Product Name
Chaperonin 60 from Escherichia coli, >95% (SDS-PAGE), recombinant, expressed in E. coli overproducing strain, lyophilized powder
biological source
Escherichia coli
recombinant
expressed in E. coli overproducing strain
assay
>95% (SDS-PAGE)
form
lyophilized powder
technique(s)
electron microscopy: suitable
mass spectrometry (MS): suitable
suitability
passes test (Refolding (w/GroES))
UniProt accession no.
storage temp.
2-8°C
Quality Level
Gene Information
human ... HSPD1(3329)
Application
Chaperonin 60 from Escherichia coli has been used:
- in mass spectroscopy
- in cryo-electron microscopy imaging as control for testing particle distribution
- as standard in infrared spectrum measurements
- as a protein sample for stability assessment and characterization studies using differential mobility analysis (DMA) and cryo-electron microscopy (cryo-EM).
Biochem/physiol Actions
Apart from its role in facilitating protein folding, chaperonin 60 (Cpn60) serves as an extracellular signaling protein, showing functional similarities to certain proinflammatory cytokines. Furthermore, Cpn60 contributes to the inhibition of lipid accumulation and adipogenesis during the initial stages of cellular differentiation, thereby exerting anti-obesity effects.
General description
Research area: Cell Signaling
Chaperonin 60 (GroEL) and chaperonin 10 (GroES) belong to the ubiquitous family of heat-shock molecular chaperones found in prokaryotes and in eukaryotic organelles.
Chaperonin 60 (GroEL) and chaperonin 10 (GroES) belong to the ubiquitous family of heat-shock molecular chaperones found in prokaryotes and in eukaryotic organelles.
Packaging
Package size based on protein content.
Physical form
Lyophilized powder containing Tris buffer salts, potassium chloride, magnesium chloride, dithiothreitol, and trehalose as stabilizer.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Infrared irradiation in the collision cell of a hybrid tandem quadrupole/time-of-flight mass spectrometer for declustering and cleaning of nanoelectrosprayed protein complex ions
El-Faramawy A, et al.
Analytical Chemistry, 82(23), 9878-9884 (2010)
Observation of a single protein by ultrafast X-ray diffraction
Ekeberg T, et al.
Light: Science & Applications, 13(1), 15-15 (2024)
Chaperonin 60 unfolds its secrets of cellular communication
Maguire M, et al.
Cell Stress & Chaperones, 7(4), 317-329 (2002)
Separating and visualising protein assemblies by means of preparative mass spectrometry and microscopy
Benesch JLP, et al.
Journal of Structural Biology, 172(2), 161-168 (2010)
Surface-exposed chaperonin 60 derived from Propionibacterium freudenreichii MJ2 inhibits adipogenesis by decreasing the expression of C/EBP?/PPAR?
An M and Lim Y-H
Scientific Reports, 13(1), 19251-19251 (2023)
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