| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ASPA |
| Uniprot No | P45381 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-313aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP FITNPRAVKK CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF GPKDSEDSYD IIFDLHNTTS NMGCTLILED SRNNFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGIEVG PQPQGVLRAD ILDQMRKMIK HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA AIIHPNLQDQ DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK LTLNAKSIRC CLH |
| 预测分子量 | 38 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ASPA重组蛋白的3篇参考文献，包含文献名称、作者及摘要内容：
1. **文献名称**：*"Recombinant human aspartoacylase: Biochemical characterization and in vitro activity against N-acetylaspartic acid"*
**作者**：Zano, S., et al.
**摘要**：本研究在HEK293细胞中成功表达并纯化了具有生物活性的重组人ASPA蛋白。通过体外实验证实其能够有效水解底物N-乙酰天冬氨酸(NAA)，并表现出良好的酶稳定性，为Canavan病的酶替代疗法提供了实验依据。
2. **文献名称**：*"Structural Characterization of Human Aspartoacylase Using X-ray Crystallography"*
**作者**：Bitto, E., et al.
**摘要**：通过X射线晶体学解析了人ASPA蛋白的1.8 Å分辨率三维结构，揭示了其活性位点的关键氨基酸残基及底物结合模式。此研究为理解Canavan病相关突变导致的酶功能丧失提供了分子机制基础。
3. **文献名称**：*"Gene Therapy Using Recombinant ASPA cDNA Rescues Myelination Deficits in ASPA-Deficient Rats"*
**作者**：Leone, P., et al.
**摘要**：利用腺相关病毒(AAV)载体递送重组ASPA基因至ASPA缺陷大鼠的中枢神经系统，结果显示脑内酶活性显著恢复，并伴随髓鞘形成改善，证实了基因治疗在Canavan病模型中的潜在疗效。
---
**备注**：以上文献为示例，部分内容基于真实研究整合，但具体作者与标题可能需进一步核实。如需精准文献，建议通过PubMed或Web of Science检索关键词“ASPA recombinant protein”或“Canavan disease gene therapy”。
**Background of ASPA Recombinant Protein**
Aspartoacylase (ASPA) is a critical enzyme encoded by the *ASPA* gene, primarily responsible for catalyzing the hydrolysis of N-acetylaspartic acid (NAA) into aspartate and acetate in the central nervous system. This metabolic process is essential for maintaining myelin synthesis and neuronal integrity. Mutations in the *ASPA* gene lead to a rare autosomal recessive disorder called Canavan disease, characterized by leukodystrophy, severe neurodegeneration, and early childhood mortality. The absence or dysfunction of ASPA results in toxic accumulation of NAA, disrupting osmotic balance, impairing myelination, and causing progressive brain damage.
Recombinant ASPA protein, produced via genetic engineering in bacterial, yeast, or mammalian expression systems, has emerged as a promising therapeutic tool. Its development aims to address the enzyme deficiency in Canavan disease through enzyme replacement therapy (ERT). Early studies focused on optimizing recombinant ASPA production to ensure proper folding, stability, and catalytic activity. Mammalian cell systems, such as Chinese hamster ovary (CHO) cells, are often preferred for generating post-translationally modified, functional enzymes compatible with human physiology.
Beyond therapeutic applications, recombinant ASPA serves as a vital reagent for studying NAA metabolism, myelination mechanisms, and disease pathophysiology. Structural analyses, including X-ray crystallography and cryo-EM, have elucidated its zinc-dependent hydrolase mechanism and substrate-binding sites, guiding the design of targeted therapies. Challenges remain in ensuring blood-brain barrier penetration for effective ERT, prompting exploration of fusion proteins, nanoparticle delivery, or gene therapy approaches.
Overall, ASPA recombinant protein represents a cornerstone in both therapeutic innovation and basic research for Canavan disease and related neurological disorders.
×
