| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CYP-40 |
| Uniprot No | Q9C566 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-361aa |
| 氨基酸序列 | MGRSKCFMDISIGGELEGRIVIELYDDVVPKTAENFRLLCTGEKGLGPNTGVPLHYKGNRFHRVIKGFMIQGGDISANDGTGGESIYGLKFDDENFELKHERKGMLSMANSGPNTNGSQFFITTTRTSHLDGKHVVFGRVTKGMGVVRSIEHVSIEEQSCPSQDVVIHDCGEIPEGADDGICDFFKDGDVYPDWPIDLNESPAELSWWMETVDFVKAHGNEHFKKQDYKMALRKYRKALRYLDICWEKEGIDEETSTALRKTKSQIFTNSAACKLKFGDAKGALLDTEFAMRDEDNNVKALFRQGQAYMALNNVDAAAESLEKALQFEPNDAGIKKEYAAVMKKIAFRDNEEKKQYRKMFV |
| 预测分子量 | 40,6 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CYP-40(Cyclophilin 40)重组蛋白的3篇代表性文献的概括(文献信息为模拟示例，仅供参考)：
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1. **文献名称**：*Recombinant Cyclophilin 40: Expression in E. coli and Chaperone Activity Analysis*
**作者**：Smith A, et al.
**摘要**：本研究报道了在大肠杆菌系统中高效表达并纯化重组CYP-40蛋白，验证其作为分子伴侣与HSP90的相互作用，并证实其在甾体激素受体复合物组装中的功能。
2. **文献名称**：*Structural Characterization of Human Cyclophilin 40 Using Recombinant Protein Crystallography*
**作者**：Jones R, et al.
**摘要**：通过昆虫细胞表达系统获得高纯度重组CYP-40.利用X射线晶体学解析其三维结构，揭示了其TPR结构域在结合客户蛋白中的关键作用。
3. **文献名称**：*Role of Recombinant CYP40 in Amyloid-β Aggregation: Implications for Alzheimer’s Disease*
**作者**：Chen L, et al.
**摘要**：研究重组CYP-40对β-淀粉样蛋白聚集的抑制作用，发现其通过调节错误折叠蛋白的构象，可能成为神经退行性疾病的潜在治疗靶点。
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**备注**：以上文献为示例性质，实际研究中建议通过PubMed、Web of Science等数据库，以关键词“Cyclophilin 40 recombinant”或“CYP40 protein purification”检索最新文献。若用户所指为细胞色素P450家族成员(如CYP3A4)，需调整关键词重新筛选。
**Background of CYP-40 Recombinant Protein**
CYP-40. also known as Cyclophilin 40 (CyP40), belongs to the cyclophilin family of proteins characterized by peptidyl-prolyl isomerase (PPIase) activity, which facilitates protein folding by catalyzing the cis-trans isomerization of proline residues. It is a 40 kDa protein initially identified through its interaction with heat shock protein 90 (HSP90), a molecular chaperone critical for the maturation of steroid hormone receptors and other signaling proteins. Unlike other cyclophilins, CYP-40 contains a unique C-terminal domain that enhances its binding to the HSP90 complex, positioning it as a key regulator of chaperone-mediated processes.
Recombinant CYP-40 protein is produced via genetic engineering in heterologous expression systems (e.g., *E. coli* or mammalian cells), enabling high-purity, scalable production for research. Its recombinant form retains PPIase activity and chaperone functionality, making it a valuable tool for studying HSP90-dependent pathways, protein folding dynamics, and cellular stress responses.
CYP-40 has been implicated in diverse physiological and pathological contexts. It plays roles in steroid receptor signaling, apoptosis, and immune regulation. Notably, it interacts with the glucocorticoid receptor (GR) and estrogen receptor (ER), influencing hormone-responsive gene expression. Dysregulation of CYP-40 has been linked to cancers, neurodegenerative disorders (e.g., Alzheimer’s disease via tau aggregation), and viral infections, where it may assist viral replication.
In drug discovery, CYP-40 is explored as a target for immunosuppressants and anticancer agents, leveraging its PPIase activity. However, its dual role in promoting and inhibiting disease pathways complicates therapeutic strategies. Research using recombinant CYP-40 continues to unravel its structural nuances, post-translational modifications, and interactions, offering insights into its therapeutic potential and mechanistic contributions to cellular homeostasis.
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