| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | groL |
| 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. |
以下是关于groL重组蛋白的3-4篇参考文献及简要摘要：
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1. **"Chaperonin-mediated protein folding: GroEL binds to one end of an elongated polypeptide chain"**
*Authors: Braig, K., Simon, M., Furuya, F., Hainfeld, J.F., Horwich, A.L.*
**摘要**：通过冷冻电镜和X射线晶体学分析，揭示了GroEL的结构及其与未折叠蛋白质的结合机制，证明GroEL通过疏水区域捕获底物蛋白的延伸链，为后续折叠提供保护环境。
2. **"Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and ATP"**
*Authors: Goloubinoff, P., Gatenby, A.A., Lorimer, G.H.*
**摘要**：研究GroEL/GroES系统在ATP依赖的蛋白质折叠中的作用，证明重组GroEL与GroES协同帮助变性的核酮糖二磷酸羧化酶(Rubisco)正确折叠并恢复活性。
3. **"The GroEL-GroES chaperonin machine: A nano-cage for protein folding"**
*Authors: Saibil, H.R.*
**摘要**：综述GroEL-GroES复合物的结构与功能，阐述其作为分子伴侣通过形成封闭“笼状结构”隔离未折叠蛋白，防止聚集并促进折叠的分子机制。
4. **"Engineering of a recombinant protein production system in Escherichia coli using the GroES-GroL chaperone team"**
*Authors: de Marco, A., Deuerling, E., Mogk, A., Tomoyasu, T., Bukau, B.*
**摘要**：提出通过共表达GroEL/GroES增强大肠杆菌中重组蛋白的可溶性和产量，验证其在改善外源蛋白(如抗体片段)折叠效率中的应用潜力。
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以上文献涵盖GroL的结构、功能机制及其在重组蛋白表达中的应用。如需具体文章细节，可进一步通过PubMed或学术数据库检索。
The groL gene encodes GroEL, a key molecular chaperone in the bacterial heat shock protein 60 (HSP60) family, best studied in *Escherichia coli*. As part of the GroEL-GroES chaperonin system, GroEL assists in the ATP-dependent folding of nascent or misfolded polypeptides, preventing aggregation under stress. Structurally, GroEL forms a double-ring complex with 14 subunits, creating a central cavity where substrate proteins fold in an isolated environment. Its cooperation with GroES, a co-chaperone, facilitates cyclical conformational changes essential for substrate release.
Recombinant GroEL protein is widely produced in heterologous expression systems (e.g., *E. coli*) for structural, functional, and biomedical studies. Its recombinant form retains the ability to stabilize and refold client proteins, making it valuable for in vitro protein folding assays and biotechnology applications. In vaccine development, GroEL’s immunogenic properties have been exploited as an antigen or adjuvant, particularly in studies targeting bacterial pathogens like *Helicobacter pylori* or *Mycobacterium tuberculosis*. Additionally, it serves as a model system to study chaperone-mediated mechanisms in neurodegenerative diseases linked to protein misfolding, such as Alzheimer’s or Parkinson’s.
Beyond basic research, recombinant GroEL has industrial relevance in enhancing soluble expression of aggregation-prone proteins during recombinant protein production. Its engineered variants are also explored for drug delivery or nanotechnology due to their cage-like structure. Despite its prokaryotic origin, GroEL’s functional conservation with eukaryotic HSP60 homologs underscores its broad applicability in understanding cellular proteostasis.
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