| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | frmA |
| Uniprot No | Q1RFI7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-369aa |
| 氨基酸序列 | MKSRAAVAFAPGKPLEIVEIDVAPPKKGEVLIKVTHTGVCHTDAFTLSGDDPEGVFPVVLGHEGAGVVVEVGEGVTSVKPGDHVIPLYTAECGECEFCRSGKTNLCVAVRETQGKGLMPDGTTRFSYNGQPLYHYMGCSTFSEYTVVAEVSLAKINPEANHEHVCLLGCGVTTGIGAVHNTAKVQPGDSVAVFGLGAIGLAVVQGARQAKAGRIIAIDTNPKKFELARRFGATDCINPNDYDKPIKDVLLDINKWGIDHTFECIGNVNVMRAALESAHRGWGQSVIIGVAGSGQEISTRPFQLVTGRVWKGSAFGGVKGRSQLPGMVEDAMKGDIDLEPFVTHTMSLDEINDAFDLMHEGKSIRTVIRY |
| 预测分子量 | 46.8 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. |
以下为模拟生成的3篇关于frmA重组蛋白的参考文献示例(实际文献请通过学术数据库验证)：
1. **文献名称**: *"Cloning and Functional Characterization of the frmA Gene in Staphylococcus aureus"*
**作者**: Lee, H., et al.
**摘要**: 本研究成功克隆并表达了frmA重组蛋白，揭示其通过催化甲硝唑代谢产物降解介导抗生素耐药性，为理解葡萄球菌耐药机制提供了新依据。
2. **文献名称**: *"Structural Analysis of Recombinant FrmA Protein in Bacterial Detoxification"*
**作者**: Zhang, Y., & Patel, R.
**摘要**: 通过X射线晶体学解析frmA重组蛋白三维结构，发现其活性位点对硝基还原反应的关键作用，提出该酶在细菌解毒通路中的分子调控模型。
3. **文献名称**: *"Heterologous Expression of frmA in E. coli and Its Application in Bioremediation"*
**作者**: Gomez, S., et al.
**摘要**: 报道了frmA基因在大肠杆菌中的高效表达策略，验证重组蛋白对环境污染物的降解能力，证明其在工业生物修复中的潜在应用价值。
提示：建议通过PubMed/Google Scholar搜索关键词 "frmA recombinant protein" "nitroreductase" 获取真实文献，重点关注近年微生物耐药性及酶催化机制相关研究。
**Background of FrmA Recombinant Protein**
FrmA is a bacterial enzyme encoded by the *frmA* gene, primarily associated with formaldehyde detoxification in microorganisms. Formaldehyde, a toxic electrophile, accumulates as a byproduct of single-carbon metabolism or environmental exposure. To mitigate its cytotoxicity, bacteria employ conserved metabolic pathways, with FrmA playing a key role in the *SgrST-FrmRA* stress response system. This system is activated under formaldehyde stress, regulating genes involved in formaldehyde oxidation and protection.
FrmA functions as a formaldehyde dehydrogenase, catalyzing the NAD(P)+-dependent oxidation of formaldehyde to formate. This reaction is critical for maintaining cellular redox balance and preventing protein/DNA damage. The enzyme is structurally classified within the aldehyde dehydrogenase superfamily, featuring conserved catalytic residues and substrate-binding domains. Studies on FrmA homologs, such as those in *E. coli* and *Pseudomonas*, have provided insights into its mechanism and regulation.
Recombinant FrmA protein is produced via heterologous expression in systems like *E. coli*, enabling high-yield purification for biochemical studies. Cloning the *frmA* gene into expression vectors with affinity tags (e.g., His-tag) facilitates efficient isolation. Recombinant FrmA retains enzymatic activity, allowing researchers to characterize its kinetics, substrate specificity, and inhibition profiles.
Research on FrmA has applications in bioremediation, industrial biocatalysis (e.g., formaldehyde removal), and understanding bacterial stress adaptation. Additionally, its role in formaldehyde metabolism intersects with studies on cancer biology, as formaldehyde is linked to genomic instability. Engineering FrmA variants or optimizing its activity could advance bio-based solutions for environmental and health challenges.
In summary, FrmA recombinant protein serves as a vital tool for dissecting formaldehyde metabolism, bacterial stress responses, and enzyme-driven detoxification mechanisms.
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