| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GALM |
| Uniprot No | Q96C23 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-342aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMASVTRAVFGELPSGGGTVEKFQLQSDLLR VDIISWGCTITALEVKDRQGRASDVVLGFAELEGYLQKQPYFGAVIGRVA NRIAKGTFKVDGKEYHLAINKEPNSLHGGVRGFDKVLWTPRVLSNGVQFS RISPDGEEGYPGELKVWVTYTLDGGELIVNYRAQASQATPVNLTNHSYFN LAGQASPNINDHEVTIEADTYLPVDETLIPTGEVAPVQGTAFDLRKPVEL GKHLQDFHLNGFDHNFCLKGSKEKHFCARVHHAASGRVLEVYTTQPGVQF YTGNFLDGTLKGKNGAVYPKHSGFCLETQNWPDAVNQPRFPPVLLRPGEE YDHTTWFKFSVA |
| 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GALM重组蛋白的3篇示例文献(注：示例基于公开研究主题构造，非真实文献)：
1. **文献名称**：*Expression and Purification of Recombinant Human GALM in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：本研究报道了人源GALM(半乳糖变旋酶)在大肠杆菌中的高效重组表达及纯化方法，通过优化表达条件获得可溶性蛋白，并验证其酶活性，为后续结构功能研究奠定基础。
2. **文献名称**：*Structural Insights into the Catalytic Mechanism of GALM through X-ray Crystallography*
**作者**：Chen L, et al.
**摘要**：通过X射线晶体学解析了重组GALM蛋白的三维结构，揭示了其催化半乳糖变旋的关键氨基酸残基及作用机制，为靶向GALM的抑制剂设计提供理论依据。
3. **文献名称**：*Role of Recombinant GALM in Galactose Metabolism Disorders*
**作者**：Yamamoto K, et al.
**摘要**：探讨了重组GALM蛋白在半乳糖代谢异常疾病模型中的作用，证明其外源性补充可改善代谢缺陷，提示潜在治疗应用价值。
如需具体文献，建议通过PubMed或SciHub检索关键词 "recombinant GALM protein" 或 "GALM enzyme expression"。
GALM (Galactose Mutarotase) is an enzyme critical in carbohydrate metabolism, specifically involved in the interconversion of α- and β-anomers of galactose. This catalytic process is essential for enabling galactose to enter metabolic pathways, such as the Leloir pathway, where it is converted into glucose-1-phosphate for energy production. Dysregulation of GALM activity has been linked to metabolic disorders, including galactosemia, a rare genetic condition characterized by the inability to metabolize galactose properly. Research on GALM spans structural biology, enzymology, and therapeutic development, driven by its role in maintaining galactose homeostasis.
Recombinant GALM protein is produced using genetic engineering techniques, typically through expression in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., yeast or mammalian cells). The gene encoding GALM is cloned into expression vectors, allowing large-scale production of the purified enzyme. This approach ensures high purity and consistent activity, overcoming limitations of extracting the protein from native tissues. Structural studies using recombinant GALM have revealed its active site architecture and mechanism of anomerization, providing insights into substrate specificity and catalytic efficiency.
Applications of recombinant GALM extend to biomedical research, including enzyme replacement therapy for galactosemia, diagnostic assay development, and drug screening platforms. Additionally, it serves as a tool to study galactose-related metabolic networks and their interplay with diseases like diabetes and cancer. Recent advances in protein engineering aim to optimize GALM stability and activity under physiological conditions, enhancing its therapeutic potential. Ongoing research continues to explore its broader biological roles, including potential involvement in cellular signaling and immune modulation, positioning GALM as a multifaceted target in metabolic and precision medicine.
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