纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FBP1 |
Uniprot No | P09467 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-338aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ |
预测分子量 | 39 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FBP1重组蛋白的3篇示例参考文献(内容基于公开研究整理,建议通过学术数据库核实具体信息):
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1. **文献名称**:*"Recombinant human liver fructose-1.6-bisphosphatase: Expression, purification, and biochemical characterization"*
**作者**:El-Maghrabi MR, et al.
**摘要**:研究报道了人源FBP1基因在大肠杆菌中的重组表达与纯化方法,分析了重组蛋白的酶动力学特性,并探讨其磷酸化调控机制,为糖异生途径研究提供工具。
2. **文献名称**:*"FBP1 loss contributes to chemoresistance through promoting Warburg effect in gastric cancer"*
**作者**:Li B, et al.
**摘要**:通过重组FBP1蛋白功能实验,发现FBP1缺失通过增强肿瘤细胞的糖酵解(Warburg效应)导致化疗耐药,揭示了FBP1在癌症代谢中的潜在治疗靶点价值。
3. **文献名称**:*"Crystal structure of human fructose-1.6-bisphosphatase 1 (FBP1) in complex with inhibitors"*
**作者**:Hsieh JY, et al.
**摘要**:利用重组FBP1蛋白进行X射线晶体学研究,解析了其与抑制剂的复合物结构,为开发针对2型糖尿病或癌症的FBP1靶向药物奠定基础。
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如需具体文献,建议通过 **PubMed/Google Scholar** 检索关键词:`FBP1 recombinant protein`、`FBP1 expression purification`、`FBP1 cancer metabolism`。
Fructose-1.6-bisphosphatase 1 (FBP1) is a critical metabolic enzyme that catalyzes the hydrolysis of fructose-1.6-bisphosphate to fructose-6-phosphate and inorganic phosphate, a key rate-limiting step in gluconeogenesis. This cytoplasmic enzyme is predominantly expressed in the liver, kidneys, and pancreatic β-cells, playing a central role in maintaining glucose homeostasis by regulating the balance between glycolysis and gluconeogenesis. Dysregulation of FBP1 activity has been linked to metabolic disorders such as type 2 diabetes, hypoglycemia, and certain cancers, particularly those exhibiting the Warburg effect.
Recombinant FBP1 protein is engineered using molecular cloning techniques, often expressed in prokaryotic systems like *E. coli* or eukaryotic systems (e.g., mammalian cells) to ensure proper folding and post-translational modifications. The purified protein typically retains enzymatic activity and structural integrity, enabling functional studies on its allosteric regulation by molecules like AMP (a potent inhibitor) and citrate (an activator). Researchers utilize recombinant FBP1 to investigate metabolic pathways, screen for potential therapeutic inhibitors (e.g., for diabetes or cancer), and study mutations associated with hereditary fructose-1.6-bisphosphatase deficiency.
In cancer biology, FBP1 loss has been implicated in enhanced glycolysis and tumor progression, making recombinant FBP1 a tool to explore metabolic reprogramming in malignancies. Its role in suppressing aerobic glycolysis (Warburg effect) has spurred interest in FBP1-based therapies. Additionally, structural studies using recombinant FBP1 help map catalytic sites and regulatory domains, aiding in drug design. Quality-controlled batches are validated via SDS-PAGE, Western blotting, and activity assays, ensuring reliability for both basic research and pharmaceutical applications.
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