纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | PPIL2 |
Uniprot No | Q13356 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-520aa |
氨基酸序列 | MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK IIDPDEEKAK QDPSYYLKNT NAETRETLQE LYKEFKGDEI LAATMKAPEK KKVDKLNAAH YSTGKVSASF TSTAMVPETT HEAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV GKYINPAATK RAAEEEPSTS ATVPMSKKKP SRGFGDFSSW |
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. |
以下是模拟生成的关于PPIL2重组蛋白的参考文献示例(仅供参考,具体文献需通过学术数据库检索确认):
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1. **Zhang, Y. et al.**
*"Expression and enzymatic characterization of recombinant human PPIL2 in E. coli"*
摘要:本研究成功在大肠杆菌中克隆表达并纯化了重组人PPIL2蛋白,通过圆二色光谱验证其正确折叠,并证实其具有肽脯氨酰顺反异构酶活性,为后续功能研究提供基础。
2. **Lee, S. et al.**
*"PPIL2 interacts with Smad3 via its cyclophilin-like domain and modulates TGF-β signaling"*
摘要:利用重组PPIL2蛋白进行Pull-down实验,发现其通过亲环素结构域与Smad3蛋白结合,调控TGF-β信号通路,提示PPIL2可能在细胞分化中起关键作用。
3. **Chen, X. & Wang, L.**
*"Crystal structure of PPIL2 reveals substrate binding specificity"*
摘要:通过X射线晶体学解析重组PPIL2的三维结构,阐明其底物结合口袋的氨基酸残基特征,为设计靶向PPIL2的小分子抑制剂提供结构基础。
4. **Smith, J. et al.**
*"Overexpression of recombinant PPIL2 promotes tumor cell migration in vitro"*
摘要:在乳腺癌细胞中过表达重组PPIL2.发现其通过激活MAPK通路增强细胞迁移能力,提示PPIL2可能作为癌症治疗的潜在靶点。
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**注意**:以上为模拟示例,实际文献需通过PubMed、Web of Science或Google Scholar等平台,以关键词“PPIL2 recombinant protein”“PPIL2 function”等检索。部分真实研究可能涉及PPIL2在剪接体组装、病毒感染或自身免疫疾病中的功能。
PPIL2 (Peptidylprolyl Isomerase L2), a member of the cyclophilin family, is a protein-coding gene that plays a role in protein folding and cellular signaling. It encodes an enzyme with peptidyl-prolyl cis-trans isomerase (PPIase) activity, facilitating the conformational changes of proline-containing peptides during post-translational modifications. PPIL2 is structurally characterized by a conserved PPIase domain, which binds to cyclosporine A (CsA) and catalyzes isomerization reactions critical for protein stability, trafficking, and interaction networks.
Recombinant PPIL2 protein is engineered through genetic expression systems (e.g., E. coli or mammalian cell lines) to produce purified, functional proteins for research and therapeutic applications. Its recombinant form retains enzymatic activity and is widely used to study PPIL2's biological roles, including involvement in cell cycle regulation, RNA processing, and immune response modulation. Emerging studies suggest its association with diseases such as cancer, neurodegenerative disorders, and viral infections, positioning it as a potential therapeutic target. For instance, PPIL2 interacts with viral proteins, influencing viral replication, and may contribute to tumor progression via pathways like Wnt/β-catenin signaling.
In drug discovery, recombinant PPIL2 serves as a tool for screening inhibitors or modulators of PPIase activity. Its role as a molecular chaperone also makes it valuable in biomanufacturing to enhance recombinant protein yields. Despite functional overlap with other cyclophilins, PPIL2's distinct expression patterns and substrate preferences highlight its unique contributions to cellular processes. Ongoing research aims to clarify its mechanistic nuances and explore its diagnostic or therapeutic potential in precision medicine.
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