纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PPIL5 |
Uniprot No | Q96L50 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-414 aa |
活性数据 | MKLHCEVEVI SRHLPALGLR NRGKGVRAVL SLCQQTSRSQ PPVRAFLLIS TLKDKRGTRY ELRENIEQFF TKFVDEGKAT VRLKEPPVDI CLSKAISSSL KGFLSAMRLA HRGCNVDTPV STLTPVKTSE FENFKTKMVI TSKKDYPLSK NFPYSLEHLQ TSYCGLVRVD MRMLCLKSLR KLDLSHNHIK KLPATIGDLI HLQELNLNDN HLESFSVALC HSTLQKSLRS LDLSKNKIKA LPVQFCQLQE LKNLKLDDNE LIQFPCKIGQ LINLRFLSAA RNKLPFLPSE FRNLSLEYLD LFGNTFEQPK VLPVIKLQAP LTLLESSART ILHNRIPYGS HIIPFHLCQD LDTAKICVCG RFCLNSFIQG TTTMNLHSVA HTVVLVDNLG GTEAPIISYF CSLGCYVNSS DMLK |
分子量 | 46.7 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. |
以下是关于重组人PPIL5蛋白的假设性参考文献示例(注:实际文献可能需要通过数据库检索获取):
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1. **文献名称**: "Expression and Functional Characterization of Recombinant Human PPIL5 in Cancer Cell Proliferation"
**作者**: Zhang Y, et al.
**摘要**: 该研究通过大肠杆菌系统成功表达了重组人PPIL5蛋白,并证明其具有肽酰-脯氨酰异构酶活性。功能实验表明,PPIL5通过调节特定信号通路(如Wnt/β-catenin)促进肿瘤细胞增殖,提示其可能作为癌症治疗靶点。
2. **文献名称**: "Crystal Structure Analysis of PPIL5 Reveals Substrate Binding Specificity"
**作者**: Wang X, et al.
**摘要**: 本研究首次解析了重组人PPIL5蛋白的晶体结构(分辨率2.1Å),揭示了其活性位点关键氨基酸残基对底物结合的选择性,为设计靶向PPIL5的小分子抑制剂提供了结构基础。
3. **文献名称**: "PPIL5 Interacts with Spliceosomal Components via Recombinant Protein Affinity Assay"
**作者**: Li H, et al.
**摘要**: 通过重组PPIL5的体外pull-down实验,发现其与剪接体蛋白(如SF3B1)存在直接相互作用,暗示PPIL5可能参与RNA剪接调控,拓展了PPIL家族蛋白的功能认知。
4. **文献名称**: "PPIL5 Deficiency Leads to Neuronal Protein Misfolding in Alzheimer's Models"
**作者**: Chen L, et al.
**摘要**: 研究利用重组PPIL5蛋白进行体外蛋白折叠拯救实验,发现在阿尔茨海默病模型中,PPIL5通过协助tau蛋白正确折叠减轻神经毒性,提示其潜在治疗神经退行性疾病的价值。
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注:以上文献信息为模拟示例,实际引用时需以真实出版物为准。建议通过PubMed或Web of Science检索具体文献。
Recombinant human PPIL5 (peptidylprolyl isomerase like 5) protein belongs to the peptidyl-prolyl cis-trans isomerase (PPIase) family, enzymes that catalyze the isomerization of peptide bonds preceding proline residues—a critical step in protein folding, trafficking, and functional regulation. PPIL5 is structurally characterized by a conserved PPIase domain, though its enzymatic activity remains less characterized compared to other PPIases like cyclophilins or FK506-binding proteins (FKBPs). It is encoded by the *PPIL5* gene located on human chromosome 14 and is expressed in various tissues, with higher levels observed in the brain, suggesting potential roles in neuronal function or development.
PPIL5 has been implicated in mRNA splicing regulation through interactions with spliceosome components, notably the CDC5L complex, linking it to post-transcriptional gene expression control. Additionally, studies associate PPIL5 with cancer progression, where altered expression correlates with tumor aggressiveness and patient prognosis, possibly via modulating cell cycle or apoptosis-related pathways. As a recombinant protein, PPIL5 is typically produced in *E. coli* or mammalian expression systems, enabling structural, biophysical, and functional studies. Its recombinant form is essential for investigating molecular mechanisms in vitro, drug discovery targeting PPIase-related diseases, and exploring its enigmatic roles in cellular processes beyond traditional folding assistance. Research gaps persist in understanding its substrate specificity, physiological partners, and disease-specific contributions.
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