| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GAL7 |
| Uniprot No | P47929 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-136aa |
| 氨基酸序列 | MASMTGGQQMGRGHHHHHHGNLYFQGGEFSNVPHKSSLPEGIRPGTVLRI RGLVPPNASRFHVNLLCGEEQGSDAALHFNPRLDTSEVVFNSKEQGSWGR EERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQYHHFRHRLPLARVRLV EVGGDVQLDSVRIF |
| 预测分子量 | 18 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GAL7重组蛋白的3篇示例文献(内容为模拟概括，仅供参考)：
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1. **文献名称**：*Cloning and Expression of the Saccharomyces cerevisiae GAL7 Gene in Escherichia coli*
**作者**：Smith, J. et al. (2005)
**摘要**：本研究报道了通过PCR扩增酵母GAL7基因，构建重组质粒并在大肠杆菌中高效表达可溶性重组GAL7蛋白。实验验证了该蛋白具有半乳糖-1-磷酸尿苷酰转移酶活性，为后续酶学分析奠定基础。
2. **文献名称**：*Purification and Kinetic Characterization of Recombinant GAL7 Enzyme from Pichia pastoris*
**作者**：Jones, R. et al. (2010)
**摘要**：作者利用毕赤酵母表达系统生产重组GAL7蛋白，通过亲和层析纯化获得高纯度酶，并测定其最适反应pH、温度及动力学参数(Km=0.8 mM，Vmax=120 U/mg)，揭示了其催化机制的特性。
3. **文献名称**：*Metabolic Engineering of GAL7-Expressing Yeast for Improved Galactose Utilization*
**作者**：Lee, H. et al. (2018)
**摘要**：通过过表达重组GAL7蛋白，优化酵母半乳糖代谢途径，显著提升菌株在半乳糖培养基中的生长速率和乙醇产率，为生物燃料生产提供新策略。
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*注：以上文献信息为示例性内容，实际引用需根据具体研究检索真实文献。*
The GAL7 recombinant protein is derived from the GAL7 gene, a key component of the galactose utilization pathway in yeast, particularly *Saccharomyces cerevisiae*. GAL7 encodes galactose-1-phosphate uridylyltransferase (GALT), an essential enzyme in the Leloir pathway responsible for galactose metabolism. This pathway converts galactose to glucose-6-phosphate, enabling yeast to utilize galactose as an energy source. In humans, GALT deficiency causes classic galactosemia (Type I), a rare genetic disorder leading to toxic accumulation of galactose metabolites, resulting in severe complications if untreated.
Recombinant GAL7 protein is produced through genetic engineering, often expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., yeast or mammalian cells) for research and therapeutic applications. Its production enables detailed studies of galactose metabolism mechanisms, enzyme kinetics, and substrate specificity. Researchers use recombinant GAL7 to investigate mutations linked to galactosemia, analyzing how specific genetic variants impair enzyme activity or stability. This has advanced understanding of disease pathogenesis and informed potential therapeutic strategies, such as enzyme replacement therapies or pharmacological chaperones.
Additionally, recombinant GAL7 serves as a tool for biotechnological applications, including metabolic engineering of microbes for industrial galactose processing or synthetic biology projects. Its high purity and controlled production allow for structural analyses (e.g., X-ray crystallography) to map active sites and optimize enzyme performance. Beyond basic research, recombinant GAL7 is explored in diagnostic assays to measure GALT activity in clinical samples, aiding galactosemia screening. Overall, this recombinant protein bridges fundamental biochemistry with translational medicine, offering insights into both cellular metabolism and genetic disease management.
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