| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | GPM1 |
| Uniprot No | P00950 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-247aa |
| 氨基酸序列 | PKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPDVLYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAETLKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKDLLSGKTVMIAAHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAAVANQGKK |
| 预测分子量 | 29.5 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GPM1重组蛋白的参考文献示例(注：部分文献为假设性示例，建议通过学术数据库核实具体信息)：
1. **《Heterologous expression and characterization of recombinant GPM1 in Escherichia coli》**
*作者：A. Smith, B. Lee*
摘要：本研究在大肠杆菌中成功表达了重组GPM1蛋白，优化了表达条件并采用亲和层析技术纯化。通过酶活实验证实重组蛋白具有甘油醛-3-磷酸脱氢酶活性，为工业化应用提供了基础。
2. **《Structural insights into GPM1 from Saccharomyces cerevisiae by X-ray crystallography》**
*作者：C. Zhang 等*
摘要：通过X射线晶体学解析了酿酒酵母GPM1蛋白的三维结构，揭示了其底物结合位点及催化机制，为设计靶向该酶的抑制剂提供了结构基础。
3. **《Functional analysis of GPM1 in glycolysis regulation using recombinant protein mutants》**
*作者：K. Nakamura, T. Watanabe*
摘要：利用定点突变技术构建了GPM1重组突变体，发现其特定氨基酸残基对酶活性和酵母细胞糖酵解通量调控具有关键作用。
4. **《Application of recombinant GPM1 in enzymatic synthesis of high-value metabolites》**
*作者：L. García 等*
摘要：将重组GPM1与其它糖酵解酶偶联，开发了一种体外合成途径，高效生成1.3-二磷酸甘油酸，展示了其在生物催化领域的潜力。
**建议**：可通过PubMed、Web of Science或Google Scholar搜索关键词“GPM1 recombinant protein”“GPM1 expression”等获取最新文献。注意结合具体研究领域(如物种、应用场景)筛选结果。
**Background of GPM1 Recombinant Protein**
GPM1. or Glycerol-3-phosphate dehydrogenase 1. is a critical enzyme involved in cellular metabolism, particularly in the glycolysis and gluconeogenesis pathways. It catalyzes the reversible conversion of dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate (G3P), a key step in lipid biosynthesis, energy production, and redox balance. In eukaryotic organisms, including yeast and mammals, GPM1 plays a dual role: it supports carbohydrate metabolism under aerobic conditions and aids in adapting to anaerobic environments by modulating glycerol synthesis.
The recombinant GPM1 protein is engineered through heterologous expression systems, such as *E. coli* or yeast, to produce high-purity, functional enzyme for research and industrial applications. Cloning the *GPM1* gene into expression vectors allows controlled overexpression, followed by affinity chromatography (e.g., His-tag purification) to isolate the protein. This recombinant form retains native enzymatic activity, enabling studies on its structure-function relationships, kinetic properties, and regulatory mechanisms.
Interest in GPM1 spans multiple fields. In biotechnology, it is explored for metabolic engineering to enhance microbial production of biofuels and value-added chemicals. In medicine, dysregulation of GPM1 has been linked to metabolic disorders, cancer, and neurodegenerative diseases, making it a potential therapeutic target. Additionally, structural analyses of recombinant GPM1 (e.g., X-ray crystallography) provide insights into substrate binding sites and catalytic residues, aiding drug design.
Overall, GPM1 recombinant protein serves as a vital tool for advancing both basic science and applied research in metabolism, disease mechanisms, and bioproduction.
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