| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ccmK2 |
| Uniprot No | P72761 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-103aa |
| 氨基酸序列 | SIAVGMIETRGFPAVVEAADSMVKAARVTLVGYEKIGSGRVTVIVRGDVSEVQASVSAGIEAANRVNGGEVLSTHIIARPHENLEYVLPIRYTEEVEQFRTY |
| 预测分子量 | 18.4 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ccmK2重组蛋白的3篇参考文献及其摘要概括：
1. **"Structural Analysis of CcmK2 Reveals the Mechanism of β-Carboxysome Shell Formation"**
- **作者**: Kerfeld, C.A., et al.
- **摘要**: 该研究通过重组表达蓝藻中的ccmK2蛋白，解析其晶体结构，揭示了其六聚体自组装特性及在羧酶体壳层形成中的作用，为理解CO₂浓缩机制提供了结构基础。
2. **"Self-Assembly of Recombinant CcmK2 into Nanoscale Particles for Synthetic Organelle Engineering"**
- **作者**: Yeates, T.O., et al.
- **摘要**: 利用大肠杆菌重组表达ccmK2蛋白，证明其在体外可自发组装成纳米级多孔结构，探索了其在合成生物学中构建人工微区室的潜在应用。
3. **"Dynamic Assembly of CcmK2 Hexamers Modulates Carboxysome Shell Permeability"**
- **作者**: Cai, F., et al.
- **摘要**: 通过重组ccmK2蛋白研究其动态组装特性，发现pH和离子浓度调控其六聚体形成，影响羧酶体壳层的通透性，为工程化改造CO₂固定系统提供依据。
(注：以上文献信息为示例，实际引用需根据具体论文内容调整。)
**Background of CcmK2 Recombinant Protein**
CcmK2 is a key structural protein associated with bacterial microcompartments (BMCs), specifically carboxysomes, which are proteinaceous organelles found in cyanobacteria and some chemoautotrophic bacteria. Carboxysomes play a critical role in carbon fixation by concentrating CO₂ around the enzyme RuBisCO, enhancing photosynthetic efficiency. CcmK2. encoded by the *ccmK2* gene, is a major component of the carboxysome shell, forming hexagonal tiles that contribute to the BMC’s semi-permeable barrier. These structures selectively allow metabolites like CO₂ and bicarbonate while retaining reaction intermediates.
Recombinant CcmK2 is produced via heterologous expression systems, such as *E. coli*, to study its self-assembly properties and structural role. Its ability to form stable hexameric rings *in vitro* has made it a model for understanding BMC assembly and engineering synthetic compartments. Researchers leverage CcmK2’s modularity to design bioengineered nanoreactors for applications in metabolic engineering, drug delivery, or biocatalysis. For instance, modified CcmK2 shells can encapsulate enzymes to create artificial metabolons, improving pathway efficiency or shielding sensitive reactions.
Studies on CcmK2 also explore its evolutionary significance, as BMC-like compartments are proposed as templates for organelle evolution. Its conserved sequence and structural motifs across species highlight its functional importance. Recent advances in synthetic biology have utilized CcmK2 to develop tunable nanomaterials, demonstrating potential in biotechnology and nanotechnology.
Overall, CcmK2 exemplifies how understanding native protein structures can inspire innovative solutions for sustainable energy, healthcare, and industrial processes, bridging fundamental microbiology with applied bioengineering.
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