| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSF2 |
| Uniprot No | Q03933 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 411-536aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSENKGLETTKNNVVQPVSEEGRKSKSKPD KQLIQYTAFPLLAFLDGNPASSVEQASTTASSEVLSSVDKPIEVDELLDS SLDPEPTQSKLVRLEPLTEA EASEATLFYLCELAPAPLDSDMPLLDS |
| 预测分子量 | 16 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HSF2重组蛋白的3篇参考文献示例：
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1. **文献名称**: *"Cloning and Functional Analysis of Recombinant Human HSF2 in Stress Response"*
**作者**: Mathew, A., et al.
**摘要**: 该研究通过原核表达系统成功克隆并纯化了人源HSF2重组蛋白，证明其在热应激条件下能特异性结合DNA，并调控下游靶基因HSP70的表达，揭示了HSF2在细胞应激反应中的关键作用。
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2. **文献名称**: *"Structural Insights into HSF2-DNA Interaction via Recombinant Protein Crystallography"*
**作者**: Vihervaara, T., et al.
**摘要**: 利用重组HSF2蛋白的X射线晶体学分析，揭示了HSF2与DNA结合域的三维结构，阐明了其通过保守氨基酸残基与热休克元件(HSE)结合的分子机制，为靶向HSF2的药物设计提供依据。
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3. **文献名称**: *"Recombinant HSF2 Modulates Chromatin Remodeling in Mammalian Cells"*
**作者**: Östling, P., & Sistonen, L.
**摘要**: 通过哺乳动物细胞(HEK293)表达重组HSF2蛋白，结合ChIP-seq技术，发现HSF2通过招募组蛋白乙酰转移酶p300促进染色质开放，从而在胚胎发育和癌症中调控特定基因网络的激活。
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注：上述文献为示例性内容，实际引用时请以真实发表的论文为准。
**Background of HSF2 Recombinant Protein**
Heat Shock Factor 2 (HSF2) is a member of the heat shock factor (HSF) family, which regulates the expression of heat shock proteins (HSPs) in response to cellular stress, such as elevated temperatures, oxidative stress, or proteotoxic conditions. Unlike HSF1. the primary mediator of the heat shock response, HSF2 is less directly involved in acute stress signaling. Instead, it plays a nuanced role in development, differentiation, and homeostasis, particularly in the nervous system, reproductive organs, and during embryogenesis.
Structurally, HSF2 contains conserved DNA-binding domains, oligomerization regions, and regulatory motifs that enable it to bind heat shock elements (HSEs) in target gene promoters. Its activity is modulated by post-translational modifications, including phosphorylation and SUMOylation, which influence its stability, localization, and transcriptional competence. HSF2 often cooperates or competes with HSF1. creating a dynamic regulatory network for stress adaptation and cellular survival.
Recombinant HSF2 protein is produced using expression systems (e.g., *E. coli* or mammalian cells) to study its biochemical properties, DNA-binding kinetics, and interactions with co-regulators. Purification techniques, such as affinity chromatography, ensure high specificity and functionality. Researchers employ HSF2 recombinant protein in *in vitro* assays (e.g., electrophoretic mobility shift assays) and cell-based studies to dissect its role in gene regulation, stress responses, and disease contexts like cancer or neurodegeneration.
Recent studies highlight HSF2’s involvement in non-canonical pathways, including chromatin remodeling, cell cycle control, and apoptosis, expanding its significance beyond HSP regulation. Its recombinant form remains a critical tool for elucidating molecular mechanisms and developing therapeutic strategies targeting stress-related disorders.
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