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C7688

Sigma-Aldrich

Chaperonin 60 from Escherichia coli

>95% (SDS-PAGE), recombinant, expressed in E. coli overproducing strain, lyophilized powder

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Synonym(s):
Cpn60, GroEL
MDL number:
MFCD00163256
NACRES:
NA.32

biological source

Escherichia coli

Quality Level

200

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.

P10809

storage temp.

2-8°C

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.

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Observation of a single protein by ultrafast X-ray diffraction
Ekeberg T, et al.
Light: Science & Applications, 13(1), 15-15 (2024)
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)
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)
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