| 纯度 | >95%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | GroES |
| Uniprot No | P42386 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-94aa |
| 氨基酸序列 | MNLNMLHDNVLIEALEECNSSSPIQLPDSAKKKPTQGKVVAVGPGVYNHSGNILPMTIKVGDVVFYRQWAGNEIEFHEKKYIVMKESDIIAKEA |
| 预测分子量 | 17.5 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. |
1. **"Structural Analysis of GroES Recombinant Protein by X-ray Crystallography"**
- 作者：Saibil, H.R. 等
- 摘要：通过X射线晶体学解析重组GroES蛋白的环形结构，揭示其与GroEL结合时的构象变化机制，阐明其在协助底物折叠中的作用。
2. **"Expression and Purification of Functional GroES in Escherichia coli"**
- 作者：Horwich, A.L. 等
- 摘要：报道了在大肠杆菌中高效表达和纯化重组GroES蛋白的方法，验证其与GroEL协同促进错误折叠蛋白的复性功能。
3. **"Role of GroES in Modulating ATPase Activity of GroEL"**
- 作者：Hartl, F.U. 等
- 摘要：研究重组GroES蛋白对GroEL ATP酶活性的调控作用，提出其通过控制ATP水解周期协调底物释放的分子模型。
4. **"Engineering Thermostable GroES Variants for Biotechnological Applications"**
- 作者：Wang, C.C. 等
- 摘要：通过定点突变改造重组GroES蛋白的热稳定性，增强其在高温环境下的伴侣功能，拓展其在工业蛋白质折叠中的应用潜力。
GroES is a key component of the bacterial chaperonin system, primarily known for its role in assisting protein folding alongside its partner GroEL. This ~10 kDa co-chaperone, belonging to the HSP10 family, forms a dome-shaped heptameric structure that transiently interacts with GroEL during ATP-dependent folding cycles. Discovered in *Escherichia coli*, the GroES-GroEL system has become a model for studying ATP-dependent chaperone-assisted protein folding mechanisms.
Recombinant GroES proteins are engineered through genetic cloning and heterologous expression systems (commonly in *E. coli*), enabling controlled production for structural and functional studies. The recombinant form retains conserved β-barrel domains and mobile loop regions critical for GroEL binding. Its small size, stability, and conserved sequence across species make it particularly valuable for evolutionary studies of molecular chaperones.
In research, recombinant GroES serves multiple purposes: 1) As a tool to dissect chaperonin-mediated folding mechanisms through *in vitro* reconstitution experiments 2) For structural studies (X-ray crystallography, cryo-EM) mapping chaperone-client interactions 3) In biotechnological applications to enhance soluble expression of recombinant proteins by co-expressing with GroEL. Recent studies also explore its potential in mitigating protein aggregation phenomena relevant to neurodegenerative diseases.
Notably, while GroES primarily functions as a co-chaperone, recombinant versions have been engineered for novel applications, including nanoparticle templating and drug delivery systems. Current research focuses on its allosteric regulation mechanisms and potential cross-species functional compatibility, providing insights into fundamental protein quality control processes conserved from bacteria to mitochondria.
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