| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PPIC |
| Uniprot No | P45877 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-182aa |
| 氨基酸序列 | MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEY QGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQL KEFLDANLAGSGSGHMHHHHHHSSGLVPRGSGMKETAAAKFERQHMDSPD LGTDDDDKAMAKRGPSVTAKVFFDVRIGDKDVGRIVIGLFGKVVPKTVEN FVALATGEKGYGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYGETFPD ENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDG MTVVHSIELQATD |
| 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PPIC重组蛋白的3-4条参考文献示例，包含文献名称、作者及摘要概括：
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1. **文献名称**：*High-yield Expression and Purification of Recombinant PPIC in E. coli*
**作者**：Zhang et al. (2020)
**摘要**：研究提出了一种在大肠杆菌中高效表达和纯化重组PPIC的优化方案，通过调整诱导温度、IPTG浓度和亲和层析步骤，获得了高纯度、高活性的PPIC蛋白，适用于功能与结构研究。
2. **文献名称**：*Crystal Structure Analysis of PPIC Reveals Key Residues for Catalytic Activity*
**作者**：Smith et al. (2018)
**摘要**：利用X射线晶体学解析了重组PPIC的三维结构，揭示了其催化活性中心的关键氨基酸残基，并发现与免疫抑制剂环孢菌素A的结合模式，为靶向药物设计提供依据。
3. **文献名称**：*Functional Characterization of Recombinant PPIC in Protein Folding Assays*
**作者**：Lee et al. (2019)
**摘要**：通过体外酶活性和分子伴侣功能实验，证明重组PPIC能够加速底物蛋白的折叠速率，并验证其在细胞应激反应中对错误折叠蛋白的修复作用。
4. **文献名称**：*Recombinant PPIC as a Therapeutic Target in Inflammatory Diseases*
**作者**：Wang et al. (2021)
**摘要**：在小鼠炎症模型中，重组PPIC的活性抑制显著降低了促炎因子水平，表明其可能成为治疗自身免疫疾病的新靶点。
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**注**：以上文献为示例性内容，实际引用时建议通过学术数据库(如PubMed、Web of Science)检索真实文献。如需进一步协助定位具体论文，可提供更详细的研究方向或关键词。
**Background of PPIC Recombinant Protein**
PPIC (Peptidyl-Prolyl *cis-trans* Isomerase C), also known as cyclophilin C, belongs to the cyclophilin family of proteins characterized by their peptidyl-prolyl isomerase (PPIase) activity. This enzymatic function enables PPIC to catalyze the *cis-trans* isomerization of proline residues, a rate-limiting step in protein folding. PPIC shares structural homology with other cyclophilins, including a conserved catalytic domain, but exhibits tissue-specific expression patterns, predominantly in immune cells and tissues like the liver and kidneys.
Recombinant PPIC is produced through genetic engineering, often using bacterial (e.g., *E. coli*) or mammalian expression systems. Its recombinant form retains the native protein’s functional properties, including binding to immunosuppressive drugs like cyclosporin A (CsA), which inhibits PPIC’s PPIase activity. This interaction highlights PPIC’s role in modulating immune responses, as cyclophilins are implicated in T-cell activation and inflammation regulation.
Beyond its canonical role in protein folding, PPIC is involved in diverse cellular processes, such as apoptosis, signal transduction, and viral replication. Studies link PPIC to pathologies including hepatitis C virus (HCV) propagation, where it interacts with viral proteins to facilitate infection. In neurodegenerative diseases, aberrant PPIC activity may contribute to protein misfolding aggregates, such as amyloid-β plaques in Alzheimer’s disease.
Therapeutic interest in recombinant PPIC stems from its dual utility as a research tool and a potential drug target. It aids in studying protein interactions, immune pathways, and viral mechanisms, while inhibitors targeting PPIC’s active site are explored for treating inflammatory and infectious diseases. However, challenges remain in optimizing recombinant PPIC production for stability and post-translational modifications critical for its biological activity.
In summary, PPIC recombinant protein serves as a vital resource for understanding protein dynamics, immune regulation, and disease mechanisms, with translational applications in drug discovery and biotechnology.
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