纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | PPIF |
Uniprot No | P30405 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 30-207aa |
氨基酸序列 | C SKGSGDPSSS SSSGNPLVYL DVDANGKPLG RVVLELKADV VPKTAENFRA LCTGEKGFGY KGSTFHRVIP SFMCQAGDFT NHNGTGGKSI YGSRFPDENF TLKHVGPGVL SMANAGPNTN GSQFFICTIK TDWLDGKHVV FGHVKEGMDV VKKIESFGSK SGRTSKKIVI TDCGQLS |
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PPIF(Cyclophilin F)重组蛋白的3篇示例文献,格式为虚构内容,仅供参考:
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1. **文献名称**:*Recombinant human PPIF induces mitochondrial permeability transition in vitro*
**作者**:Zhang L, et al.
**摘要**:本研究成功在大肠杆菌中表达并纯化重组人源PPIF蛋白,证实其通过调控线粒体膜通透性转换孔(mPTP)促进细胞凋亡,为癌症治疗的靶点研究提供了实验依据。
2. **文献名称**:*Structural and functional characterization of recombinant Cyclophilin F (PPIF) in cardiac ischemia*
**作者**:Smith J, et al.
**摘要**:通过X射线晶体学解析了重组PPIF的三维结构,并发现其在心脏缺血再灌注损伤模型中通过结合线粒体蛋白ANT1加剧氧化应激反应,提示其作为心脏保护药物的潜在靶点。
3. **文献名称**:*Recombinant PPIF as a biomarker for neurodegenerative diseases*
**作者**:Wang Y, et al.
**摘要**:利用昆虫细胞系统表达重组PPIF蛋白,发现其在阿尔茨海默病模型小鼠脑脊液中异常聚集,并与tau蛋白磷酸化水平相关,提示其可能作为神经退行性疾病的生物标志物。
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**注意**:以上文献为示例,非真实存在。如需真实文献,建议通过PubMed或Google Scholar搜索关键词“PPIF recombinant protein”或“Cyclophilin F expression”获取最新研究。
PPIF (Peptidylprolyl Isomerase F), also known as cyclophilin D (CypD), is a mitochondrial matrix protein belonging to the cyclophilin family of peptidyl-prolyl cis-trans isomerases (PPIases). It plays a critical role in regulating the mitochondrial permeability transition pore (mPTP), a channel implicated in cell death pathways. Under stress conditions such as calcium overload or oxidative stress, PPIF facilitates mPTP opening, leading to mitochondrial swelling, loss of membrane potential, and release of pro-apoptotic factors. This process is closely associated with ischemia-reperfusion injury, neurodegenerative diseases, and aging.
Structurally, PPIF contains a conserved cyclophilin domain that binds immunosuppressive drugs like cyclosporine A (CsA), which inhibits its PPIase activity and blocks mPTP opening. Recombinant PPIF proteins are typically produced in *E. coli* or mammalian expression systems, often fused with tags (e.g., His-tag) for purification via affinity chromatography. These recombinant forms retain enzymatic activity and binding properties, enabling functional studies.
Research applications of recombinant PPIF include mechanistic studies of mPTP regulation, drug screening for inhibitors targeting mitochondrial dysfunction, and disease modeling. Its involvement in pathologies like heart failure and Alzheimer's disease has made it a therapeutic target, with efforts to develop PPIF-specific modulators. Additionally, recombinant PPIF serves as a tool to study protein folding, mitochondrial dynamics, and apoptosis signaling pathways. Despite its small size (~18-22 kDa), PPIF's central role in mitochondrial integrity underscores its significance in both basic research and translational medicine. Current challenges include elucidating its interaction partners and tissue-specific regulatory mechanisms. Ongoing studies aim to harness PPIF modulation for cytoprotective strategies in clinical settings.
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