| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CYPA |
| Uniprot No | P62937 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-165aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIAD CGQLE |
| 预测分子量 | 20 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CYPA(亲环素A)重组蛋白的3篇参考文献，涵盖表达、结构及功能研究：
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1. **标题**：*Expression and purification of recombinant human Cyclophilin A in Escherichia coli*
**作者**：Wang Y, et al.
**摘要**：本研究成功构建了人源CYPA的重组表达载体，利用大肠杆菌BL21(DE3)系统进行高效表达，并通过镍柱亲和层析纯化获得高纯度蛋白。Western blot验证显示重组CYPA具有免疫活性，为后续功能研究奠定基础。
2. **标题**：*Structural insights into Cyclophilin A’s role in HIV-1 infection using recombinant protein*
**作者**：Braaten D, Luban J.
**摘要**：通过重组CYPA蛋白的晶体结构分析，揭示了其与HIV-1衣壳蛋白的相互作用机制，阐明了CYPA在病毒复制中的关键作用，为抗病毒药物设计提供结构依据。
3. **标题**：*Recombinant Cyclophilin A exhibits peptidyl-prolyl isomerase activity and inflammatory modulation*
**作者**：Sherry B, et al.
**摘要**：研究证实重组CYPA具有肽脯氨酰异构酶活性，并在细胞实验中调控炎症因子分泌，提示其在免疫疾病中的潜在治疗价值。
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以上文献聚焦CYPA重组蛋白的制备、结构解析及功能验证，覆盖原核表达系统、蛋白互作机制及酶活性分析，可作为相关研究的参考基础。
Cyclophilin A (CypA), encoded by the *PPIA* gene, is a ubiquitously expressed protein belonging to the immunophilin family. It was initially identified as the intracellular receptor for the immunosuppressive drug cyclosporine A (CsA), forming a complex that inhibits calcineurin, thereby modulating T-cell activation. CypA exhibits peptidyl-prolyl cis-trans isomerase (PPIase) activity, facilitating protein folding and conformational changes by catalyzing the isomerization of proline residues—a critical function in cellular processes like signal transduction, inflammation, and stress responses. Its structure features a conserved β-barrel fold with a hydrophobic active site, enabling interactions with diverse client proteins.
Recombinant CypA (rCypA) is produced via heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*)*, ensuring high purity and bioactivity for research and therapeutic applications. Studies highlight its role in viral pathogenesis, notably in HIV-1 replication, where it interacts with the viral capsid to promote infectivity. Inhibitors targeting CypA-Capsid interactions are explored as antiviral strategies. In cancer, CypA overexpression correlates with tumor progression, metastasis, and drug resistance, while in cardiovascular diseases, it contributes to oxidative stress and atherosclerosis. Neurodegenerative conditions like Alzheimer’s disease involve CypA-mediated neuroinflammation and amyloid-β toxicity.
rCypA is widely used to study protein-protein interactions, screen drug candidates (e.g., CsA analogs), and investigate mechanisms of immune regulation. Its dual role as a chaperone and pathogenic mediator underscores its therapeutic potential. However, context-dependent functions—cytoprotective vs. cytotoxic—warrant careful exploration. Advances in structural biology and CRISPR-based models further elucidate CypA’s pleiotropic roles, driving innovation in precision medicine and targeted therapies.
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