| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSBP1 |
| Uniprot No | O75506 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-75aa |
| 氨基酸序列 | MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQK |
| 预测分子量 | 35.5kDa |
| 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HSBP1重组蛋白的3篇参考文献示例(注：内容为模拟概括，实际文献需根据具体研究检索)：
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1. **文献名称**：*HSBP1 regulates heat shock-induced protein aggregation by modulating chaperone activity*
**作者**：Zhang Y, et al.
**摘要**：本研究通过表达并纯化重组HSBP1蛋白，探究其在热应激条件下对分子伴侣HSP70的调控作用。实验表明，HSBP1通过抑制HSP70的ATP酶活性，影响错误折叠蛋白的再折叠过程，并促进蛋白聚集体的形成。
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2. **文献名称**：*Crystal structure of recombinant human HSBP1 reveals a novel α-helical dimerization motif*
**作者**：Lee S, et al.
**摘要**：作者利用大肠杆菌系统成功表达并纯化重组人源HSBP1蛋白，通过X射线晶体学解析其三维结构。研究发现，HSBP1通过独特的α螺旋二聚化结构域形成同源二聚体，为理解其与热休克因子(HSF)的相互作用机制提供结构基础。
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3. **文献名称**：*Functional characterization of HSBP1 in proteostasis and cellular stress response*
**作者**：Wang X, et al.
**摘要**：通过体外重组HSBP1蛋白实验，结合细胞敲除模型，揭示HSBP1在蛋白质稳态中的双重作用：低浓度时促进HSP70介导的折叠，高浓度时加速错误蛋白的聚集清除。研究提示HSBP1是细胞应激适应的关键调控因子。
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**备注**：以上文献信息为模拟生成，实际研究中请通过PubMed、Google Scholar等平台检索具体文献(关键词：HSBP1 recombinant, HSBP1 chaperone, HSBP1 structure)。
HSBP1 (Heat Shock Factor Binding Protein 1) is a conserved eukaryotic protein implicated in regulating the heat shock response (HSR), a critical cellular defense mechanism against proteotoxic stress. It interacts directly with heat shock factor 1 (HSF1), the master transcriptional regulator of molecular chaperones like HSP70 and HSP90. HSBP1 modulates HSF1 activity by forming a ternary complex with HSP70. acting as a negative feedback regulator to terminate the HSR once stress subsides. This fine-tuning prevents excessive chaperone production, maintaining cellular homeostasis.
Recombinant HSBP1 protein is engineered for in vitro studies to dissect its structural and functional roles. Typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems, it retains the ability to bind HSF1 and HSP70. enabling investigations into stress-response regulation. The protein’s small size (~12 kDa) and conserved coiled-coil domain structure facilitate interaction analyses via techniques like pull-down assays, surface plasmon resonance, or crystallography.
Research applications include:
1. **Mechanistic studies**: Elucidating how HSBP1-HSF1-HSP70 complexes disassemble to terminate HSR signaling.
2. **Disease models**: Exploring links between HSBP1 dysregulation and pathologies such as neurodegenerative diseases or cancer, where proteostasis failure is implicated.
3. **Therapeutic screening**: Testing compounds that modulate HSBP1 interactions to fine-tune stress response pathways.
Recent studies highlight its role beyond HSR, including involvement in ciliogenesis and developmental processes. Recombinant HSBP1 serves as a vital tool for probing cellular stress adaptation mechanisms and their broader physiological impacts.
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