纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | pat |
Uniprot No | Q57146 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-183aa |
氨基酸序列 | MSPERRPVEIRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQEWIDDLERLQDRYPWLVAEVEGVVAGIAYAGPWKARNAYDWTVESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHDVGFWQRDFELPAPPRPVRPVTQI |
预测分子量 | 36.6 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PAT重组蛋白的3-4篇模拟参考文献(非真实文献,仅示例格式):
1. **《Heterologous Expression and Characterization of PAT Recombinant Protein in Transgenic Plants》**
- 作者:Zhang et al., 2020
- 摘要:研究通过大肠杆菌表达系统成功克隆并纯化PAT(phosphinothricin acetyltransferase)重组蛋白,证明其在转基因植物中赋予草铵膦抗性,为抗除草剂作物开发提供依据。
2. **《Optimization of PAT Recombinant Protein Production in E. coli for Industrial Applications》**
- 作者:Lee et al., 2018
- 摘要:系统优化PAT重组蛋白在大肠杆菌中的表达条件(如温度、诱导剂浓度),显著提高蛋白产量和酶活性,为大规模生产提供技术方案。
3. **《Structural and Functional Analysis of PAT Recombinant Protein in Herbicide Detoxification》**
- 作者:Singh et al., 2019
- 摘要:通过X射线晶体学解析PAT重组蛋白的三维结构,揭示其催化草铵膦乙酰化的分子机制,并验证其在体外环境中的高效解毒功能。
4. **《PAT Recombinant Protein as a Novel Adjuvant in Vaccine Development》**
- 作者:Garcia et al., 2021
- 摘要:首次报道PAT重组蛋白作为免疫佐剂的应用,实验表明其可增强模型抗原的体液免疫应答,拓展了PAT蛋白在生物医学领域的潜在用途。
(注:以上文献为示例性质,实际研究中请根据具体需求检索真实数据库。)
PAT recombinant proteins are engineered fusion proteins that incorporate the phosphinothricin acetyltransferase (PAT) enzyme, derived from soil bacteria like *Streptomyces viridochromogenes*. Initially identified for its role in herbicide resistance, PAT detoxifies phosphinothricin (PPT), the active component of herbicides such as glufosinate, by acetylation. This property has made PAT a critical selectable marker in plant biotechnology, particularly in generating genetically modified crops resistant to herbicides.
In recombinant protein design, PAT is often fused to target proteins of interest via genetic engineering. This serves dual purposes: enabling simplified purification of the recombinant protein through PAT's enzymatic activity and providing a visual or biochemical marker for screening successfully transformed organisms. The PAT gene is typically co-expressed with the target gene in host systems like *E. coli*, yeast, or mammalian cells, leveraging its prokaryotic origin for minimal cross-reactivity in eukaryotic systems.
Beyond agricultural applications, PAT recombinant proteins are utilized in basic research to study protein-protein interactions, cellular localization, and metabolic pathways. Their stability and ease of detection also make them valuable in industrial enzyme production and biopharmaceutical development. However, concerns about antibiotic resistance gene analogs in transgenic products have spurred innovations, such as PAT variants with reduced environmental persistence. Ongoing research focuses on optimizing PAT fusion tags for enhanced solubility and yield, reflecting its enduring utility in synthetic biology and biomanufacturing.
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