| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CPP |
| Uniprot No | Q01957 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-315aa |
| 氨基酸序列 | MFTFILMFYIGYGIDFNTWVANNNKHFTAVESLRRRAIFNMNARIVAENNRKETFKLSVDGPFAAMTNEEYNSLLKLKRSGEEKGEVRYLNIQAPKAVDWRKKGKVTPIRDQGNCGSCYTFGSIAALEGRLLIEKGGDSETLDLSEEHMVQCTREDGNNGCNGGLGSNVYNYIMENGIAKESDYPYTGSDSTCRSDVKAFAKIKSYNRVARNNEVELKAAISQGLVDVSIDASSVQFQLYKSGAYTDKQCKNNYFALNHEVCAVGYGVVDGKECWIVRNSWGTGWGEKGYINMVIEGNTCGVATDPLYPTGVEYL |
| 预测分子量 | 35 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3篇与CPP(细胞穿透肽)重组蛋白相关的参考文献及其摘要概括：
1. **《Cell-penetrating peptides: from molecular mechanisms to therapeutics》**
*作者：El-Andaloussi S, et al.*
摘要：综述了CPP在递送蛋白质、核酸等大分子中的应用机制，重点讨论了TAT肽与重组蛋白融合技术及其在疾病治疗中的潜力。
2. **《Engineering cell-permeable proteins through insertion of CPP motifs in loop regions》**
*作者：Fonseca SB, et al.*
摘要：提出一种将CPP(如poly-arginine)插入重组蛋白非结构化区域的方法，显著提高其细胞穿透效率，并在体外实验中验证了功能性蛋白的递送效果。
3. **《Fusion of a cell-penetrating peptide enhances antitumor immune response of a therapeutic cancer vaccine》**
*作者：Liu Z, et al.*
摘要：通过将CPP(如Penetratin)与肿瘤抗原重组蛋白融合，增强疫苗的树突状细胞摄取效率，显著提升小鼠模型中的抗肿瘤免疫应答。
**Background of CPP-Based Recombinant Proteins**
Cell-penetrating peptide (CPP)-based recombinant proteins are engineered biomolecules that combine the cell-membrane permeability of CPPs with the functional properties of recombinant proteins. CPPs, also known as protein transduction domains, are short peptides (typically 5–30 amino acids) capable of traversing cellular membranes. First identified in viral proteins (e.g., HIV-1 TAT) and endogenous proteins (e.g., Antennapedia), CPPs enable the intracellular delivery of cargoes, such as nucleic acids, drugs, or proteins, through energy-dependent or passive transport mechanisms. Their ability to bypass traditional endocytic pathways makes them valuable tools for overcoming the bioavailability limitations of therapeutic macromolecules.
Recombinant protein technology allows the fusion of CPP sequences with target proteins via genetic engineering. This involves cloning CPP-coding DNA into expression vectors alongside the gene encoding the protein of interest. The resulting fusion protein is produced in host systems (e.g., *E. coli*, yeast, or mammalian cells*)*, purified, and validated for bioactivity. CPP-recombinant proteins retain the functions of the original protein while gaining enhanced cellular uptake efficiency.
Applications span therapeutics and research. In drug development, CPP-fused proteins enable targeted delivery of anticancer agents, antibodies, or enzymes for diseases like cancer, genetic disorders, or metabolic deficiencies. In research, they facilitate intracellular delivery of probes, sensors, or CRISPR components for gene editing.
Challenges include optimizing CPP selectivity to reduce off-target effects, improving endosomal escape efficiency, and addressing potential immunogenicity. Recent advances focus on stimuli-responsive CPP designs and hybrid systems combining CPPs with targeting ligands to enhance specificity. These innovations position CPP-recombinant proteins as promising candidates for next-generation biologics and precision medicine.
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