| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HOP |
| Uniprot No | Q9BPY8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-73aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMSAETA SGPTEDQVEI LEYNFNKVDK HPDSTTLCLI AAEAGLSEEE TQKWFKQRLA KWRRSEGLPS ECRSVTD |
| 预测分子量 | 11 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HOP重组蛋白的3篇代表性文献概览：
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1. **文献名称**：*Structural insights into the Hsp70-Hsp90 organizing protein (HOP) reveals a modular architecture*
**作者**：Johnson, J.L., et al.
**摘要**：通过X射线晶体学解析HOP重组蛋白的三维结构，揭示其包含TPR结构域和功能模块的模块化设计，阐明其作为Hsp70/Hsp90分子伴侣复合体“桥梁”的结构基础。
2. **文献名称**：*Functional characterization of recombinant HOP in the assembly of Hsp70-Hsp90 chaperone machinery*
**作者**：Smith, D.M., et al.
**摘要**：体外重组表达HOP蛋白，验证其通过TPR结构域分别结合Hsp70和Hsp90的能力，证明其在调控客户蛋白折叠中的动态协调作用。
3. **文献名称**：*HOP overexpression modulates tau aggregation and Alzheimer's disease pathology in cellular models*
**作者**：Lee, S., et al.
**摘要**：利用重组HOP蛋白研究其与Tau蛋白的相互作用，发现HOP通过调节分子伴侣网络抑制Tau异常聚集，为神经退行性疾病治疗提供潜在靶点。
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**注**：以上文献为示例性质，实际引用需根据具体研究主题补充真实文献信息。建议通过PubMed或Web of Science以关键词“HOP protein recombinant”或“Hsp70-Hsp90 organizing protein”检索最新研究。
**Background of HOP Recombinant Protein**
HOP (HSP70-HSP90 Organizing Protein), also known as STIP1 (Stress-Induced Phosphoprotein 1), is a co-chaperone that plays a pivotal role in coordinating the functional interplay between two major molecular chaperones, HSP70 and HSP90. These chaperones are critical for maintaining protein homeostasis by facilitating the folding, stabilization, and maturation of client proteins, particularly signaling molecules like steroid hormone receptors and kinases. HOP acts as an adaptor, bridging HSP70 and HSP90 through its tetratricopeptide repeat (TPR) domains, enabling the transfer of client proteins between the two chaperone systems during stress responses or normal cellular processes.
Recombinant HOP protein is engineered using genetic cloning techniques, where the *HOP* gene is inserted into expression vectors (e.g., bacterial, yeast, or mammalian systems) to produce purified protein for functional studies. Its recombinant form retains the ability to interact with HSP70/HSP90. making it a valuable tool for dissecting chaperone-mediated protein folding mechanisms. Researchers utilize HOP recombinant protein to investigate its role in diseases linked to proteostasis dysregulation, including cancer, neurodegenerative disorders (e.g., Alzheimer’s), and viral infections, where chaperone systems are often hijacked.
Despite its importance, challenges remain in optimizing recombinant HOP production due to its multidomain structure and post-translational modifications. Advances in structural biology and biophysical assays continue to unravel its conformational dynamics and interactions, offering insights into therapeutic targeting. By modulating HOP activity, novel strategies could emerge to restore proteostasis in pathological conditions, underscoring its biomedical relevance.
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