| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GAL |
| Uniprot No | P22466 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 44-123aa |
| 氨基酸序列 | GPHAVGNHRSFSDKNGLTSKRELRPEDDMKPGSFDRSIPENNIMRTIIEFLSFLHLKEAGALDRLLDLPAAASSEDIERS |
| 预测分子量 | 16.4 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GAL重组蛋白的3篇示例参考文献(内容为虚构示例，仅用于格式参考)：
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1. **文献名称**：*Expression and Purification of Recombinant GAL4 Protein in Escherichia coli*
**作者**：Smith J, et al.
**摘要**：研究利用大肠杆菌表达系统高效表达GAL4重组蛋白，通过His标签纯化获得高纯度产物，并验证其DNA结合活性，为转录调控研究提供工具。
2. **文献名称**：*Structural Analysis of GAL1 Recombinant Protein in Yeast Signaling Pathways*
**作者**：Lee H, et al.
**摘要**：解析GAL1重组蛋白的晶体结构，揭示其与半乳糖代谢相关的功能域，为酵母糖响应机制的分子基础提供新见解。
3. **文献名称**：*Application of GAL-UAS System in Mammalian Cell Gene Regulation*
**作者**：Brown K, et al.
**摘要**：将酵母GAL4-UAS调控系统改造用于哺乳动物细胞，证明重组GAL蛋白可诱导靶基因表达，为可控基因治疗技术奠定基础。
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注：以上文献为示例，实际文献需通过PubMed、Web of Science等数据库检索。如需具体论文，建议结合关键词“GAL recombinant protein”“GAL4 expression”等进一步查询。
**Background of GAL Recombinant Proteins**
Recombinant GAL proteins, derived from the *GAL* gene family, are engineered through genetic recombination technology to study or utilize their biological functions. The *GAL* genes, first characterized in yeast (*Saccharomyces cerevisiae*), encode proteins critical for galactose metabolism, such as galactokinase (GAL1), galactose permease (GAL2), and transcriptional activators (GAL4). These proteins gained prominence due to their role in regulating the *GAL* gene cluster, a model system for understanding eukaryotic gene regulation.
The development of recombinant DNA technology in the 1970s enabled the cloning and heterologous expression of GAL proteins in bacterial or eukaryotic systems. GAL4. for instance, became a pivotal tool in molecular biology. Its DNA-binding domain and transcriptional activation domain were repurposed to create the GAL4-UAS (Upstream Activating Sequence) system, widely used to control gene expression in organisms like *Drosophila* and plants.
Recombinant GAL proteins are produced by inserting the target gene into expression vectors, followed by transfection into host cells (e.g., *E. coli*, insect, or mammalian cells). Purification methods, such as affinity chromatography, ensure high yield and specificity. These proteins retain functional domains, allowing researchers to manipulate cellular processes, study protein interactions, or engineer metabolic pathways.
Applications span basic research and biotechnology. For example, GAL-based systems are used to study gene regulatory networks, while engineered GAL variants aid in synthetic biology or therapeutic development, such as enzyme replacement therapies for metabolic disorders. Challenges include optimizing expression conditions and minimizing post-translational modifications in non-native hosts.
Overall, GAL recombinant proteins exemplify the synergy between foundational genetics and modern biotechnology, offering versatile tools to dissect biological mechanisms and innovate solutions in biomedicine and industry.
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