| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ASM |
| Uniprot No | P17405 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 47-631aa |
| 氨基酸序列 | LALSDSRVLWAPAEAHPLSPQGHPARLHRIVPRLRDVFGWGNLTCPICKGLFTAINLGLKKEPNVARVGSVAIKLCNLLKIAPPAVCQSIVHLFEDDMVEVWRRSVLSPSEACGLLLGSTCGHWDIFSSWNISLPTVPKPPPKPPSPPAPGAPVSRILFLTDLHWDHDYLEGTDPDCADPLCCRRGSGLPPASRPGAGYWGEYSKCDLPLRTLESLLSGLGPAGPFDMVYWTGDIPAHDVWHQTRQDQLRALTTVTALVRKFLGPVPVYPAVGNHESTPVNSFPPPFIEGNHSSRWLYEAMAKAWEPWLPAEALRTLRIGGFYALSPYPGLRLISLNMNFCSRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKVHIIGHIPPGHCLKSWSWNYYRIVARYENTLAAQFFGHTHVDEFEVFYDEETLSRPLAVAFLAPSATTYIGLNPGYRVYQIDGNYSGSSHVVLDHETYILNLTQANIPGAIPHWQLLYRARETYGLPNTLPTAWHNLVYRMRGDMQLFQTFWFLYHKGHPPSEPCGTPCRLATLCAQLSARADSPALCRHLMPDGSLPEAQSLWPRPLFC |
| 预测分子量 | 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. |
以下是关于重组酸性鞘磷脂酶(ASM)的参考文献示例(注：以下内容为模拟生成，非真实文献)：
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1. **标题**: *Production and Characterization of Recombinant Human Acid Sphingomyelinase for Therapeutic Use*
**作者**: Smith, J.R., et al.
**摘要**: 该研究描述了利用哺乳动物细胞表达系统生产重组人源ASM的工艺优化，分析了其酶活性、稳定性和糖基化修饰特征，并验证了其在体外细胞模型中降解鞘磷脂的效果，为治疗尼曼-匹克病(Niemann-Pick disease)提供了候选药物基础。
2. **标题**: *Enzyme Replacement Therapy with Recombinant ASM Improves Lipid Metabolism in a Mouse Model of Niemann-Pick Disease*
**作者**: Chen, L., & Wang, H.
**摘要**: 通过动物实验评估重组ASM对尼曼-匹克病模型小鼠的治疗效果，结果显示定期注射重组ASM显著减少了肝脏和神经组织的鞘磷脂沉积，并改善了脂质代谢指标，支持其临床转化潜力。
3. **标题**: *Structural Insights into Recombinant Acid Sphingomyelinase: Implications for Substrate Binding and Catalytic Mechanism*
**作者**: Müller, S., et al.
**摘要**: 利用X射线晶体学解析了重组ASM的三维结构，揭示了其活性位点与鞘磷脂结合的关键氨基酸残基，并通过定点突变实验验证了催化机制，为设计高效变体提供了结构基础。
4. **标题**: *Large-Scale Purification of Recombinant ASM Using Affinity Chromatography: Process Development and Challenges*
**作者**: Gupta, A., & Patel, R.
**摘要**: 探讨了基于亲和层析技术的大规模重组ASM纯化工艺，优化了洗脱条件和去污剂使用策略，解决了蛋白聚集和活性损失问题，最终获得高纯度、高活性的制剂。
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(注：以上文献信息为示例性质，实际研究中请参考真实数据库如PubMed或Web of Science获取准确文献。)
Acid Sphingomyelinase (ASM), a lysosomal enzyme encoded by the *SMPD1* gene, plays a critical role in lipid metabolism by hydrolyzing sphingomyelin into ceramide and phosphocholine. Deficiencies in ASM activity lead to sphingomyelin accumulation in lysosomes, causing Niemann-Pick disease types A and B (NPA/NPB), rare lysosomal storage disorders characterized by neurodegeneration, hepatosplenomegaly, and respiratory failure. Historically, treatment options were limited to symptomatic management, highlighting the need for enzyme replacement therapies (ERTs).
Recombinant ASM production emerged as a breakthrough, leveraging genetic engineering to produce functional enzyme variants. Using mammalian cell lines (e.g., CHO cells), researchers developed recombinant human ASM (rhASM) with post-translational modifications mimicking native enzyme structure and activity. Early challenges included optimizing protein stability, glycosylation patterns, and delivery efficiency to target tissues. Preclinical studies demonstrated rhASM’s ability to reduce sphingomyelin storage in animal models, paving the way for clinical trials.
Olipudase alfa, a recombinant ASM, has shown promise in clinical trials, improving pulmonary function and reducing organomegaly in NPB patients. However, immune responses and variable tissue penetration remain hurdles. Advances in protein engineering, such as PEGylation or cell-targeting modifications, aim to enhance therapeutic efficacy and reduce immunogenicity.
Beyond Niemann-Pick disease, recombinant ASM holds potential in treating conditions linked to ceramide signaling dysregulation, including cystic fibrosis and viral infections. Its development underscores the synergy between molecular biology and therapeutic innovation, offering a template for addressing lysosomal disorders through recombinant protein technology.
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