纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | GAL12 |
Uniprot No | A0A7L0LBI1 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-65aa |
氨基酸序列 | MGILVLVFIFISLTQHGDAHGPDICNHGGGLCRMGTCDSGEYPAQFCFEPVILCCKNPSAATTES |
预测分子量 | 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GAL12重组蛋白的3篇虚构参考文献示例,涵盖不同研究方向:
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1. **文献名称**:*Expression and Functional Characterization of Recombinant GAL12 Protein in Saccharomyces cerevisiae*
**作者**:Martinez A, et al.
**摘要**:本研究报道了GAL12基因在大肠杆菌中的高效表达及在酵母系统中的功能验证。通过亲和层析纯化获得高纯度GAL12蛋白,并证实其参与半乳糖代谢途径的调控作用,为后续代谢工程研究奠定基础。
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2. **文献名称**:*Structural Insights into GAL12 Recombinant Protein via Cryo-EM Analysis*
**作者**:Chen L, et al.
**摘要**:利用冷冻电镜技术解析了GAL12重组蛋白的三维结构,揭示了其与底物结合的活性位点及构象变化机制,为靶向药物设计提供结构生物学依据。
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3. **文献名称**:*Development of a GAL12-Based Biosensor for Monitoring Cellular Stress Response*
**作者**:Kim S, et al.
**摘要**:通过将GAL12重组蛋白与荧光报告系统结合,开发了一种新型生物传感器,实时监测细胞应激反应中的转录激活水平,展示了其在动态代谢监测中的应用潜力。
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**注**:以上文献为示例性内容,实际研究中建议通过学术数据库(如PubMed、Web of Science)检索真实文献。若需进一步调整方向或补充细节,请随时说明!
**Background of GAL12 Recombinant Protein**
The GAL12 recombinant protein is a genetically engineered biomolecule derived from the *GAL* gene family, which is primarily associated with galactose metabolism in various organisms. Originally identified in yeast (*Saccharomyces cerevisiae*), the *GAL* genes encode enzymes and regulatory proteins critical for the conversion of galactose into glucose-1-phosphate, a key step in energy production. GAL12. though less characterized than other *GAL* members (e.g., GAL1. GAL4. or GAL10), is hypothesized to play a role in modulating galactose-responsive pathways or interacting with metabolic regulators.
Recombinant GAL12 is produced using expression systems such as *E. coli* or yeast, where the gene encoding GAL12 is cloned into a plasmid, expressed under inducible promoters, and purified via affinity chromatography (e.g., His-tag). Its recombinant form enables detailed study of its structural and functional properties, including enzymatic activity, substrate specificity, or protein-protein interactions.
Research on GAL12 is often linked to understanding metabolic disorders, microbial biotechnology, or synthetic biology. For instance, in industrial fermentation, optimizing galactose utilization pathways through proteins like GAL12 could enhance bioethanol production. In biomedicine, dysregulation of galactose metabolism is tied to diseases like galactosemia, making GAL12 a potential diagnostic or therapeutic target.
Despite its emerging significance, the precise biological role of GAL12 remains under investigation. Current studies focus on elucidating its 3D structure, catalytic mechanisms, and regulatory networks using techniques like X-ray crystallography, CRISPR-based gene editing, or omics approaches. These efforts aim to expand its applications in biotechnology, metabolic engineering, and precision medicine.
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