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Principaux documents

C7688

Sigma-Aldrich

Chaperonin 60 from Escherichia coli

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

Synonyme(s) :

Cpn60, GroEL

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About This Item

Numéro MDL:
MFCD00163256
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

Escherichia coli

Niveau de qualité

200

Produit recombinant

expressed in E. coli overproducing strain

Essai

>95% (SDS-PAGE)

Forme

lyophilized powder

Technique(s)

electron microscopy: suitable
mass spectrometry (MS): suitable

Adéquation

passes test (Refolding (w/GroES))

Numéro d'accès UniProt

P10809

Température de stockage

2-8°C

Informations sur le gène

human ... HSPD1(3329)

Description générale

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).

Actions biochimiques/physiologiques

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.

Conditionnement

Package size based on protein content.

Forme physique

Lyophilized powder containing Tris buffer salts, potassium chloride, magnesium chloride, dithiothreitol, and trehalose as stabilizer.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

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Certificats d'analyse (COA)

Lot/Batch Number
069M4115V
11190116
027M4094V
11160914
086M4092V

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Consulter la Bibliothèque de documents

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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