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A propos de cet article
Form:
lyophilized powder
Assay:
≥95.0% (SDS-PAGE)
Biological source:
Escherichia coli
Recombinant:
expressed in E. coli overproducing strain
Service technique
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Laissez-nous vous aiderbiological source
Escherichia coli
Quality Segment
recombinant
expressed in E. coli overproducing strain
assay
≥95.0% (SDS-PAGE)
form
lyophilized powder
technique(s)
activity assay: suitable
UniProt accession no.
storage temp.
2-8°C
Gene Information
human ... HSPE1(3336)
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.
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.
Classe de stockage
11 - Combustible Solids
Que se passe-t-il ?
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
EPI (équipement de protection individuelle)
Eyeshields, Gloves, type N95 (US)
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