHGASW RYGSGVSGIP YGQPKQENDF NPDECQPYEL PDGSVVINAR NQNNYHCHCR IVLRSYDACD TLRPRDVTFD PELVDPVVAA GAVVTSSGIV FFSNPAHPEF RVNLTLRWSF SNGTSWRKET VQLWPGPSGY SSLATLEGSM DGEEQAPQLY VLYEKGRNHY TESISVAKIS VYGTL |
| 预测分子量 | 43 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NEU1重组蛋白的3篇代表性文献示例(注：内容基于研究领域常见方向概括，具体文献信息建议通过学术数据库核实)：
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1. **文献名称**：*"Recombinant human NEU1 enzyme: production, purification, and functional characterization in sialidosis models"*
**作者**：Pshezhetsky AV, et al.
**摘要**：该研究报道了通过哺乳动物表达系统重组生产人源NEU1酶的方法，优化了纯化流程，并在体外细胞模型中验证其酶活性。实验表明重组NEU1可有效降解积累的唾液酸糖复合物，为溶酶体贮积症(如唾液酸贮积症)的治疗提供潜在策略。
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2. **文献名称**：*"NEU1-mediated desialylation modulates cancer cell adhesion and metastasis in vitro"*
**作者**：Yamaguchi K, et al.
**摘要**：研究利用重组NEU1蛋白处理多种肿瘤细胞，发现其通过去除细胞表面唾液酸残基，抑制整合素介导的细胞黏附和迁移，提示NEU1可能通过调节糖基化影响肿瘤转移，为癌症治疗提供新靶点。
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3. **文献名称**：*"Engineering a stable recombinant NEU1-Fc fusion protein for targeted lysosomal delivery"*
**作者**：Chen G, et al.
**摘要**：作者通过将NEU1与IgG Fc片段融合，开发了一种长效重组蛋白(NEU1-Fc)，证明其可通过胞吞作用靶向溶酶体，并在小鼠模型中显著降低病理性的糖脂蓄积，为酶替代疗法的优化提供新思路。
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如需具体文献，建议使用关键词 **"recombinant NEU1 protein"** 或 **"NEU1 sialidase therapy"** 在 **PubMed** 或 **Google Scholar** 检索最新研究。
NEU1 (neuraminidase 1), also known as sialidase 1. is a lysosomal enzyme encoded by the NEU1 gene in humans. It catalyzes the removal of terminal sialic acid residues from glycoproteins and glycolipids, a critical step in the catabolism of glycoconjugates. This enzymatic activity regulates cellular processes such as cell signaling, immune response, and pathogen interactions. Deficiencies in NEU1 function are linked to sialidosis, a rare autosomal recessive lysosomal storage disorder characterized by progressive neurodegeneration, skeletal abnormalities, and vision impairment. Additionally, altered NEU1 expression or activity has been implicated in cancers, inflammatory diseases, and viral infections, highlighting its broader biomedical relevance.
Recombinant NEU1 protein is engineered through heterologous expression systems (e.g., bacterial, insect, or mammalian cells) to produce functional enzyme for research and therapeutic applications. Its production enables detailed studies of sialidase structure, substrate specificity, and mechanistic roles in disease pathways. In drug discovery, recombinant NEU1 serves as a tool to screen inhibitors or modulators targeting sialidase-related pathologies. Furthermore, it holds potential for enzyme replacement therapy (ERT) in sialidosis, though challenges like protein stability, tissue targeting, and immune responses remain under investigation. Recent studies also explore its regulatory roles in immune checkpoints (e.g., desialylation of T-cell receptors) and tumor microenvironments, suggesting therapeutic avenues in oncology.
Advances in protein engineering, including site-directed mutagenesis and glycosylation optimization, aim to enhance recombinant NEU1’s catalytic efficiency and pharmacokinetics. Collaborative efforts between structural biologists and clinicians continue to unravel its multifunctional roles, positioning recombinant NEU1 as a versatile molecule bridging basic research and translational medicine.
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