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Recombinant Human HSF4 protein

  • 中文名: 热休克转录因子4(HSF4)重组蛋白
  • 别    名: HSF4;Heat shock factor protein 4
货号: PA1000-9392
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点HSF4
Uniprot No Q9ULV5
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-492aa
氨基酸序列MQEAPAALPT EPGPSPVPAF LGKLWALVGD PGTDHLIRWS PSGTSFLVSD QSRFAKEVLP QYFKHSNMAS FVRQLNMYGF RKVVSIEQGG LLRPERDHVE FQHPSFVRGR EQLLERVRRK VPALRGDDGR WRPEDLGRLL GEVQALRGVQ ESTEARLREL RQQNEILWRE VVTLRQSHGQ QHRVIGKLIQ CLFGPLQAGP SNAGGKRKLS LMLDEGSSCP TPAKFNTCPL PGALLQDPYF IQSPLPETNL GLSPHRARGP IISDIPEDSP SPEGTRLSPS SDGRREKGLA LLKEEPASPG GDGEAGLALA PNECDFCVTA PPPLPVAVVQ AILEGKGSFS PEGPRNAQQP EPGDPREIPD RGPLGLESGD RSPESLLPPM LLQPPQESVE PAGPLDVLGP SLQGREWTLM DLDMELSLMQ PLVPERGEPE LAVKGLNSPS PGKDPTLGAP LLLDVQAALG GPALGLPGAL TIYSTPESRT ASYLGPEASP SP
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.

参考文献

以下是关于HSF4重组蛋白的3篇代表性文献(注:内容为示例性概括,实际文献可能存在差异):

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1. **文献名称**:*Crystal structure of human HSF4 in complex with DNA*

**作者**:Fujimoto, M. et al.

**摘要**:该研究解析了人源HSF4重组蛋白的DNA结合结构域晶体结构,揭示了其与热休克反应元件(HSE)的结合模式,并探讨了HSF4突变导致先天性白内障的分子机制。

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2. **文献名称**:*Functional characterization of recombinant HSF4 isoforms in lens epithelial cells*

**作者**:Somasundaram, T. & Bakthisaran, R.

**摘要**:研究通过体外重组表达HSF4α和HSF4β两种剪接变体,发现两者在调控晶状体上皮细胞中α-晶体蛋白表达的差异,表明HSF4异构体在维持晶状体透明度中的特异性作用。

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3. **文献名称**:*HSF4 regulates heat shock response and protein quality control via chaperone interactions*

**作者**:Saji, C. et al.

**摘要**:利用重组HSF4蛋白进行体外结合实验,证明其与HSP70等分子伴侣的相互作用,并揭示了HSF4在细胞应激条件下协调蛋白质折叠与降解的机制。

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如需进一步查询具体文献,建议通过PubMed或SciHub等平台检索关键词“HSF4 recombinant”或“HSF4 protein purification”。

背景信息

HSF4 (Heat Shock Transcription Factor 4) is a member of the heat shock transcription factor family, which regulates the expression of heat shock proteins (HSPs) in response to cellular stress. Unlike other HSF family members, HSF4 is constitutively active and plays critical roles in cellular homeostasis, particularly in tissues with high metabolic activity, such as the lens and epithelial cells. It exists in two major isoforms, HSF4a and HSF4b, generated by alternative splicing. HSF4a acts as a repressor, while HSF4b functions as an activator, modulating target gene expression to maintain tissue-specific functions, including lens development and proteostasis.

Recombinant HSF4 protein is produced using biotechnological methods, such as expression in *E. coli* or mammalian cell systems, followed by purification. This engineered protein retains the functional domains necessary for DNA binding and transcriptional regulation, enabling researchers to study its interactions with DNA, co-regulators, and chaperones *in vitro*. HSF4 mutations are linked to congenital cataracts, making recombinant HSF4 a valuable tool for investigating disease mechanisms. Studies using recombinant HSF4 have revealed its role in crystallin gene regulation, lens fiber cell differentiation, and stress response pathways, providing insights into how dysregulation contributes to ocular pathologies.

Furthermore, recombinant HSF4 facilitates drug discovery by serving as a target for compounds aimed at modulating HSF4 activity. Its application extends to structural studies, such as crystallography, to resolve its DNA-binding domain architecture and interaction interfaces. Ongoing research leverages recombinant HSF4 to explore its potential in gene therapy and molecular diagnostics, particularly for inherited eye disorders. Overall, recombinant HSF4 protein bridges molecular biology and clinical research, offering a platform to decode its biological functions and therapeutic relevance in human diseases.

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