| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CPD |
| Uniprot No | O75976 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 383-461aa |
| 氨基酸序列 | GVKGFVKDSITGSGLENATISVAGINHNITTGRFGDFYRLLVPGTYNLTVVLTGYMPLTVTNVVVKEGPATEVDFSLRP |
| 预测分子量 | 15.8 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. |
以下为3篇关于CPD(羧肽酶D)重组蛋白的参考文献，信息简明概括：
1. **文献名称**：*Expression and Characterization of Recombinant Carboxypeptidase D in Insect Cells*
**作者**：Smith J, et al.
**摘要**：本研究利用杆状病毒-昆虫细胞系统成功表达重组CPD蛋白，并通过质谱验证其金属羧肽酶活性，证明其在体外可高效切割病毒包膜糖蛋白，为病毒入侵机制研究提供工具。
2. **文献名称**：*Functional Analysis of Recombinant CPD Domains in pH-Dependent Substrate Processing*
**作者**：Lee H, Kim S.
**摘要**：通过大肠杆菌表达CPD的多个结构域重组蛋白，发现其C端结构域在酸性pH下对多肽底物的切割效率显著提升，揭示了CPD在细胞内运输过程中的pH依赖性功能调控机制。
3. **文献名称**：*Purification and Crystallization of Human CPD for Structural Studies*
**作者**：Zhang R, et al.
**摘要**：报道了人源CPD重组蛋白在HEK293细胞中的表达优化及结晶方法，获得2.8Å分辨率晶体结构，为基于结构的药物设计(如抗病毒抑制剂开发)奠定基础。
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**注**：以上文献为示例，实际研究中建议通过PubMed或Web of Science以关键词“recombinant carboxypeptidase D”检索最新论文。CPD常与乙型肝炎病毒(HBV)等病原体的宿主因子研究相关，可结合具体研究方向细化检索策略。
**Background of CPD Recombinant Proteins**
CPD (Circularly Permuted DARPins) recombinant proteins are engineered biomolecules derived from Designed Ankyrin Repeat Proteins (DARPins), a class of synthetic binding proteins known for their high stability, specificity, and versatility. Traditional DARPins are composed of repeated structural motifs that form a rigid scaffold capable of binding target antigens with antibody-like affinity. CPD technology introduces circular permutation—rearranging the protein sequence while maintaining the native fold—to create novel functional variants. This approach repositions the N- and C-termini of the protein, enabling new interaction surfaces or fusion sites for applications like multispecific targeting or conjugation.
The development of CPD recombinant proteins leverages advances in genetic engineering and structural biology. By combining computational design with directed evolution, researchers optimize these proteins for enhanced binding, solubility, and stability under diverse conditions. They are typically produced in microbial systems (e.g., *E. coli*) or mammalian cell cultures, ensuring scalability for therapeutic or diagnostic use.
CPD-based proteins have gained attention in biopharmaceuticals, particularly in oncology and immunotherapy. Their modular design allows for creating bispecific molecules that engage multiple disease targets simultaneously, such as linking tumor antigens to immune cells. Additionally, their small size and lack of disulfide bonds improve tissue penetration and reduce immunogenicity compared to antibodies.
Challenges include optimizing expression yields and ensuring proper folding in complex permutations. Despite this, CPD recombinant proteins represent a promising tool for precision medicine, offering tailored solutions for drug delivery, molecular imaging, and targeted therapies. Ongoing research focuses on expanding their functional diversity and translational potential.
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