| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | dSIP |
| Uniprot No | Q99576 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-134aa |
| 氨基酸序列 | MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAI DNKIEQAMDL VKNHLMYAVR EEVEILKEQI RELVEKNSQL ERENTLLKTL ASPEQLEKFQ SCLSPEEPAP ESPQVPEAPG GSAV |
| 预测分子量 | 14,8 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dSIP(δ睡眠诱导肽)重组蛋白研究的示例参考文献(注：部分内容为假设性示例，具体文献需通过学术数据库核实)：
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1. **标题**: "Expression and Purification of Recombinant δ-Sleep-Inducing Peptide in Escherichia coli"
**作者**: Smith A, et al.
**摘要**: 本研究报道了通过大肠杆菌系统高效表达重组dSIP的方法，优化了表达条件并采用亲和层析技术纯化，验证了重组肽的免疫活性。
2. **标题**: "Functional Characterization of Recombinant dSIP in a Rodent Sleep Model"
**作者**: Tanaka K, et al.
**摘要**: 通过重组dSIP注射大鼠模型，证实其显著延长慢波睡眠时间，并探讨了其与GABA受体的潜在相互作用机制。
3. **标题**: "Structural Analysis of δ-Sleep-Inducing Peptide Using Recombinant Expression and NMR Spectroscopy"
**作者**: Müller B, et al.
**摘要**: 利用核磁共振技术解析了重组dSIP的三维结构，揭示了其与睡眠调控相关的关键功能域构象。
4. **标题**: "Scale-Up Production of Recombinant dSIP in Yeast and Its Therapeutic Potential in Insomnia"
**作者**: Chen L, et al.
**摘要**: 开发了基于酵母的重组dSIP规模化生产工艺，并在小鼠失眠模型中验证其持续改善睡眠质量的疗效。
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**备注**：以上为模拟示例，实际文献需通过PubMed、Google Scholar等平台检索关键词(如"recombinant delta sleep-inducing peptide"或"dSIP expression")。早期经典研究多发表于20世纪末，近年研究可能侧重其机制或应用拓展。
dSIP (disulfide-stabilized immunogenic protein) is a class of engineered recombinant proteins designed to enhance stability, immunogenicity, and therapeutic efficacy in biomedical applications. These proteins are typically derived from antigenic or functional domains of pathogens, tumor-associated antigens, or immune signaling molecules, modified by introducing strategically positioned disulfide bonds. The disulfide bridges confer structural rigidity, improving resistance to proteolytic degradation and thermal denaturation, which is critical for maintaining functionality in physiological environments.
The development of dSIPs stems from challenges in conventional protein-based therapies, such as short half-life, low stability, and suboptimal immune activation. By stabilizing conformational epitopes through covalent disulfide bonds, dSIPs enhance antigen presentation and immune recognition, making them particularly promising for vaccine development and cancer immunotherapy. For instance, dSIPs targeting viral surface proteins or tumor neoantigens can elicit stronger and more durable adaptive immune responses compared to their native counterparts.
Production of dSIPs involves recombinant DNA technology, where codon-optimized sequences are expressed in microbial (e.g., *E. coli*) or mammalian systems, followed by purification and oxidative folding to ensure proper disulfide bond formation. Recent advances include fusion with adjuvant domains or checkpoint inhibitors to further amplify immune activation. Preclinical studies have demonstrated their potential in models of infectious diseases and oncology, with several candidates entering early-phase clinical trials. Despite challenges in scalability and immunogenicity balancing, dSIPs represent a versatile platform bridging protein engineering and immunology, offering tailored solutions for next-generation biologics.
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