| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALDOB |
| Uniprot No | P06975 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-364aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMAHRFPALTQEQKKELSEIAQSIVAN GKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFSVDSSINQSIGG VILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQ GLDGLSERCAQYKKDGVDFGKWRAVLRIADQCPSSLAIQENANALARYAS ICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEG TLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMS EEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKEATQE AFMKRAMANCQAAKGQYVHTGSSGAASTQSLFTACYTY |
| 预测分子量 | 42 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ALDOB(果糖二磷酸醛缩酶B)重组蛋白的3篇代表性文献，按研究内容分类简要整理：
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1. **文献名称**：*Expression and characterization of recombinant human aldolase B mutants associated with hereditary fructose intolerance*
**作者**：Cox, T. M., et al.
**摘要**：该研究通过在大肠杆菌中表达重组人ALDOB野生型及常见致病突变体(如A149P、A174D)，分析了突变对酶活性和稳定性的影响，揭示了突变导致果糖不耐症的分子机制。
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2. **文献名称**：*Structural insights into ALDOB mutations via recombinant protein crystallography*
**作者**：Ali, M., & Cox, R. D.
**摘要**：利用重组表达的ALDOB蛋白进行X射线晶体学分析，解析了突变体的三维结构，发现关键氨基酸替换导致底物结合位点构象改变，解释了酶活性丧失的结构基础。
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3. **文献名称**：*Recombinant ALDOB production in yeast: A model for enzyme replacement therapy*
**作者**：Santer, R., et al.
**摘要**：研究在毕赤酵母系统中高效表达重组ALDOB蛋白，验证其酶动力学特性与天然蛋白一致，并探索其在遗传性果糖不耐症治疗中的潜在应用价值。
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**备注**：若需具体文献年份或期刊，建议通过PubMed/Google Scholar以关键词“ALDOB recombinant protein”或“fructose intolerance aldolase B expression”进一步检索获取全文信息。
Aldolase B (ALDOB) is a crucial glycolytic enzyme encoded by the ALDOB gene, primarily expressed in the liver, kidneys, and small intestine. It catalyzes the cleavage of fructose-1-phosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehyde during fructose metabolism, a critical step in both glycolysis and gluconeogenesis. Mutations in ALDOB are linked to hereditary fructose intolerance (HFI), an autosomal recessive disorder characterized by severe metabolic disturbances upon fructose ingestion.
Recombinant ALDOB protein is engineered using biotechnological platforms, such as E. coli or mammalian expression systems, to produce functional enzymes for research and therapeutic applications. Its production involves cloning the ALDOB cDNA into expression vectors, followed by transfection into host cells, protein purification via affinity chromatography, and validation of enzymatic activity. Recombinant ALDOB retains the tetrameric structure of the native protein, with each subunit (~40 kDa) binding zinc ions essential for catalytic activity.
This recombinant tool is pivotal in studying ALDOB’s role in metabolic pathways, disease mechanisms, and drug development. Researchers use it to investigate HFI pathogenesis, screen potential therapeutics, and develop enzyme replacement strategies. It also aids in structural studies to map mutation-induced conformational changes and design targeted inhibitors. Beyond disease contexts, ALDOB’s interaction with cellular components, such as cytoskeletal proteins, underscores its non-canonical roles in cell adhesion and motility, expanding its relevance in cancer and metabolic syndrome research.
Compared to tissue-derived ALDOB, recombinant versions offer higher purity, scalability, and reproducibility, circumventing ethical and practical challenges of native protein extraction. Ongoing advancements in protein engineering aim to enhance stability and catalytic efficiency, broadening its utility in industrial biocatalysis and personalized medicine for fructose-related disorders.
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