| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FKBP2 |
| Uniprot No | P26885 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-142aa |
| 氨基酸序列 | ATGAEGKRKLQIGVKKRVDHCPIKSRKGDVLHMHYTGKLEDGTEFDSSLP QNQPFVFSLGTGQVIKGWDQGLLGMCEGEKRKLVIPSELGYGERGAPPKI PGGATLVFEVELLKIERRTELVDHHHHHH |
| 预测分子量 | 14 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FKBP2重组蛋白的模拟参考文献示例(注：文献信息为虚构，仅供格式参考)：
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1. **文献名称**: *Recombinant FKBP2 promotes protein folding in vitro*
**作者**: Zhang L. et al.
**摘要**: 本研究在大肠杆菌中成功表达并纯化了重组人FKBP2蛋白，验证其体外促进底物蛋白正确折叠的分子伴侣功能，并揭示其通过肽基脯氨酰异构酶活性加速折叠速率。
2. **文献名称**: *FKBP2 interacts with TGF-β receptors and modulates signaling*
**作者**: Kim S., Patel R.
**摘要**: 通过哺乳动物细胞表达重组FKBP2.发现其与TGF-β受体复合物直接结合，调控SMAD通路活性，提示FKBP2在细胞分化与纤维化疾病中的潜在作用。
3. **文献名称**: *Structural analysis of FKBP2 reveals a unique substrate-binding pocket*
**作者**: Watanabe T. et al.
**摘要**: 利用X射线晶体学解析重组FKBP2的三维结构，发现其活性位点具有独特的疏水腔结构，为设计靶向FKBP2的小分子抑制剂提供结构基础。
4. **文献名称**: *FKBP2 overexpression enhances neuronal survival in Alzheimer's models*
**作者**: Chen H. et al.
**摘要**: 在神经细胞中过表达重组FKBP2.显著减少tau蛋白异常磷酸化并抑制凋亡，表明其在神经退行性疾病中的保护机制可能与错误蛋白清除相关。
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建议通过PubMed或Web of Science检索真实文献，关键词如 "recombinant FKBP2" 或 "FKBP11"(注：FKBP2又名FKBP11)。
**Background of FKBP2 Recombinant Protein**
FKBP2 (FK506-binding protein 2), also known as FKBP13. is a member of the immunophilin family characterized by its peptidyl-prolyl isomerase (PPIase) activity. It plays a regulatory role in protein folding, trafficking, and signaling by catalyzing the cis-trans isomerization of proline residues, a rate-limiting step in conformational changes of polypeptides. Structurally, FKBP2 contains a conserved FK506-binding domain that interacts with immunosuppressive drugs like FK506 and rapamycin, though its biological functions extend beyond immunosuppression.
This protein is predominantly localized in the endoplasmic reticulum (ER), where it associates with molecular chaperones such as BiP/GRP78 and calnexin, aiding in the quality control of nascent glycoproteins. FKBP2 also modulates calcium signaling and ER stress responses, linking it to cellular homeostasis and apoptosis. Its expression is tissue-specific, with elevated levels observed in secretory cells and organs like the pancreas and liver.
Recombinant FKBP2 is produced via heterologous expression systems (e.g., E. coli or mammalian cells) to study its biochemical properties and interactions. Researchers utilize it to explore PPIase-dependent mechanisms, screen for small-molecule inhibitors, or investigate its role in diseases. For instance, dysregulation of FKBP2 has been implicated in neurodegenerative disorders, cancer progression, and diabetes, where ER stress and protein misfolding are central pathophysiological features.
The recombinant form enables precise analysis of FKBP2’s structure-function relationships and its potential as a therapeutic target, offering insights into diseases associated with proteostatic imbalance.
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