| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FUM |
| Uniprot No | P93033 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-492aa |
| 氨基酸序列 | MSIYVASRRLSGGTTVTALRYATSLRSYSTSFREERDTFGPIQVPSDKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGVLKKCAAKVNMEYGLDPTIGKAIMQAAQEVAEGKLNDHFPLVVWQTGSGTQSNMNANEVIANRAAEILGRKRGEKCVHPNDHVNRSQSSNDTFPTVMHIAAATEINSRLIPSLKTLHSTLESKSFEFKDIVKIGRTHTQDATPLTLGQEFGGYATQVKYGLNRVTCTLPRLYQLAQGGTAVGTGLNTKKGFDVKIAAAVAEETNLPFVTAENKFEALAAHDACVETSGSLNTIATSLMKIANDIRFLGSGPRCGLGELVLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAVTVGGSNGHFELNVFKPVIASALLHSVRLIADASASFEKNCVRGIEANRERISKLLHESLMLVTSLNPKIGYDNAAAVAKKAHKEGCTLKEAALNLGVLTAEEFDTLVVPEKMIGPSD |
| 预测分子量 | 53 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FUM(伏马菌素)重组蛋白的示例参考文献(内容为模拟，建议通过学术数据库核实具体文献)：
1. **《重组伏马菌素解毒酶的表达及活性分析》**
- 作者：Zhang Y, Liu X, Wang L
- 摘要：本研究克隆并表达了来源于鞘氨醇单胞菌的重组FumD蛋白，证实其可高效降解伏马菌素B1.为生物解毒提供潜在方案。
2. **《基于重组FUM抗原的伏马菌素免疫检测方法建立》**
- 作者：Li H, Chen J, Xu M
- 摘要：通过大肠杆菌表达重组伏马菌素半抗原-载体蛋白，制备高灵敏度单克隆抗体，成功开发伏马菌素ELISA检测试剂盒。
3. **《伏马菌素合成关键酶FUM1的重组表达与功能验证》**
- 作者：Proctor RH, Brown DW, Plattner RD
- 摘要：解析串珠镰刀菌中FUM1基因编码的聚酮合酶功能，重组蛋白证实其在伏马菌素生物合成中的核心作用。
**注**：若“FUM”指其他特定蛋白，建议补充全称或研究背景以精确检索。实际文献请通过PubMed、Web of Science等平台查询。
FUM recombinant proteins are a class of biologically engineered molecules derived from fungal or bacterial sources, primarily associated with the detoxification or metabolic processing of fumonisins. Fumonisins are toxic secondary metabolites produced by *Fusarium* species, notably *Fusarium verticillioides* and *Fusarium proliferatum*. These mycotoxins contaminate staple crops like maize, posing significant health risks to humans and livestock, including carcinogenic and immunosuppressive effects. Traditional methods to mitigate fumonisin contamination, such as physical removal or chemical treatments, are often inefficient or environmentally unsustainable. This has driven interest in biocatalytic solutions, including enzymatic degradation using FUM recombinant proteins.
The FUM gene cluster in *Fusarium* encodes enzymes responsible for fumonisin biosynthesis. Researchers have leveraged recombinant DNA technology to express key enzymes, such as Fumonisins Esterase (FUMD) or Fumonisin Aminotransferase (FUMI), in heterologous hosts like *E. coli* or yeast. These recombinant proteins exhibit catalytic activity to hydrolyze or modify fumonisins into less toxic derivatives, offering a promising strategy for food safety and agricultural applications. Additionally, recombinant FUM proteins are utilized in diagnostic assays to detect fumonisin levels in crops, enabling early intervention.
Beyond detoxification, FUM recombinant proteins contribute to understanding fungal secondary metabolism and toxin biosynthesis pathways. Their study aids in developing genetically modified crops resistant to *Fusarium* infection or engineering microbial consortia for bioremediation. Challenges remain in optimizing enzyme stability, scalability, and cost-effectiveness for industrial use. Nonetheless, FUM recombinant proteins represent a critical intersection of synthetic biology, environmental science, and public health, addressing global food security challenges posed by mycotoxin contamination.
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