| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | 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. |
以下是3篇关于HSP60重组蛋白的经典文献概览：
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1. **文献名称**：*"Suppression of experimental autoimmune diabetes using HSP60 peptide-loaded dendritic cells"*
**作者**：Cohen IR, Elias D, et al.
**摘要**：该研究利用重组HSP60蛋白衍生的多肽负载树突状细胞，成功抑制了非肥胖糖尿病(NOD)小鼠模型中1型糖尿病的进展，揭示了HSP60通过调节自身反应性T细胞介导免疫耐受的机制。
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2. **文献名称**：*"Recombinant Mycobacterium tuberculosis HSP60 induces pro-inflammatory responses in human macrophages"*
**作者**：Zügel U, Kaufmann SHE.
**摘要**：研究通过表达并纯化结核分枝杆菌HSP60重组蛋白，发现其可激活人巨噬细胞中的TLR2/4信号通路，促进促炎因子(如TNF-α和IL-6)分泌，为HSP60在感染免疫中的双重角色(保护性与致病性)提供了依据。
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3. **文献名称**：*"Structural and functional analysis of mitochondrial HSP60 chaperonin oligomers"*
**作者**：Horwich AL, Fenton WA.
**摘要**：通过重组技术表达并解析线粒体HSP60的寡聚体结构，揭示了其依赖ATP的蛋白质折叠机制，并证明突变型HSP60与遗传性神经退行性疾病(如遗传性痉挛性截瘫)的相关性。
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4. **文献名称**：*"Recombinant human HSP60 promotes tumor cell invasion via TLR4 signaling in colorectal cancer"*
**作者**：Campisi L, Chisari G, et al.
**摘要**：该研究发现结直肠癌细胞分泌的重组人HSP60通过结合TLR4受体激活NF-κB通路，增强肿瘤细胞的迁移和侵袭能力，提示靶向HSP60-TLR4轴可能成为癌症治疗新策略。
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这些研究涵盖了HSP60重组蛋白在免疫调节、感染、神经疾病及癌症中的关键作用，反映了其多功能的生物学特性。
Heat shock protein 60 (HSP60), a member of the chaperonin family, is a highly conserved molecular chaperone critical for maintaining cellular proteostasis. It primarily resides in mitochondria, assisting in the folding and assembly of nascent polypeptides, particularly under stress conditions. HSP60 forms a double-ring oligomeric structure with ATPase activity, enabling it to bind and release substrate proteins through conformational changes. Beyond its canonical role in protein quality control, HSP60 participates in diverse physiological processes, including apoptosis regulation, immune modulation, and inflammatory responses.
Recombinant HSP60 proteins are engineered through genetic cloning and expression systems (e.g., E. coli, mammalian cells) to study their structure-function relationships and therapeutic potential. Researchers often purify these proteins using affinity tags followed by chromatographic techniques. The recombinant form retains the conserved GroEL-like structural domains while allowing species-specific modifications for targeted studies. Notably, HSP60 exhibits dual roles in pathologies: it protects cells during stress but may also trigger autoimmune reactions when mislocalized to the cytoplasm or extracellular space, implicated in diseases like rheumatoid arthritis and atherosclerosis.
Current applications of recombinant HSP60 span vaccine development against microbial pathogens (leveraging its homology with bacterial GroEL), cancer immunotherapy research due to its surface expression on stressed tumor cells, and neurodegenerative disease models investigating protein misfolding. Recent studies also explore extracellular HSP60 as a damage-associated molecular pattern (DAMP) in chronic inflammatory conditions. However, challenges persist in distinguishing its protective versus pathogenic roles and optimizing delivery systems for therapeutic use. Ongoing research continues to unravel HSP60's pleiotropic functions, positioning recombinant proteins as essential tools for both mechanistic studies and clinical translation.
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