| 纯度 | >90%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | glpK |
| Uniprot No | P0A6F3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-502aa |
| 氨基酸序列 | TEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTLVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPISGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEHDE |
| 预测分子量 | 60.1kDa |
| 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glpK重组蛋白的示例参考文献(基于常见研究方向构建，建议通过学术数据库获取具体文献)：
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1. **文献名称**: "Cloning, Expression, and Characterization of Recombinant Glycerol Kinase (glpK) from *Escherichia coli*"
**作者**: Smith A, et al.
**摘要**: 本研究报道了大肠杆菌glpK基因的克隆及其在重组宿主中的高效表达，通过亲和层析纯化获得高活性蛋白，并分析了酶的最适pH、温度及动力学参数(Km和Vmax)，为后续代谢工程研究奠定基础。
2. **文献名称**: "Structural Insights into the Allosteric Regulation of Bacterial Glycerol Kinase"
**作者**: Johnson B, et al.
**摘要**: 通过X射线晶体学解析了重组glpK蛋白的三维结构，揭示了其变构调节机制，阐明了甘油结合位点与ATP催化域之间的构象变化，为设计酶活性调节剂提供结构基础。
3. **文献名称**: "Enhancing Glycerol Utilization in *Saccharomyces cerevisiae* by Heterologous Expression of glpK"
**作者**: Chen L, et al.
**摘要**: 将细菌glpK基因导入酿酒酵母中重组表达，显著提高了菌株对甘油的代谢能力，优化了发酵工艺，证明外源glpK在真核宿主中的功能活性及其在生物燃料生产中的应用潜力。
4. **文献名称**: "Site-Directed Mutagenesis of glpK Improves Thermal Stability and Activity"
**作者**: Wang Y, et al.
**摘要**: 通过定点突变技术改造glpK重组蛋白，获得热稳定性与催化效率提升的突变体，分子动力学模拟表明关键氨基酸残基对酶构象稳定的贡献，为工业酶优化提供策略。
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**注**：以上文献为示例，实际研究中请通过PubMed、Web of Science等平台以关键词“glpK recombinant protein”、“glycerol kinase expression”检索最新论文。
**Background of glpK Recombinant Protein**
The *glpK* gene encodes glycerol kinase (GlpK), a key enzyme in bacterial glycerol metabolism. Found in organisms like *Escherichia coli*, GlpK catalyzes the ATP-dependent phosphorylation of glycerol to glycerol-3-phosphate (G3P), the first step in glycerol utilization. This reaction links glycerol to central carbon metabolism, enabling its use as a carbon source for energy production or biosynthesis. GlpK activity is tightly regulated at transcriptional and post-translational levels, often controlled by the GlpR repressor or cAMP-CRP complexes, ensuring metabolic flexibility under varying nutrient conditions.
Recombinant GlpK protein is produced via heterologous expression in bacterial hosts (e.g., *E. coli*) or eukaryotic systems. The gene is cloned into expression vectors, expressed under inducible promoters, and purified using affinity chromatography. Recombinant GlpK retains enzymatic activity, making it valuable for studying glycerol metabolism, enzyme kinetics, and allosteric regulation. Structural studies using recombinant GlpK have revealed insights into its catalytic mechanism and regulatory domains, aiding drug design targeting pathogenic bacteria reliant on glycerol metabolism.
In biotechnology, GlpK is leveraged in metabolic engineering to enhance microbial production of biofuels (e.g., ethanol) or biochemicals by optimizing glycerol uptake. It also serves as a model enzyme for investigating carbon source prioritization in mixed-substrate environments. Additionally, GlpK’s role in bacterial virulence has spurred interest in developing inhibitors against pathogens like *Klebsiella pneumoniae* or *Staphylococcus aureus*.
Overall, recombinant GlpK is a critical tool for advancing both basic research and applied microbiology, bridging gaps between metabolic regulation, structural biology, and biotechnological innovation.
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