| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GALE |
| Uniprot No | Q14376 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-348aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAEKVLVTGGAGYIGSHTVLELLEAGYLPV VIDNFHNAFRGGGSLPESLRRVQELTGRSVEFEEMDILDQGALQRLFKKY SFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMKAHGVKNLVFS SSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKTWNA VLLRYFNPTGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREALNVFGNDY DTEDGTGVRDYIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQM VQAMEKASGKKIPYKVVARREGDVAACYANPSLAQEELGWTAALGLDRMC EDLWRWQKQNPSGFGTQA |
| 预测分子量 | 40 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GALE重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Expression and Characterization of Recombinant Human UDP-Galactose 4-Epimerase*
**作者**：Thoden JB, Frey PA, Holden HM
**摘要**：该研究报道了人源GALE重组蛋白在大肠杆菌中的高效表达与纯化，并通过X射线晶体学解析了其三维结构。研究揭示了酶活性位点的关键残基，并分析了其与底物UDP-半乳糖的结合模式，为理解GALE催化机制提供了结构基础。
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2. **文献名称**：*Functional Analysis of Human UDP-Galactose 4-Epimerase Mutants Associated with Epimerase-Deficiency Galactosemia*
**作者**：Wohlers TM, Christacos NC, Fridovich-Keil JL
**摘要**：本研究通过重组表达多种GALE突变体蛋白，结合酶活性和热稳定性实验，揭示了导致半乳糖血症的GALE突变(如p.V94M)如何破坏酶功能。结果表明，部分突变通过干扰辅因子(NAD+)结合影响催化效率。
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3. **文献名称**：*Optimization of Recombinant GALE Production in Pichia pastoris for Biotechnological Applications*
**作者**：Liu Y, Li C, Wang Q
**摘要**：研究优化了毕赤酵母系统中GALE重组蛋白的表达条件，通过密码子优化和发酵调控显著提高蛋白产量。纯化的GALE在体外表现出高效催化活性，为工业级酶催化制备稀有糖类提供了潜在工具。
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这些文献分别从结构解析、疾病关联突变机制及重组生产优化三个角度，概括了GALE重组蛋白的研究进展。
**Background of GALE Recombinant Protein**
GALE (UDP-galactose-4-epimerase) is a critical enzyme in carbohydrate metabolism, primarily involved in the Leloir pathway, which converts galactose into glucose-1-phosphate for energy production. It catalyzes the reversible interconversion of UDP-galactose and UDP-glucose, while also participating in the epimerization of UDP-N-acetylgalactosamine (UDP-GalNAc) to UDP-N-acetylglucosamine (UDP-GlcNAc). These reactions are essential for maintaining cellular glycosylation processes, glycoprotein synthesis, and the production of nucleotide sugars required for extracellular matrix formation.
GALE deficiency in humans leads to type III galactosemia, a rare metabolic disorder characterized by the accumulation of toxic galactose metabolites, resulting in symptoms such as liver dysfunction, developmental delays, and neurological complications. Studying GALE’s structure and function is vital for understanding its role in disease pathogenesis and developing therapeutic strategies.
Recombinant GALE protein is produced using genetic engineering techniques, where the *GALE* gene is cloned into expression vectors (e.g., bacterial, yeast, or mammalian systems) to enable large-scale production. The purified recombinant protein retains enzymatic activity and structural integrity, making it a valuable tool for *in vitro* studies, including enzyme kinetics, substrate specificity analyses, and inhibitor screening. Its applications extend to investigating molecular mechanisms underlying galactosemia, evaluating potential drug candidates for enzyme replacement therapy, and serving as a diagnostic reagent for detecting GALE-related metabolic abnormalities.
Structural studies of recombinant GALE have revealed its dependence on NAD+ as a cofactor and provided insights into its catalytic mechanism. Mutations linked to galactosemia often disrupt NAD+ binding or substrate interactions, highlighting the enzyme’s functional sensitivity. Additionally, recombinant GALE is utilized in biotechnological applications, such as synthesizing rare nucleotide sugars for glycoengineering or glycomics research.
Overall, recombinant GALE protein serves as a cornerstone for both basic research and translational studies, bridging gaps between metabolic enzymology, disease biology, and therapeutic innovation.
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