| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPD1 / HSP60 |
| Uniprot No | P10809 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-573aa |
| 氨基酸序列 | AKDV KFGADARALM LQGVDLLADA VAVTMGPKGR TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ VATISANGDK EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV TKDDAMLLKG KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLTPANED QKIGIEIIKR TLKIPAMTIA KNAGVEGSLI VEKIMQSSSE VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEVVVTEIP KEEKDPGMGA MGGMGGGMGG GMF |
| 预测分子量 | 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. **"Recombinant human HSP60 produced in Escherichia coli enhances antigen-specific T-cell responses in vitro"**
- **作者**: Zanin-Zhorov, A. et al.
- **摘要**: 研究通过大肠杆菌表达重组人HSP60蛋白，验证其分子伴侣活性及免疫调节功能，发现其可增强抗原特异性T细胞反应，提示在免疫治疗中的应用潜力。
2. **"Production and characterization of recombinant HSP60 (GroEL) from Chlamydia pneumoniae"**
- **作者**: Kol, A. et al.
- **摘要**: 报道肺炎衣原体HSP60(GroEL同源物)的重组表达与纯化，分析其促炎特性，揭示其在动脉粥样硬化等慢性炎症疾病中的潜在作用机制。
3. **"Functional analysis of mitochondrial HSP60 chaperonin in Parkinson’s disease models"**
- **作者**: De Mena, L. et al.
- **摘要**: 利用重组HSP60蛋白研究其在帕金森病模型中对线粒体蛋白错误折叠的修复能力，表明HSP60过表达可减轻神经细胞毒性，为神经退行性疾病提供治疗靶点。
4. **"Recombinant HSP60 from Helicobacter pylori induces pro-inflammatory cytokine production in macrophages"**
- **作者**: Takeda, K. et al.
- **摘要**: 通过重组幽门螺杆菌HSP60验证其激活巨噬细胞并诱导IL-6、TNF-α等炎症因子释放的作用，探讨其在胃部感染及免疫病理中的角色。
HSPD1. also known as heat shock protein 60 (HSP60), is a mitochondrial chaperonin encoded by the HSPD1 gene in humans. As a member of the heat shock protein family, it plays a critical role in maintaining cellular homeostasis by assisting in the folding and assembly of newly synthesized proteins within mitochondria. HSP60 forms a characteristic double-ring structure that binds unfolded polypeptides in an ATP-dependent manner, preventing misfolding and aggregation under stress conditions. Its expression is upregulated during cellular stress, such as heat shock, oxidative damage, or pathogen invasion, to protect mitochondrial integrity.
Recombinant HSP60 proteins are engineered using expression systems like *E. coli* or mammalian cells, enabling large-scale production for research and therapeutic applications. These proteins retain the functional domains required for chaperone activity, making them valuable tools for studying mitochondrial protein dynamics, stress response pathways, and disease mechanisms. Dysregulation of HSP60 has been linked to neurodegenerative disorders (e.g., Alzheimer’s), autoimmune diseases (e.g., rheumatoid arthritis), and cancer, where it may promote tumor survival by inhibiting apoptosis.
Notably, HSP60 exhibits dual roles in immunity. While it assists in antigen presentation and modulates inflammatory responses, its extracellular release can trigger autoimmune reactions through molecular mimicry. Recombinant HSP60 is being explored as a diagnostic biomarker for inflammatory conditions and a therapeutic target. In vaccine development, its immunomodulatory properties are harnessed to enhance immune responses against pathogens or tumor antigens. Ongoing research also investigates its potential in mitochondrial-targeted therapies and as a stress-indicator in aging-related studies. However, its context-dependent pro-inflammatory or anti-inflammatory effects require careful evaluation in clinical applications.
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