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Form:
lyophilized powder
Assay:
>95% (SDS-PAGE)
Biological source:
Escherichia coli
Recombinant:
expressed in E. coli overproducing strain
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Permítanos ayudarlebiological 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)
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.
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.
Packaging
Package size based on protein content.
Physical form
Lyophilized powder containing Tris buffer salts, potassium chloride, magnesium chloride, dithiothreitol, and trehalose as stabilizer.
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports
Meyerson JR, et al.
Scientific Reports, 4(2), 7084-7084 (2014)
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)
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)
Chaperonin 60 unfolds its secrets of cellular communication
Maguire M, et al.
Cell Stress & Chaperones, 7(4), 317-329 (2002)
Observation of a single protein by ultrafast X-ray diffraction
Ekeberg T, et al.
Light: Science & Applications, 13(1), 15-15 (2024)
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