纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | EPSPS1 |
Uniprot No | W0FAR5 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-332aa |
氨基酸序列 | AAGGNASYVLDGVPRMRERPIGDLVAGLKQLGADVDCFMGTNCPPVRVNAMGGLPGGKVKLSGSISSQYLTALLMAAPLALGDVEIEIIDKLISIPYVEMTLKLMERFGVKVEHSDNWDRFYIKGAQKYKSPGNAYVEGDASSASYFLAGAAVTGGTVTVEGCGTSSLQGDVKFAEVLEKMGAKVSWTENSVTVTGPPRDPSKKGHLRGIDVNMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMVAICTELRKLGATVEEGPDFCIITPPEKLNITAIDTYDDHRMAMAFSIAACADVPVTIRDPGCTRKTFPDYFDVLQRFTKH |
预测分子量 | 35,6 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EPSPS1重组蛋白的3篇虚构参考文献示例(仅供格式参考):
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1. **标题**: *Heterologous Expression and Characterization of EPSPS1 in Escherichia coli*
**作者**: Zhang, L., et al.
**摘要**: 研究通过克隆植物来源的EPSPS1基因,在大肠杆菌中实现高效可溶性表达,并利用亲和层析纯化获得活性重组蛋白。酶动力学分析表明该蛋白对底物PEP和S3P具有高亲和力,为后续抗草甘膦机制研究提供基础。
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2. **标题**: *Structural Insights into EPSPS1 Mutants Conferring Glyphosate Resistance*
**作者**: Smith, J.R., & Thompson, M.
**摘要**: 通过X射线晶体学解析重组EPSPS1蛋白及其突变体(Pro106Ser)的三维结构,揭示突变导致草甘膦结合位点空间位阻增加,从而降低除草剂敏感性,为抗性作物设计提供结构依据。
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3. **标题**: *Optimization of EPSPS1 Recombinant Protein Production in Pichia pastoris*
**作者**: Chen, H., et al.
**摘要**: 报道在毕赤酵母系统中优化EPSPS1的分泌表达条件,通过诱导温度、pH和甲醇浓度调控,使重组蛋白产量提高3倍,并验证其体外酶活稳定性,为大规模工业化制备奠定基础。
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注:以上文献为示例性质,实际引用时请以真实出版物为准。建议通过PubMed、Web of Science等数据库检索关键词(如“EPSPS recombinant protein”“glyphosate resistance”)获取权威文献。
**Background of EPSPS1 Recombinant Protein**
EPSPS1 (5-enolpyruvylshikimate-3-phosphate synthase 1) is a key enzyme in the shikimate pathway, a metabolic route essential for the biosynthesis of aromatic amino acids (phenylalanine, tyrosine, and tryptophan) in plants, bacteria, fungi, and some microbes. This pathway is absent in animals, making EPSPS a target for herbicides like glyphosate, which competitively inhibits its activity. Glyphosate-resistant crops (e.g., Roundup Ready® varieties) often express a modified *EPSPS* gene derived from *Agrobacterium* strain CP4 (CP4 EPSPS), which retains functionality even in the presence of the herbicide.
Recombinant EPSPS1 proteins are produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or eukaryotic (e.g., yeast, insect cells) expression systems. These systems enable large-scale production of the enzyme for research and industrial applications. The recombinant protein retains the catalytic function of native EPSPS, converting shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) into 5-enolpyruvylshikimate-3-phosphate (EPSP), a precursor for chorismate synthesis.
Studies on EPSPS1 focus on understanding its structure-activity relationship, herbicide resistance mechanisms, and potential biotechnological uses. For example, engineered EPSPS variants with reduced glyphosate sensitivity are critical for developing next-generation herbicide-tolerant crops. Additionally, recombinant EPSPS1 serves as a tool for enzymatic assays, inhibitor screening, and antibody production in diagnostic kits.
Overall, EPSPS1 recombinant proteins bridge agricultural innovation and biochemical research, addressing challenges in crop protection and sustainable agriculture while providing insights into enzyme evolution and metabolic engineering.
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