C7688
Chaperonin 60 from Escherichia coli
>95% (SDS-PAGE), recombinant, expressed in E. coli overproducing strain, lyophilized powder
Sinónimos:
Cpn60, GroEL
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About This Item
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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.
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)
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