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C7438 Sigma

Chaperonin 10 from Escherichia coli

≥90% (SDS-PAGE), recombinant, expressed in E. coli overproducing strain, lyophilized powder

Synonym: GroES

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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   ≥90% (SDS-PAGE)
form   lyophilized powder
storage temp.   2-8°C
Gene Information   human ... HSPE1(3336)

Description

Biochem/physiol Actions

Chaperonin60 (GroEL) and chaperonin10 (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, dithiothreitol and trehalose as stabilizer.

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Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
3
Protocols & Articles
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