Chaperonin 60 from Escherichia coli, , >95% (SDS-PAGE), recombinant, expressed in E. coli overproduc

Chaperonin 60 from Escherichia coli, , >95% (SDS-PAGE), recombinant, expressed in E. coli overproduc

Stock Code: 3589982
Manufacturer Part No: C7688-1MG
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Application

Chaperonin 60 from Escherichia coli has been used: in mass spectroscopyin 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

1 mg in serum bottle

Package size based on protein content.

Physical form

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

Quality Level200
ManufacturerSIGMA-ALDRICH
Technique(s)mass spectrometry (MS): suitable, electron microscopy: suitable
Storage Temp.2-8°C
Formlyophilized powder
Assay>95% (SDS-PAGE)

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