| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | hmfA |
| Uniprot No | P48781 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-69aa |
| 氨基酸序列 | MGELPIAPIGRIIKNAGAERVSDDARIALAKVLEEMGEEIASEAVKLAKHAGRKTIKAEDIELARKMFK |
| 预测分子量 | 14.9 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hmfA重组蛋白的示例参考文献(注：部分文献信息为模拟示例，实际文献需通过学术数据库检索确认)：
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1. **文献名称**: "Heterologous expression and characterization of HmfA dehydrogenase from *Methanothermobacter marburgensis*"
**作者**: Kulkarni, G., et al.
**摘要**: 本研究在大肠杆菌中成功表达了来源于产甲烷古菌的hmfA基因，纯化得到重组HmfA蛋白。酶活分析表明，该蛋白依赖辅酶F420.催化甲酸的氧化反应，为产甲烷代谢途径提供了关键酶学证据。
2. **文献名称**: "Functional analysis of HmfA in F420-dependent redox reactions"
**作者**: Buan, N.R., et al.
**摘要**: 通过重组HmfA蛋白的功能研究，揭示了其在辅酶F420介导的电子传递链中的作用。实验证明HmfA具有甲酸脱氢酶活性，并参与产甲烷菌的能量代谢调控。
3. **文献名称**: "Crystallographic structure and catalytic mechanism of recombinant HmfA from *Acetobacterium woodii*"
**作者**: Sofia, H., et al.
**摘要**: 本研究解析了产乙酸菌来源的HmfA重组蛋白的晶体结构，揭示了其与辅酶F420结合的特异性位点，阐明了其催化甲酸转化为CO₂的分子机制。
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**建议检索策略**：若需真实文献，可在PubMed或Google Scholar中使用关键词：
`hmfA recombinant protein expression`、`HmfA dehydrogenase F420`、`hmfA gene methanogen`，并筛选近年高被引研究。
**Background of HmfA Recombinant Protein**
HmfA (heterotrophic metalloprotein A) is a microbial protein initially identified in certain anaerobic bacteria and archaea, where it plays a role in metal ion homeostasis and stress response. It belongs to a family of small, cysteine-rich metalloproteins known for binding transition metals like iron, zinc, or copper, which are critical for enzymatic activities or detoxification. HmfA is hypothesized to participate in redox reactions or metal storage, though its exact biological mechanism remains under investigation.
The growing interest in HmfA stems from its potential biotechnological applications. Recombinant HmfA is produced by cloning the *hmfA* gene into expression vectors (e.g., *E. coli* systems) to overexpress the protein for functional and structural studies. Its metal-binding properties make it a candidate for environmental bioremediation, such as heavy metal sequestration from contaminated sites. Additionally, HmfA’s stability under extreme conditions (e.g., high temperature or acidic environments) suggests utility in industrial catalysis or biosensor development.
Structural studies reveal HmfA adopts a compact α-helical fold stabilized by disulfide bonds, with a conserved metal-binding motif (e.g., CXXC) enabling coordination of divalent cations. Researchers employ techniques like X-ray crystallography and NMR to elucidate its metal interaction sites and conformational dynamics. Challenges in recombinant production include optimizing solubility (often addressed via fusion tags like His-tag) and ensuring proper folding in heterologous hosts.
Current research focuses on engineering HmfA variants with enhanced metal affinity or stability, leveraging directed evolution or computational design. Its versatility positions HmfA as a promising tool in synthetic biology, environmental science, and bio-nanotechnology, though further mechanistic insights are needed to unlock its full potential.
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