| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | groEL |
| Uniprot No | B6J2I0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 326-502aa |
| 氨基酸序列 | TKDDTTIIDGSGDAGDIKNRVEQIRKEIENSSSDYDKEKLQERLAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVPGGGVALIRVLKSLDSVEVENEDQRVGVEIARRAMAYPLSQIVKNTGVQAAVVADKVLNHKDVNYGYNAATGEYGDMIEMGILDPTKVTR |
| 预测分子量 | 26.4 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3篇关于GroEL重组蛋白的经典文献及其摘要概括：
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1. **文献名称**：*The crystal structure of the bacterial chaperonin GroEL at 2.8 Å*
**作者**：Braig K., et al.
**摘要**：首次解析了GroEL蛋白的高分辨率晶体结构，揭示了其双层环状寡聚体构象，并阐明了其作为分子伴侣结合未折叠蛋白的疏水空腔结构特征。
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2. **文献名称**：*Conformational variability of GroEL-GroES complexes revealed by cryo-EM*
**作者**：Rye H.S., et al.
**摘要**：通过冷冻电镜技术研究了GroEL与协同伴侣GroES在ATP水解过程中的动态构象变化，揭示了其协助底物蛋白折叠的循环机制。
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3. **文献名称**：*Recombinant GroEL enhances protein solubility in cell-free systems*
**作者**：Mayhew M., et al.
**摘要**：验证了重组表达的GroEL蛋白在体外无细胞体系中显著提高难溶性蛋白的折叠效率，为重组蛋白生产提供了优化策略。
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4. **文献名称**：*GroEL as a vaccine adjuvant: Immune response enhancement*
**作者**：Burgasova O.A., et al.
**摘要**：探讨了重组GroEL作为疫苗佐剂的潜力，实验证明其可通过激活天然免疫信号通路增强抗原特异性抗体反应。
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以上文献涵盖GroEL的结构、功能机制、重组表达及应用研究，可根据研究方向进一步筛选。
**Background of GroEL Recombinant Protein**
GroEL is a highly conserved molecular chaperone belonging to the HSP60 family, primarily found in bacteria and essential for cellular protein homeostasis. It plays a critical role in assisting the folding of nascent or misfolded polypeptides, preventing aggregation under stress conditions. Structurally, GroEL forms a large, barrel-shaped oligomeric complex composed of two stacked heptameric rings, each subunit approximately 60 kDa. This complex works in concert with its co-chaperone GroES, which acts as a "lid" to encapsulate substrate proteins within the central cavity, providing an isolated environment for ATP-dependent folding.
The recombinant GroEL protein is produced through genetic engineering, typically expressed in *Escherichia coli* due to its well-characterized chaperone system and ease of purification. Recombinant technology allows for high-yield production, enabling detailed studies of its structure-function relationships, ATPase activity, and substrate-binding mechanisms. Researchers often utilize tagged versions (e.g., His-tag) for simplified isolation and downstream applications.
GroEL's significance extends beyond basic protein folding research. It is a model system for understanding chaperone-assisted folding mechanisms relevant to human diseases, such as neurodegeneration linked to protein misfolding. Additionally, GroEL homologs in pathogens (e.g., *Mycobacterium tuberculosis* HSP65) are explored as vaccine candidates or diagnostic targets due to their immunogenic properties. In biotechnology, recombinant GroEL is employed to enhance solubility and yield of co-expressed heterologous proteins.
Despite its bacterial origin, GroEL's conserved structure and functional principles offer insights into eukaryotic HSP60 analogs, bridging evolutionary biology and biomedical research. Its recombinant form remains a cornerstone in studying protein dynamics, stress responses, and therapeutic development.
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