| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SMN |
| Uniprot No | Q16637 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-282aa |
| 氨基酸序列 | MAMSSGGSGGGVPEQEDSVLFRRGTGQSDDSDIWDDTALIKAYDKAVASF KHALKNGDICETSGKPKTTPKRKPAKKNKSQKKNTAASLQQWKVGDKCSA IWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDLLSPICEVAN NIEQNAQENENESQVSTDESENSRSPGNKSDNIKPKSAPWNSFLPPPPPM PGPRLGPGKPGLKFNGPPPPPPPPPPHLLSCWLPPFPSGPPIIPPPPPIC PDSLDDADALGSMLISWYMSGYHTGYYMEMLA |
| 预测分子量 | 57 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SMN重组蛋白的模拟参考文献示例(部分信息为虚构，仅作格式参考)：
1. **文献名称**：Recombinant SMN protein enhances survival in a mouse model of spinal muscular atrophy
**作者**：Smith J, et al.
**摘要**：研究通过重组SMN蛋白在小鼠SMA模型中系统性递送，证明其能有效穿透血脑屏障并延长生存期，为蛋白替代疗法提供实验依据。
2. **文献名称**：Production of functional human SMN protein in E. coli: Implications for SMA therapeutics
**作者**：Li X, et al.
**摘要**：报道了一种大肠杆菌表达系统高效生产具有生物活性的重组人SMN蛋白，并验证其在体外恢复运动神经元功能的能力。
3. **文献名称**：Structural analysis of recombinant SMN complex reveals oligomerization-dependent mechanism
**作者**：Garcia R, et al.
**摘要**：通过冷冻电镜解析重组SMN蛋白复合物的三维结构，阐明其寡聚化状态对snRNP组装功能的调控机制。
4. **文献名称**：Intranasal delivery of recombinant SMN improves motor function in neonatal SMA pigs
**作者**：Chen L, et al.
**摘要**：开发鼻黏膜递送重组SMN蛋白的新方法，在大型动物模型(猪)中观察到运动神经元保护和运动能力改善效果。
注：以上文献信息为模拟生成，实际引用请查询PubMed、Web of Science等数据库获取真实文献。
**Background of Recombinant SMN Protein**
Spinal muscular atrophy (SMA) is a devastating neurodegenerative disorder primarily caused by mutations or deletions in the *SMN1* gene, which encodes the survival motor neuron (SMN) protein. SMN is essential for the assembly of small nuclear ribonucleoproteins (snRNPs), critical components of the spliceosome machinery responsible for pre-mRNA splicing. Reduced SMN levels lead to impaired RNA processing, motor neuron degeneration, and progressive muscle weakness.
Humans possess a paralog gene, *SMN2*, which produces insufficient functional SMN protein due to a splicing defect in exon 7. While *SMN2* generates mostly truncated SMNΔ7 protein (∼10% functional protein), its copy number correlates with disease severity. This genetic redundancy underpins therapeutic strategies aimed at modulating *SMN2* splicing or supplementing functional SMN protein.
Recombinant SMN protein therapy emerged as a promising approach to directly restore SMN levels, bypassing genetic limitations. Early challenges included protein stability, delivery across the blood-brain barrier, and intracellular targeting. Advances in protein engineering, such as cell-penetrating peptides or fusion tags, have improved bioavailability and neuronal uptake.
Notably, FDA-approved SMA therapies like antisense oligonucleotides (e.g., nusinersen) and gene therapy (e.g., onasemnogene abeparvovec) focus on enhancing SMN production from *SMN2* or delivering functional *SMN1* genes. Recombinant SMN protein could complement these by providing immediate, dose-controlled supplementation, particularly for patients with low *SMN2* copies or resistance to existing treatments.
Preclinical studies in SMA mouse models demonstrated that recombinant SMN protein extends survival and improves motor function. However, challenges remain in optimizing pharmacokinetics, minimizing immunogenicity, and ensuring sustained efficacy. Ongoing research explores hybrid strategies, combining recombinant proteins with gene therapies or small molecules, to maximize therapeutic outcomes.
In summary, recombinant SMN protein represents a direct, versatile therapeutic avenue for SMA, addressing the root cause of SMN deficiency while offering potential synergies with established modalities.
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