| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FH |
| Uniprot No | P07954 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-510aa |
| 氨基酸序列 | MYRALRLLARSRPLVRAPAAALASAPGLGGAAVPSFWPPNAARMASQNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYGLDPKIANAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK |
| 预测分子量 | 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FH(延胡索酸酶，Fumarate Hydratase)重组蛋白的模拟参考文献示例，供参考。实际文献请通过学术数据库(如PubMed、Google Scholar)检索获取：
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1. **文献名称**：*Recombinant Human Fumarate Hydratase: Production, Purification, and Functional Characterization*
**作者**：Smith A, et al.
**摘要**：本研究报道了人源FH蛋白在大肠杆菌中的重组表达与纯化，通过酶活性实验证实了重组蛋白的催化功能，并分析了其热稳定性，为FH缺陷相关疾病的研究提供了工具。
2. **文献名称**：*Structural Insights into FH Mutations Linked to Hereditary Leiomyomatosis*
**作者**：Brown C, et al.
**摘要**：利用重组FH蛋白的晶体结构分析，揭示了与遗传性平滑肌瘤病相关的突变位点如何破坏酶活性，阐明了FH功能丧失导致代谢异常和肿瘤发生的分子机制。
3. **文献名称**：*Metabolic Rescue via Recombinant FH in Renal Cell Carcinoma Models*
**作者**：Zhang Y, et al.
**摘要**：在FH缺陷的肾癌细胞中导入重组FH蛋白，恢复了三羧酸循环功能并抑制了缺氧信号通路，提示补充FH可能成为特定癌症亚型的潜在治疗策略。
4. **文献名称**：*Development of a High-Yield FH Expression System in Insect Cells*
**作者**：Lee J, et al.
**摘要**：通过杆状病毒-昆虫细胞系统高效表达重组FH蛋白，优化后的工艺显著提高了蛋白产量和溶解度，支持了大规模药物筛选和结构生物学研究。
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**建议**：如需具体文献，可检索关键词“recombinant fumarate hydratase”或“FH protein expression”，并筛选与您研究方向相关的论文。注意FH也可能指补体因子H(Factor H)，需结合上下文确认缩写含义。
**Background of FH Recombinant Protein**
The FH (fumarate hydratase) protein is a critical enzyme in the tricarboxylic acid (TCA) cycle, catalyzing the reversible hydration of fumarate to L-malate. This mitochondrial enzyme plays a central role in cellular energy production and metabolic homeostasis. Mutations in the *FH* gene are linked to hereditary leiomyomatosis and renal cell cancer (HLRCC), a genetic disorder characterized by benign skin tumors, uterine fibroids, and aggressive kidney cancer. The loss of FH function leads to fumarate accumulation, disrupting cellular metabolism and promoting tumorigenesis via hypoxia-inducible factor (HIF) stabilization and oxidative stress.
Recombinant FH protein is produced using genetic engineering techniques, often expressed in *E. coli* or mammalian cell systems to ensure proper folding and enzymatic activity. Its production enables detailed biochemical studies, including structural analysis, substrate specificity, and inhibitor screening. Recombinant FH is pivotal in researching HLRCC mechanisms, as it allows scientists to examine the effects of specific mutations on enzyme function and stability. Additionally, it serves as a tool for developing diagnostic assays and targeted therapies, such as small-molecule inhibitors to counteract metabolic dysregulation in FH-deficient cancers.
The use of recombinant FH also addresses challenges in studying the native protein, such as low abundance in tissues and difficulties in purification. By providing a scalable and pure protein source, recombinant technology accelerates both basic research and translational applications, bridging gaps between metabolic dysfunction understanding and clinical intervention strategies. Overall, FH recombinant protein is indispensable for unraveling the molecular basis of FH-related diseases and advancing therapeutic innovations.
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