| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PPIA |
| Uniprot No | P0AFL5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-190aa |
| 氨基酸序列 | AKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVI PGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSAT SQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQ NVPSKPVVILSAKVLP |
| 预测分子量 | 34 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PPIA(亲环素A)重组蛋白的3篇参考文献摘要：
1. **文献名称**：Expression and Purification of Recombinant Human Cyclophilin A (PPIA) in Escherichia coli
**作者**：Wang Y, et al.
**摘要**：本研究报道了在大肠杆菌中高效表达重组人亲环素A(PPIA)的优化方法，通过His标签亲和层析技术纯化获得高纯度蛋白，并验证其肽基脯氨酰异构酶活性，为后续功能研究提供基础。
2. **文献名称**：Structural Insights into the Functional Diversity of Cyclophilin A (PPIA) through Recombinant Protein Crystallography
**作者**：Li X, et al.
**摘要**：通过重组表达PPIA并进行X射线晶体学分析，揭示了其与免疫抑制剂环孢素A结合的分子机制，阐明了PPIA在细胞信号转导中的构象变化及其生物学意义。
3. **文献名称**：Role of Recombinant PPIA in HIV-1 Viral Replication: Implications for Therapeutic Targeting
**作者**：Smith J, et al.
**摘要**：该研究利用重组PPIA蛋白探究其与HIV-1衣壳蛋白的相互作用，证明PPIA通过促进病毒衣壳组装增强HIV-1感染效率，提示其作为抗病毒治疗靶点的潜力。
4. **文献名称**：Recombinant PPIA Modulates Oxidative Stress Response in Neurodegenerative Disease Models
**作者**：Chen L, et al.
**摘要**：研究发现重组PPIA可通过抑制线粒体凋亡通路减轻神经元氧化损伤，在帕金森病细胞模型中表现出神经保护作用，为神经退行性疾病治疗提供新思路。
注：以上文献为示例性内容，实际引用时需核对原文准确性。
**Background of Recomcombinant PPIA (Cyclophilin A)**
PPIA, or cyclophilin A (CyPA), is a ubiquitously expressed intracellular protein belonging to the immunophilin family, initially identified as a binding partner for the immunosuppressive drug cyclosporine A (CsA). It functions as a peptidyl-prolyl *cis-trans* isomerase (PPIase), catalyzing the isomerization of peptide bonds preceding proline residues, a critical step in protein folding and conformational regulation. PPIA plays roles in diverse cellular processes, including immune response modulation, apoptosis, and transcriptional regulation.
Recombinant PPIA is engineered through genetic cloning, typically expressed in *E. coli* or eukaryotic systems, ensuring high purity and activity for research or therapeutic applications. Its recombinant form retains enzymatic activity and structural integrity, enabling studies on its interaction with CsA, which inhibits PPIA’s PPIase activity, forming a complex that blocks calcineurin signaling in T-cells—a mechanism central to immunosuppression.
Beyond immunosuppression, PPIA is implicated in pathological conditions. It acts as a chemotactic factor when secreted under oxidative stress, promoting inflammation in diseases like atherosclerosis and rheumatoid arthritis. PPIA also facilitates viral replication (e.g., HIV-1 via interaction with viral capsid proteins) and is overexpressed in cancers, correlating with metastasis and drug resistance.
Research on recombinant PPIA focuses on structural analysis, drug discovery (e.g., CsA analogs), and understanding its extracellular roles in disease progression. Its dual function as a chaperone and signaling mediator makes it a valuable tool for probing protein-protein interactions, immune pathways, and therapeutic target validation. Challenges include optimizing expression systems to avoid misfolding and ensuring functional consistency across studies. Overall, recombinant PPIA remains pivotal in elucidating cyclophilin biology and developing targeted therapies.
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