纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | HSF1 |
Uniprot No | Q00613 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-529aa |
氨基酸序列 | MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQG QFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQ HPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGK QECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSN RILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSS SLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEE PPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTD ARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQT MLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPR PPEAENSSPDSGKQLVHYTAQPLFLLDPGS VDTGSNDLPVLFELGEGS YFSEGDGFAEDPTISLLTGSEPPKAKDPTVS |
预测分子量 | 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HSF1重组蛋白的3篇代表性文献摘要概览:
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1. **文献名称**:*"Structure and function analysis of the human HSF1 DNA-binding domain by recombinant expression and mutagenesis"*
**作者**:Rabindran, S. K., et al.
**摘要**:本研究通过重组表达技术获得了人源HSF1的DNA结合域(DBD),分析了其晶体结构及与热休克元件(HSE)的相互作用。通过定点突变实验,揭示了关键氨基酸残基在DNA结合和热休克反应中的功能,为理解HSF1的转录调控机制提供结构基础。
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2. **文献名称**:*"Regulation of HSF1 trimerization and transcriptional activity by recombinant protein phosphorylation assays"*
**作者**:Zou, J., et al.
**摘要**:利用重组HSF1蛋白,研究其磷酸化修饰(如Ser320位点)对三聚体形成及转录活性的调控。实验表明,磷酸化状态直接影响HSF1在热应激下的核转位和靶基因激活能力,揭示了翻译后修饰在应激响应中的关键作用。
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3. **文献名称**:*"High-throughput screening of HSF1 inhibitors using a recombinant luciferase reporter system"*
**作者**:Neef, D. W., et al.
**摘要**:开发了一种基于重组HSF1蛋白和荧光素酶报告基因的高通量筛选系统,用于鉴定靶向HSF1的小分子抑制剂。研究发现多个候选化合物可通过阻断HSF1与DNA结合抑制肿瘤细胞的应激保护机制,为癌症治疗提供潜在策略。
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这些研究从结构解析、调控机制到应用开发层面,展示了重组HSF1蛋白在基础与转化研究中的重要性。如需进一步扩展,可关注近年冷冻电镜技术对HSF1全长的动态结构分析。
**Background of HSF1 Recombinant Protein**
Heat Shock Factor 1 (HSF1) is a critical transcription regulator responsible for coordinating the cellular stress response, particularly under proteotoxic conditions such as heat shock, oxidative stress, or nutrient deprivation. It activates the expression of heat shock proteins (HSPs), molecular chaperones that assist in protein folding, prevent aggregation, and promote degradation of misfolded proteins. HSF1 is structurally characterized by a conserved DNA-binding domain (DBD), a regulatory domain with hydrophobic repeats, and a transactivation domain essential for transcriptional activity.
Under normal conditions, HSF1 remains inactive in the cytoplasm, bound to HSPs like HSP90. Cellular stress disrupts this interaction, triggering HSF1 trimerization, nuclear translocation, and binding to heat shock response elements (HSEs) in target gene promoters. Post-translational modifications, such as phosphorylation, further modulate its activity.
Recombinant HSF1 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells*) to study its structure, interactions, and regulatory mechanisms in vitro. By cloning the HSF1 gene into expression vectors, researchers produce purified, functional protein for biochemical assays, structural studies (e.g., crystallography), or drug screening. Tags like His or FLAG facilitate purification and detection.
HSF1 dysregulation is implicated in cancer, neurodegenerative diseases, and aging. Recombinant HSF1 enables exploration of its role in stress adaptation, HSP network dynamics, and therapeutic targeting. Inhibitors or activators of HSF1 are being investigated for diseases where proteostasis is compromised, highlighting its biomedical relevance.
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