| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FKBP11 |
| Uniprot No | Q9NYL4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-201aa |
| 氨基酸序列 | MTLRPSLLPLHLLLLLLLSAAVCRAEAGLETESPVRTLQVETLVEPPEPCAEPAAFGDTLHIHYTGSLVDGRIIDTSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGFPPSVPADAVVQYDVELIALIRANYWLKLVKGILPLVGMAMVPALLGLIGYHLYRKANRPKVSKKKLKEEKRNKSKKK |
| 分子量 | 48.6 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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FKBP11蛋白的3篇文献示例(内容基于研究方向推测，部分信息可能需要进一步验证)：
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1. **文献名称**: *Expression and purification of recombinant human FKBP11 in Escherichia coli: A peptidyl-prolyl cis-trans isomerase involved in endoplasmic reticulum stress*
**作者**: Zhang Y, et al.
**摘要**: 该研究成功构建了人源FKBP11的重组表达系统，利用大肠杆菌进行可溶性表达，并通过镍柱亲和层析纯化。实验表明重组FKBP11具有肽基脯氨酰异构酶活性，可能参与内质网未折叠蛋白应答(UPR)调控。
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2. **文献名称**: *FKBP11 modulates TGF-β signaling by mediating Smad protein stability in pulmonary fibrosis*
**作者**: Lee S, et al.
**摘要**: 研究发现FKBP11通过结合Smad2/3蛋白增强其稳定性，促进TGF-β信号通路激活，从而加剧肺纤维化进程。研究使用重组FKBP11蛋白进行体外相互作用实验，揭示了其在纤维化疾病中的潜在作用靶点。
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3. **文献名称**: *Structural insights into human FKBP11 by X-ray crystallography: Implications for substrate recognition*
**作者**: Gupta R, et al.
**摘要**: 通过X射线晶体学解析了重组人FKBP11的三维结构(分辨率2.1Å)，揭示了其催化口袋的保守氨基酸残基特征，并基于分子对接模拟提出其识别特定脯氨酸残基底物的分子机制。
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**备注**：以上文献为模拟示例，实际研究请通过PubMed或Web of Science以“FKBP11”和“recombinant protein”为关键词检索最新成果。真实文献可能集中于蛋白功能、疾病关联或结构解析等领域。
**Background of Recombinant Human FKBP11 Protein**
FKBP11 (FK506-binding protein 11) belongs to the FKBP family of immunophilins, characterized by their peptidyl-prolyl *cis-trans* isomerase (PPIase) activity. These proteins play roles in protein folding, chaperoning, and modulating signaling pathways by interacting with diverse molecular targets. Human FKBP11 is localized to the endoplasmic reticulum (ER) and is implicated in regulating secretory pathway dynamics, particularly in the processing of secretory proteins like digestive enzymes.
Recombinant human FKBP11 is produced via *in vitro* expression systems (e.g., *E. coli* or mammalian cells) to enable functional studies. Its recombinant form retains enzymatic activity and structural integrity, allowing researchers to explore its interactions with client proteins, calcium channels, or other ER-resident chaperones (e.g., BiP/GRP78). Studies suggest FKBP11 may influence ER stress responses, apoptosis, and diseases linked to protein misfolding, such as pancreatitis, cancer, and neurodegenerative disorders.
Research on recombinant FKBP11 also focuses on its potential as a therapeutic target or biomarker, given its dysregulation in certain pathologies. Structural analyses highlight conserved FKBP12-like domains and unique C-terminal motifs critical for substrate recognition. Current efforts aim to elucidate its precise mechanistic roles in cellular proteostasis and disease contexts, leveraging recombinant protein tools for *in vitro* assays or drug screening platforms.
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