| 纯度 | >90%SDS-PAGE. |
| 种属 | E. coli |
| 靶点 | rbcL |
| Uniprot No | P0C512 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 3-477aa |
| 氨基酸序列 | PQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVVGEDNQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRARGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVQARNEGRDLAREGNEIIRSACKWSPELAAACEIWKAIKFEFEPVDKLDS |
| 预测分子量 | 60.1 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rbcL重组蛋白的3条参考文献示例(基于领域内常见研究方向概括，部分信息为模拟内容)：
1. **文献名称**：*Heterologous expression of rbcL in E. coli reveals the role of specific residues in Rubisco assembly*
**作者**：Spreitzer, R.J., et al.
**摘要**：研究通过在大肠杆菌中重组表达烟草rbcL蛋白，结合突变分析，揭示了多个保守氨基酸位点对Rubisco大亚基与小亚基(rbcS)组装的关键作用，为酶复合体工程化改造提供依据。
2. **文献名称**：*Chloroplast-targeted expression of recombinant rbcL enhances photosynthetic efficiency in transgenic tobacco*
**作者**：Sharwood, R.E., et al.
**摘要**：通过在烟草叶绿体中高效表达重组rbcL蛋白，优化Rubisco的叶绿体定位与活性，显著提升了转基因植物的CO₂固定速率和生物量积累，证实了重组技术在光合作用改良中的应用潜力。
3. **文献名称**：*Cryo-EM structure of recombinant rbcL dimer provides insights into Rubisco catalytic mechanism*
**作者**：Whitney, S.M., et al.
**摘要**：利用重组表达的rbcL蛋白进行冷冻电镜结构解析，首次揭示了Rubisco大亚基二聚体的高分辨率三维构象，阐明了其催化位点的动态变化及CO₂/O₂选择性机制。
(注：以上文献信息为模拟归纳，具体研究请以实际数据库检索结果为准。)
The rbcL gene encodes the large subunit of ribulose-1.5-bisphosphate carboxylase/oxygenase (RuBisCO), a critical enzyme in the Calvin-Benson cycle of photosynthesis. RuBisCO catalyzes the fixation of atmospheric CO₂ into organic molecules, making it essential for carbon assimilation in plants, algae, and photosynthetic bacteria. The rbcL protein forms the catalytic core of RuBisCO, working alongside small subunits (encoded by rbcS) to assemble into a functional holoenzyme. Due to its central role in photosynthesis, rbcL has been extensively studied to understand enzyme kinetics, evolutionary adaptations, and responses to environmental stressors like temperature or CO₂ fluctuations.
Recombinant rbcL protein is produced by cloning the rbcL gene into heterologous expression systems (e.g., E. coli, yeast, or cell-free systems) to enable large-scale production for research or biotechnological applications. This approach bypasses challenges in isolating native RuBisCO from plant tissues, which is often low-yield and contaminated with secondary metabolites. Recombinant rbcL allows detailed structural studies (e.g., X-ray crystallography) and mutagenesis experiments to probe catalytic mechanisms or engineer improved CO₂/O₂ specificity—a key goal for enhancing crop photosynthetic efficiency.
Applications extend beyond basic science. Modified rbcL variants are explored in synthetic biology for carbon capture systems or biofuel production. However, functional expression remains technically demanding; proper folding of rbcL requires chaperonins and co-expression with rbcS in many cases. Current research focuses on optimizing expression platforms, engineering thermostable or high-activity variants, and integrating recombinant rbcL into metabolic pathways for sustainable biomanufacturing. These efforts highlight its dual significance as a model for enzyme evolution and a tool for green biotechnology.
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