纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | Aspdh |
Uniprot No | A6ND91 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-283aa |
氨基酸序列 | MADRGPWRVG VVGYGRLGQS LVSRLLAQGP ELGLELVFVW NRDPGRMAGS VPPSLQLQNL AALGERRPDL VVEVAHPKII HESGAQILRH ANLLVGSPSA LSDQTTERQL LEASQHWDHA VFVARGALWG AEDIRRLDAA GGLRSLRVTM ATHPDGFRLE GPLAAAHSPG PCTVLYEGPV RGLCPFAPRN SNTMAAAALA APSLGFDGVI GVLVADTSLT DMHVVDVELS GPRGPTGRSF AVHTRRENPA EPGAVTGSAT VTAFWQSLLA CCQLPSRPGI HLC |
预测分子量 | 29,9 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Aspdh(假设为天冬氨酸脱氢酶,Aspartate Dehydrogenase)重组蛋白的模拟参考文献示例,供参考格式使用。实际文献建议通过学术数据库进一步检索:
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1. **文献名称**:*Heterologous Expression and Characterization of Recombinant Aspdh from Bacillus subtilis*
**作者**:Zhang L., et al.
**摘要**:本研究在大肠杆菌中成功表达了重组Aspdh蛋白,优化了表达条件,并证实其催化天冬氨酸转化为草酰乙酸的活性,为工业酶应用提供了基础。
2. **文献名称**:*Structural Insights into Aspdh: Crystallographic Analysis of a Novel Recombinant Enzyme*
**作者**:Tanaka K., et al.
**摘要**:通过X射线晶体学解析了Aspdh的三维结构,揭示了其底物结合位点及催化机制,为理性设计高活性突变体提供了依据。
3. **文献名称**:*Application of Recombinant Aspdh in Biocatalytic Synthesis of L-Aspartate Derivatives*
**作者**:Müller R., et al.
**摘要**:开发了一种基于重组Aspdh的生物催化体系,高效合成L-天冬氨酸衍生物,展示了其在药物合成中的潜力。
4. **文献名称**:*Thermostability Engineering of Aspdh through Directed Evolution*
**作者**:Chen H., et al.
**摘要**:利用定向进化技术改良Aspdh的热稳定性,获得在高温下仍保持活性的突变体,拓展了其在高温工业流程中的应用。
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**注意**:以上为模拟文献,如需真实文献,建议检索关键词如“Aspartate Dehydrogenase recombinant expression”或“Aspdh protein purification”在PubMed、Web of Science等平台。
**Background of Aspartate Dehydrogenase (AspDH) Recombinant Protein**
Aspartate dehydrogenase (AspDH) is an enzyme that catalyzes the reversible conversion of L-aspartate to oxaloacetate using NAD(P)+ as a cofactor. This reaction plays a role in nitrogen metabolism and the tricarboxylic acid (TCA) cycle, linking amino acid metabolism with energy production. Although AspDH is less studied compared to other dehydrogenases, its potential applications in biotechnology, such as biosensors or enzymatic synthesis of aspartate-derived compounds, have driven interest in its recombinant production.
Recombinant AspDH is typically produced via heterologous expression in bacterial hosts like *Escherichia coli*. The gene encoding AspDH is cloned into expression vectors, often fused with affinity tags (e.g., His-tag) to facilitate purification. Optimization of expression conditions (e.g., induction temperature, IPTG concentration) ensures high yield and solubility. Structural studies of recombinant AspDH have provided insights into its catalytic mechanism, substrate specificity, and stability, aiding in protein engineering efforts to enhance activity or thermostability for industrial use.
Applications of recombinant AspDH span biocatalysis, where it enables eco-friendly synthesis of chiral intermediates for pharmaceuticals, and diagnostics, where it serves as a component in enzymatic assays. Additionally, its role in metabolic pathways makes it a target for metabolic engineering in microbial cell factories. Challenges remain in scaling production and improving enzyme performance under non-physiological conditions. Continued research focuses on tailoring AspDH properties through directed evolution or computational design, aiming to expand its utility in sustainable biomanufacturing and biomedical research.
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