| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | folD |
| Uniprot No | P24186 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-288aa |
| 氨基酸序列 | MAAKIIDGKTIAQQVRSEVAQKVQARIAAGLRAPGLAVVLVGSNPASQIYVASKRKACEEVGFVSRSYDLPETTSEAELLELIDTLNADNTIDGILVQLPLPAGIDNVKVLERIHPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDTFGLNAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLIVAVGKPGFIPGDWIKEGAIVIDVGINRLENGKVVGDVVFEDAAKRASYITPVPGGVGPMTVATLIENTLQACVEYHDPQDE |
| 预测分子量 | 31,0 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folD重组蛋白的3篇参考文献示例，涵盖功能、结构与应用研究：
1. **标题**：*Cloning, expression, and characterization of recombinant folD protein from Escherichia coli*
**作者**：Smith A, et al.
**摘要**：研究报道了大肠杆菌folD基因的克隆与重组蛋白表达，通过体外酶活实验验证其双功能酶(脱氢酶/环水解酶)活性，为叶酸代谢机制提供基础数据。
2. **标题**：*Structural insights into the bifunctional enzyme FolD through X-ray crystallography*
**作者**：Lee JH, et al.
**摘要**：利用X射线晶体学解析重组folD蛋白的三维结构，揭示其底物结合口袋及催化关键残基，阐明其双功能催化机制。
3. **标题**：*Targeting FolD in antimicrobial drug discovery: High-throughput screening using recombinant enzyme*
**作者**：Garcia-Sánchez M, et al.
**摘要**：建立基于重组folD蛋白的高通量抑制剂筛选平台，发现新型抗菌先导化合物，验证folD作为抗感染药物靶点的潜力。
(注：以上文献信息为示例，实际引用时请核实具体文章。)
**Background of FolD Recombinant Protein**
The *folD* gene encodes a bifunctional enzyme, FolD, which plays a critical role in one-carbon metabolism across bacteria and eukaryotes. This enzyme catalyzes two sequential reactions in the folate cycle: the dehydrogenation of 5.10-methylenetetrahydrofolate to 5.10-methenyltetrahydrofolate and the hydrolysis of the latter to form 10-formyltetrahydrofolate. These steps are essential for purine and thymidine biosynthesis, as well as methionine regeneration, making FolD vital for DNA/RNA synthesis, cell proliferation, and methylation processes.
In pathogenic bacteria, FolD is a validated antimicrobial target due to its indispensability in folate metabolism. Its absence disrupts nucleotide synthesis, impairing bacterial growth. Consequently, FolD inhibitors are being explored as potential antibiotics, particularly against drug-resistant strains.
Recombinant FolD protein is typically produced via heterologous expression in *E. coli* or yeast systems, enabling large-scale purification for structural and functional studies. Structural analyses (e.g., X-ray crystallography, cryo-EM) have elucidated its catalytic mechanisms and interaction with inhibitors. Additionally, recombinant FolD is used in enzymatic assays to screen for inhibitors or study mutations affecting activity.
In eukaryotes, FolD homologs (e.g., human MTHFD1) share similar functions but differ in structural features, necessitating species-specific studies. Dysregulation of FolD-related pathways is linked to diseases like cancer, highlighting its therapeutic relevance.
Overall, FolD recombinant protein serves as a key tool for understanding one-carbon metabolism, advancing antimicrobial drug development, and exploring metabolic diseases. Its dual enzymatic activity and conservation across species underscore its biological and biomedical significance.
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