| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FKBP7 |
| Uniprot No | Q9Y680-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-218aa |
| 氨基酸序列 | MPKTMHFLFR FIVFFYLWGL FTAQRQKKEE STEEVKIEVL HRPENCSKTS KKGDLLNAHY DGYLAKDGSK FYCSRTQNEG HPKWFVLGVG QVIKGLDIAM TDMCPGEKRK VVIPPSFAYG KEGYAEGKIP PDATLIFEIE LYAVTKGPRS IETFKQIDMD NDRQLSKAEI NLYLQREFEK DEKPRDKSYQ DAVLEDIFKK NDHDGDGFIS PKEYNVYQ |
| 预测分子量 | 49 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3篇关于FKBP7重组蛋白的参考文献概览：
1. **《Recombinant human FKBP7 exhibits peptidyl-prolyl cis-trans isomerase activity and regulates collagen biosynthesis》**
- **作者**: Smith A, et al.
- **摘要**: 研究报道了在大肠杆菌中成功表达并纯化重组人源FKBP7蛋白，证实其具有脯氨酰异构酶活性，并发现其通过调控胶原蛋白折叠参与细胞外基质的形成。
2. **《FKBP7 interacts with heat shock proteins to modulate cellular stress response》**
- **作者**: Tanaka K, et al.
- **摘要**: 通过重组FKBP7蛋白的功能实验，揭示其与HSP90等分子伴侣的相互作用，在细胞应激条件下通过调节蛋白质稳态影响肿瘤细胞的生存能力。
3. **《Functional characterization of recombinant FKBP7 in neuronal differentiation》**
- **作者**: Lee S, et al.
- **摘要**: 利用哺乳动物细胞系统表达重组FKBP7.发现其通过调控Wnt信号通路促进神经干细胞分化，为神经系统发育相关研究提供了分子机制依据。
备注：以上文献信息为示例，实际引用时需以真实发表的论文内容为准。建议通过PubMed或Web of Science检索关键词“FKBP7 recombinant”获取最新研究。
FKBP7. a member of the FK506-binding protein (FKBP) family, is a peptidyl-prolyl cis-trans isomerase (PPIase) implicated in protein folding, cellular signaling, and stress responses. Structurally, it contains a conserved FKBP domain that binds immunosuppressive drugs like FK506 and rapamycin, though its biological functions extend beyond PPIase activity. FKBP7 is predominantly localized in the endoplasmic reticulum (ER) and secretory pathways, where it interacts with molecular chaperones such as HSP90 and GRP94. suggesting roles in protein quality control and ER homeostasis.
Studies highlight its involvement in neurodevelopment, cancer, and fibrosis. In the nervous system, FKBP7 regulates neuronal differentiation and axon guidance via interactions with collagen and extracellular matrix components. In cancer, it exhibits context-dependent roles: elevated FKBP7 correlates with poor prognosis in glioblastoma by promoting cell invasion, yet acts as a tumor suppressor in breast cancer by modulating TGF-β signaling. Its dysregulation is also linked to fibrotic diseases, where it may influence collagen biosynthesis and myofibroblast activation.
Recombinant FKBP7 is typically produced in bacterial or mammalian expression systems, enabling structural and functional studies. Purification via affinity tags (e.g., His-tag) facilitates research on its enzymatic activity, substrate binding, and interaction networks. Recombinant proteins serve as tools to dissect FKBP7's role in diseases and screen for small-molecule modulators. Additionally, they aid in antibody development for diagnostic applications. Despite progress, mechanistic details of FKBP7's dual roles in health and disease remain under investigation, emphasizing the need for further exploration using recombinant protein-based approaches.
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