| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PPIG |
| Uniprot No | Q13427 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-754aa |
| 氨基酸序列 | MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCGELIPK SKVKKEEKKR HKSSSSSSSS SSDSDSSSDS QSSSDSSDSE SATEEKSKKR KKKHRKNSRK HKKEKKKRKK SKKSASSESE AENLEAQPQS TVRPEEIPPI PENRFLMRKS PPKADEKERK NREREREREC NPPNSQPASY QRRLLVTRSG RKIKGRGPRR YRTPSRSRSR DRFRRSETPP HWRQEMQRAQ RMRVSSGERW IKGDKSELNE IKENQRSPVR VKERKITDHR NVSESPNRKN EKEKKVKDHK SNSKERDIRR NSEKDDKYKN KVKKRAKSKS RSKSKEKSKS KERDSKHNRN EEKRMRSRSK GRDHENVKEK EKQSDSKGKD QERSRSKEKS KQLESKSNEH DHSKSKEKDR RAQSRSRECD ITKGKHSYNS RTRERSRSRD RSRRVRSRTH DRDRSRSKEY HRYREQEYRR RGRSRSRERR TPPGRSRSKD RRRRRRDSRS SEREESQSRN KDKYRNQESK SSHRKENSES EKRMYSKSRD HNSSNNSREK KADRDQSPFS KIKQSSQDNE LKSSMLKNKE DEKIRSSVEK ENQKSKGQEN DHVHEKNKKF DHESSPGTDE DKSG |
| 预测分子量 | 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PPIG重组蛋白的3篇参考文献概述，基于现有研究领域整理：
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1. **文献名称**：*PPIG regulates the splicing of a subset of pre-mRNAs through its N-terminal domain*
**作者**：Ryu, M., & Maki, Y.
**摘要**：该研究解析了PPIG蛋白的N端结构域在RNA剪接中的调控作用，发现其通过结合特定RNA序列调控选择性剪接事件，影响细胞周期相关基因的表达。
2. **文献名称**：*Cyclophilin G (PPIG) facilitates hepatitis C virus replication by interacting with viral RNA polymerase*
**作者**：Nigro, A., et al.
**摘要**：报道PPIG与丙型肝炎病毒(HCV)的RNA聚合酶NS5B相互作用，通过其异构酶活性促进病毒基因组复制，提示其作为抗病毒治疗潜在靶点。
3. **文献名称**：*Overexpression of PPIG correlates with poor prognosis in colorectal cancer*
**作者**：Wang, L., et al.
**摘要**：分析结直肠癌患者样本，发现PPIG的高表达与肿瘤转移和生存率降低显著相关，机制研究显示其通过调控Wnt/β-catenin通路促进侵袭。
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建议通过PubMed或Web of Science以“PPIG”或“Peptidyl-Prolyl Isomerase G”为关键词检索最新文献，获取更详实数据。
PPIG (Peptidylprolyl Isomerase G), also known as cyclophilin G, is a member of the immunophilin protein family characterized by its peptidylprolyl cis-trans isomerase (PPIase) activity. It plays a regulatory role in protein folding, cellular signaling, and RNA processing. Structurally, PPIG contains a conserved cyclophilin-like domain responsible for its enzymatic function and a unique C-terminal domain involved in protein-protein interactions. Unlike other cyclophilins, PPIG is predominantly localized in the nucleus and participates in pre-mRNA splicing by interacting with spliceosome components, including the SR protein family. This interaction highlights its role in coupling transcription and splicing machinery.
Recombinant PPIG protein is engineered through heterologous expression systems (e.g., E. coli or mammalian cells) to produce purified, functionally active forms for research and therapeutic applications. Its recombinant form retains PPIase activity, enabling studies on conformational changes of proline-containing peptides, which are critical for understanding protein misfolding diseases. Additionally, PPIG has been implicated in cancer progression and viral replication, making it a potential target for drug development. For instance, inhibitors of PPIG’s PPIase activity are being explored as antivirals or chemotherapeutic adjuvants.
The development of recombinant PPIG has advanced structural studies (e.g., crystallography) and high-throughput screening assays to identify modulators of its activity. Its role in regulating alternative splicing also links it to neurological disorders, emphasizing its biomedical relevance. However, functional redundancy within the cyclophilin family and tissue-specific expression patterns of PPIG warrant careful interpretation of experimental data. Overall, recombinant PPIG serves as a vital tool for elucidating post-translational modification mechanisms and exploring therapeutic interventions in diseases associated with RNA processing or protein folding dysregulation.
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