| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FBA1 |
| Uniprot No | Q9URB4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-359aa |
| 氨基酸序列 | APPAVLSKSGVIYGKDVKDLFDYAQEKGFAIPAINVTSSSTVVAALEAARDNKAPIILQTSQGGAAYFAGKGVDNKDQAASIAGSIAAAHYIRAIAPTYGIPVVLHTDHCAKKLLPWFDGMLKADEEFFAKTGTPLFSSHMLDLSEETDDENIATCAKYFERMAKMGQWLEMEIGITGGEEDGVNNEHVEKDALYTSPETVFAVYESLHKISPNFSIAAAFGNVHGVYKPGNVQLRPEILGDHQVYAKKQIGTDAKHPLYLVFHGGSGSTQEEFNTAIKNGVVKVNLDTDCQYAYLTGIRDYVTNKIEYLKAPVGNPEGADKPNKKYFDPRVWVREGEKTMSKRIAEALDIFHTKGQL |
| 预测分子量 | 46.5 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FBA1重组蛋白的模拟参考文献示例(注：内容为虚构，仅用于演示格式)：
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1. **文献名称**：*Expression and Purification of Recombinant FBA1 from Saccharomyces cerevisiae in E. coli*
**作者**：Zhang L, et al.
**摘要**：本研究成功在大肠杆菌中高效表达并纯化了酿酒酵母来源的FBA1重组蛋白，优化了诱导条件以提高可溶性蛋白产量，为酶活性研究提供了材料基础。
2. **文献名称**：*Structural Characterization of FBA1 in Glycolytic Pathway by X-ray Crystallography*
**作者**：Smith J, Patel R.
**摘要**：通过X射线晶体学解析了FBA1的三维结构，揭示了其底物结合位点的关键氨基酸残基，为设计针对病原体FBA1的抑制剂提供了结构依据。
3. **文献名称**：*Functional Analysis of FBA1 in Candida albicans Pathogenicity*
**作者**：Chen H, et al.
**摘要**：探讨了白色念珠菌中FBA1的敲除对糖代谢及宿主感染能力的影响，表明FBA1是其致病性的潜在治疗靶点。
4. **文献名称**：*FBA1 as a Novel Vaccine Candidate Against Bacterial Infections*
**作者**：Wang Y, et al.
**摘要**：评估了重组FBA1蛋白在小鼠模型中的免疫原性，结果显示其可诱导保护性抗体，提示其在抗细菌疫苗开发中的应用潜力。
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以上示例展示了不同研究方向(表达纯化、结构解析、功能研究、应用开发)，用户可根据实际需求调整关键词或物种特异性。如需真实文献，建议通过PubMed、Google Scholar等平台检索。
Fructose-1.6-bisphosphate aldolase (FBA1) is a critical enzyme in glycolysis and gluconeogenesis, catalyzing the reversible cleavage of fructose-1.6-bisphosphate (FBP) into glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). This class I aldolase is highly conserved across eukaryotes and prokaryotes, playing a central role in cellular energy metabolism. In *Saccharomyces cerevisiae*, FBA1 is essential for growth on glucose, making it a model system for studying aldolase function and metabolic regulation. Beyond its metabolic role, FBA1 exhibits "moonlighting" functions, including interactions with cytoskeletal components and involvement in stress responses.
Recombinant FBA1 production typically employs heterologous expression systems like *E. coli* or yeast, enabling large-scale purification for structural and functional studies. Its robust enzymatic activity and stability make it valuable for biotechnological applications, particularly in multi-enzyme systems for synthetic biology. In pathogenic fungi such as *Candida albicans* and *Cryptococcus neoformans*, FBA1 localizes to the cell surface and acts as a virulence factor, stimulating host immune responses and facilitating adhesion to host tissues. This dual intracellular/extracellular functionality has sparked interest in FBA1 as a potential therapeutic target for antifungal drugs and vaccine development.
Structural studies reveal a TIM barrel fold characteristic of aldolases, with conserved catalytic residues (e.g., Schiff-forming lysine) critical for substrate binding. Recent research explores engineered FBA1 variants for improved catalytic efficiency or altered substrate specificity. In industrial contexts, FBA1 is utilized in biofuel production through metabolic pathway engineering and in biosensors for monitoring glycolytic flux. Its evolutionary conservation and multifunctional nature continue to make FBA1 a focal point for understanding metabolic adaptation, host-pathogen interactions, and bioprocess optimization.
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