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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):
GroEL
MDL number:
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

UniProt accession no.

storage temp.

2-8°C

Gene Information

human ... HSPD1(3329)

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This Item
C7438MSST0007APREST89601
recombinant

expressed in E. coli overproducing strain

recombinant

expressed in E. coli overproducing strain

recombinant

expressed in HEK 293 cells

recombinant

expressed in E. coli

assay

>95% (SDS-PAGE)

assay

≥95.0% (SDS-PAGE)

assay

≥98% (SDS-PAGE)

assay

>80% (SDS-PAGE)

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

buffered aqueous solution

technique(s)

electron microscopy: suitable, mass spectrometry (MS): suitable

technique(s)

-

technique(s)

mass spectrometry (MS): suitable

technique(s)

-

UniProt accession no.

P10809

UniProt accession no.

P61604

UniProt accession no.

P10909

UniProt accession no.

P10809

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

Biochem/physiol Actions

Chaperonin 60 (GroEL) and chaperonin 10 (GroES) belong to the ubiquitous family of heat-shock molecular chaperones found in prokaryotes and in eukaryotic organelles. The chaperonins assist the folding of nascent, organelle-imported or stress-destabilized polypeptides. In vitro, purified GroEL together with purified GroES in the presence of Mg-ATP facilitate refolding and reactivation of denatured proteins, e.g., the photosynthetic enzyme rubisco and the mitochondrial enzyme rhodanese.
The folding activity of a 1:1 molar mixture of GroEL and GroES was tested using urea-denatured rhodanese. At least 2-fold reactivation of rhodanese over the spontaneous reactivation was obtained.

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

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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)
Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports
Meyerson JR, et al.
Scientific Reports, 4(2), 7084-7084 (2014)
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)
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
Abdalla Al Refaii et al.
Molecular microbiology, 71(3), 748-762 (2008-12-05)
In Escherichia coli strains carrying null mutations in either the dnaK or dnaJ genes, the late stages of 30S and 50S ribosomal subunit biogenesis are slowed down in a temperature-dependent manner. At high temperature (44 degrees C), 32S and 45S

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