Recombinant Human hmfB protein

中文名： DNA结合蛋白HMf-2(hmfB)重组蛋白
别名： hmfB；DNA-binding protein HMf-2

货号: PA2000-4106

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	Human
靶点	hmfB
Uniprot No	P19267
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-69aa
氨基酸序列	MELPIAPIGRIIKDAGAERVSDDARITLAKILEEMGRDIASEAIKLARHAGRKTIKAEDIELAVRRFKK
预测分子量	9.7 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HmfB重组蛋白的示例性参考文献，基于相关领域研究的常见主题和结构整理而成：

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1. **文献名称**: *"Cloning and Expression of Recombinant HmfB from Methanothermobacter thermautotrophicus: A Thermostable DNA-Binding Protein"*

**作者**: Smith, J. et al.

**摘要**: 本研究在大肠杆菌中成功克隆并表达了古菌Methanothermobacter thermautotrophicus的HmfB蛋白。纯化后的重组HmfB在体外表现出强DNA结合能力，并通过热稳定性实验证实其可增强DNA在高温下的保护作用，为古菌染色质耐热机制提供依据。

2. **文献名称**: *"Crystal Structure of Archaeal Histone Homolog HmfB Reveals Dimeric Assembly and DNA Interaction Motifs"*

**作者**: Tanaka, K. et al.

**摘要**: 通过X射线晶体学解析HmfB的三维结构，发现其以二聚体形式存在，并具有独特的螺旋-转角-螺旋基序。与真核组蛋白相比，HmfB通过电荷互补机制与DNA结合，提示其在古菌基因组压缩中的关键作用。

3. **文献名称**: *"Functional Characterization of Recombinant HmfB in DNA Condensation Under Extreme Conditions"*

**作者**: Lee, S. & Chen, W.

**摘要**: 利用重组HmfB进行体外DNA凝缩实验，发现其在高温和高盐环境下显著促进DNA超螺旋形成。通过原子力显微镜观察，揭示了HmfB通过多价相互作用调控染色质动态组装的过程。

4. **文献名称**: *"Comparative Study of HmfA and HmfB in Methanogenic Archaea: Implications for Chromatin Organization"*

**作者**: Zhang, Y. et al.

**摘要**: 对比分析HmfA和HmfB的重组蛋白功能，发现HmfB对A-T富集区DNA亲和力更高，且更倾向于形成高阶寡聚体。研究推测HmfB在古菌染色体分区中可能发挥特异性调控作用。

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**注**：以上文献为示例性内容，实际研究中请通过学术数据库(如PubMed、Web of Science)检索具体文献。若需进一步协助定位真实文献，建议提供更详细的背景信息或研究关键词。

背景信息

The hmfB gene encodes a histone-like protein originally identified in methanogenic archaea, such as *Methanothermus fervidus*. These organisms thrive in extreme environments, and their chromatin organization relies on small DNA-binding proteins like HmfB, which share functional similarities with eukaryotic histones. HmfB plays a critical role in compacting and stabilizing genomic DNA, regulating transcription, and protecting genetic material under high-temperature or other stress conditions. Its structure typically includes conserved domains for DNA interaction, enabling it to bend or wrap DNA into nucleosome-like architectures.

Recombinant HmfB protein is produced via heterologous expression systems, such as *E. coli*, to study its biochemical and biophysical properties. This approach allows large-scale purification for structural analyses (e.g., X-ray crystallography, NMR) and functional assays. Researchers are particularly interested in HmfB’s thermostability and DNA-binding mechanisms, which provide insights into archaeal chromatin dynamics and evolutionary links to eukaryotic histone-based systems.

Beyond basic science, recombinant HmfB has biotechnological potential. Its stability and DNA-packaging capabilities could inspire synthetic biology tools for gene delivery or nanostructure assembly. Additionally, studying HmfB may advance extremophile-derived enzyme engineering for industrial processes requiring high-temperature resilience. Despite progress, questions remain about its precise regulatory roles and adaptability across diverse archaeal species, driving ongoing research in this field.