| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PHB |
| Uniprot No | P35232 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-272aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIFTSI GEDYDERVLP SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ |
| 预测分子量 | 32 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PHB(Prohibitin或聚羟基丁酸酯相关蛋白)重组蛋白研究的**示例参考文献**(注：部分为虚构或简化内容，仅供参考)：
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1. **文献名称**: *"Heterologous Expression and Functional Analysis of Recombinant Prohibitin in Yeast Mitochondria"*
**作者**: Zhang Y. et al.
**摘要**: 研究通过酵母系统表达重组人源Prohibitin(PHB)蛋白，验证其在线粒体膜结构维持和氧化应激调控中的功能，为PHB在代谢疾病中的作用提供机制依据。
2. **文献名称**: *"Recombinant PHB Synthase Production and Its Role in Polyhydroxybutyrate Biosynthesis"*
**作者**: Tanaka K. et al.
**摘要**: 利用大肠杆菌表达重组PHB合酶，优化酶活性条件，并证明其在体外催化聚羟基丁酸酯(PHB)生物合成的高效性，为生物可降解材料生产提供新策略。
3. **文献名称**: *"Prohibitin-Targeted Nanoparticles for Cancer Therapy: A Recombinant Protein Approach"*
**作者**: Gupta R. et al.
**摘要**: 开发基于重组PHB蛋白的靶向药物递送系统，验证其在肿瘤细胞中特异性结合并抑制增殖的潜力，探索PHB作为癌症治疗靶点的应用。
4. **文献名称**: *"Structural Characterization of Recombinant Prohibitin-2 Complex and Its Role in Cellular Senescence"*
**作者**: Müller S. et al.
**摘要**: 通过重组表达纯化PHB2蛋白复合体，解析其晶体结构，揭示其与衰老相关信号通路的相互作用，为抗衰老研究提供分子基础。
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**注意**：以上文献为示例性质，实际研究需参考权威数据库(如PubMed、Web of Science)中的真实文献。若需具体文章，可进一步提供研究方向(如癌症、材料合成或结构生物学)。
**Background of PHB Recombinant Proteins**
Prohibitin (PHB) proteins, comprising PHB1 and PHB2. are evolutionarily conserved molecules found in eukaryotes. Initially identified for their anti-proliferative roles, PHBs form a heterodimeric complex localized primarily in the mitochondrial inner membrane, where they participate in maintaining mitochondrial integrity, cristae morphology, and metabolic regulation. Beyond mitochondria, PHBs are detected in the nucleus, cytoplasm, and cell membrane, implicating them in diverse processes such as transcriptional regulation, cell signaling, apoptosis, and stress responses.
Recombinant PHB proteins are engineered using expression systems like *E. coli*, yeast, or mammalian cells to study their structural and functional roles. These proteins retain key domains, such as the SPFH (stomatin/prohibitin/flotillin/HflK/C) domain, critical for membrane association and protein interactions. Recombinant PHBs enable *in vitro* investigations into their chaperone-like functions in stabilizing mitochondrial proteins (e.g., respiratory chain complexes) and their involvement in cellular pathways like RAS-RAF-MAPK signaling.
PHBs are linked to diseases, including cancer, neurodegeneration, and metabolic disorders. In cancer, PHBs exhibit dual roles—acting as tumor suppressors by stabilizing p53 or oncogenic drivers by promoting survival pathways. Recombinant PHB variants aid in deciphering these mechanisms and screening therapeutic agents. Challenges in PHB recombinant production include solubility issues and post-translational modifications, often addressed via fusion tags or mammalian expression systems.
Overall, PHB recombinant proteins serve as vital tools for unraveling mitochondrial biology, disease mechanisms, and potential therapeutic targeting, bridging gaps between structural insights and functional applications in biomedicine.
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