| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SP |
| Uniprot No | P23497 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-879aa |
| 氨基酸序列 | MAGGGGDLSTRRLNECISPVANEMNHLPAHSHDLQRMFTEDQGVDDRLLYDIVFKHFKRNKVEISNAIKKTFPFLEGLRDRDLITNKMFEDSQDSCRNLVPVQRVVYNVLSELEKTFNLPVLEALFSDVNMQEYPDLIHIYKGFENVIHDKLPLQESEEEEREERSGLQLSLEQGTGENSFRSLTWPPSGSPSHAGTTPPENGLSEHPCETEQINAKRKDTTSDKDDSLGSQQTNEQCAQKAEPTESCEQIAVQVNNGDAGREMPCPLPCDEESPEAELHNHGIQINSCSVRLVDIKKEKPFSNSKVECQAQARTHHNQASDIIVISSEDSEGSTDVDEPLEVFISAPRSEPVINNDNPLESNDEKEGQEATCSRPQIVPEPMDFRKLSTFRESFKKRVIGQDHDFSESSEEEAPAEASSGALRSKHGEKAPMTSRSTSTWRIPSRKRRFSSSDFSDLSNGEELQETCSSSLRRGSGSQPQEPENKKCSCVMCFPKGVPRSQEARTESSQASDMMDTMDVENNSTLEKHSGKRRKKRRHRSKVNGLQRGRKKDRPRKHLTLNNKVQKKRWQQRGRKANTRPLKRRRKRGPRIPKDENINFKQSELPVTCGEVKGTLYKERFKQGTSKKCIQSEDKKWFTPREFEIEGDRGASKNWKLSIRCGGYTLKVLMENKFLPEPPSTRKKRILESHNNTLVDPCEEHKKKNPDASVKFSEFLKKCSETWKTIFAKEKGKFEDMAKADKAHYEREMKTYIPPKGEKKKKFKDPNAPKRPPLAFFLFCSEYRPKIKGEHPGLSIDDVVKKLAGMWNNTAAADKQFYEKKAAKLKEKYKKDIAAYRAKGKPNSAKKRVVKAEKSKKKKEEEEDEEDEQEEENEEDDDK |
| 预测分子量 | 100 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SP(信号肽)重组蛋白的3篇参考文献及其摘要概括：
1. **《Optimization of Signal Peptides for Secretory Production of Recombinant Proteins in Escherichia coli》**
- 作者：Makrides S.C.
- 摘要：综述了大肠杆菌中重组蛋白分泌表达的关键因素，重点分析了不同信号肽(如PelB、OmpA)对蛋白分泌效率的影响，并提出了优化信号肽选择及工程化改造的策略，以提高目标蛋白的分泌产量和可溶性。
2. **《Signal Peptide Engineering for Enhanced Antibody Secretion in Mammalian Cell Cultures》**
- 作者：Li F. et al.
- 摘要：研究比较了哺乳动物细胞(CHO细胞)中天然与人工设计的信号肽对抗体分泌效率的影响。通过实验筛选发现，改造后的信号肽可显著提高抗体的分泌水平，同时降低内质网应激反应，为治疗性蛋白生产提供了优化方案。
3. **《Enhancing Recombinant Protein Secretion in Pichia pastoris by Signal Peptide Screening》**
- 作者：Ahmad M. et al.
- 摘要：系统评估了毕赤酵母中多种信号肽(如α-factor、PHO1)对异源蛋白分泌的促进作用。通过高通量筛选发现，特定信号肽与目标蛋白的适配性显著影响分泌效率，为酵母表达系统的工业化应用提供了实验依据。
4. **《Machine Learning-Based Prediction of Optimal Signal Peptides for Recombinant Protein Production》**
- 作者：Zhang Y. et al.
- 摘要：提出了一种结合生物信息学与机器学习的算法，用于预测特定重组蛋白的最适信号肽序列。该模型在细菌、酵母和哺乳动物细胞中均验证有效，显著缩短了传统试错法所需的时间，为精准设计分泌型重组蛋白提供新工具。
以上文献涵盖了信号肽在细菌、哺乳动物细胞、酵母等表达系统中的优化策略及前沿技术，涉及实验筛选、工程化改造和算法预测等多个研究方向。
**Background of SP Recombinant Proteins**
SP (Signal Peptide) recombinant proteins are engineered biomolecules designed to enhance the efficient production, secretion, and purification of target proteins in heterologous expression systems. Signal peptides are short amino acid sequences (typically 15–30 residues) naturally found at the N-terminus of nascent proteins, guiding their translocation across cellular membranes. In recombinant protein technology, these peptides are fused to the target protein to direct its secretion into the extracellular space or specific cellular compartments, simplifying downstream purification and improving yield.
The development of SP recombinant proteins is rooted in advancements in genetic engineering and synthetic biology. Since the 1970s, recombinant DNA technology has enabled the insertion of synthetic or native signal peptide sequences into expression vectors. Commonly used systems include *E. coli*, yeast, insect, and mammalian cells, each chosen based on the protein’s complexity and required post-translational modifications. For example, prokaryotic systems like *E. coli* are cost-effective but may require optimization to avoid misfolding, while eukaryotic systems ensure proper folding for therapeutic proteins.
Applications span biopharmaceuticals (e.g., insulin, monoclonal antibodies), industrial enzymes, and research tools. SP fusion is particularly valuable for proteins prone to aggregation or degradation when retained intracellularly. Challenges include variability in secretion efficiency across hosts and the need for empirical optimization of signal peptide compatibility. Recent innovations leverage computational tools to predict and design optimal signal peptides, enhancing scalability and reducing trial-and-error approaches.
Overall, SP recombinant proteins represent a cornerstone of modern biotechnology, balancing efficiency, cost, and functionality to meet diverse industrial and medical needs.
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