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C7688

Sigma-Aldrich

Chaperonin 60 from Escherichia coli

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

Synonym(s):

Cpn60, GroEL

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About This Item

MDL number:
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

Escherichia coli

Quality Level

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

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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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)
Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports
Meyerson JR, et al.
Scientific Reports, 4(2), 7084-7084 (2014)
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)
Stéphane Erb et al.
Methods in molecular biology (Clifton, N.J.), 2247, 173-191 (2020-12-11)
By maintaining intact multi-protein complexes in the gas-phase, native mass spectrometry provides their molecular weight with very good accuracy compared to other methods (typically native PAGE or SEC-MALS) (Marcoux and Robinson, Structure 21:1541-1550, 2013). Besides, heterogeneous samples, in terms of
Zachary L VanAernum et al.
Nature protocols, 15(3), 1132-1157 (2020-02-02)
It is important to assess the identity and purity of proteins and protein complexes during and after protein purification to ensure that samples are of sufficient quality for further biochemical and structural characterization, as well as for use in consumer

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