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C7688 Sigma

Chaperonin 60 from Escherichia coli

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

Synonym: GroEL

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Properties

Related Categories Application Index, Biochemicals and Reagents, Cell Biology, Cell Signaling Enzymes, Cell Signaling and Neuroscience,
recombinant   expressed in E. coli overproducing strain
assay   >95% (SDS-PAGE)
form   lyophilized powder
storage temp.   2-8°C
Gene Information   human ... HSPD1(3329)

Description

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.

Price and Availability

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis

Protocols & Articles
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